GOLGI TRANSPORT 1B Regulates Protein Export from ...€¦ · 01/11/2016 · Only those proglutelins arriving at the PBII/PSV can 122 be cleaved into the mature 40-kDa acidic and

- 1 -

RESEARCH ARTICLE 1 2

GOLGI TRANSPORT 1B (GOT1B) Regulates Protein Export from 3 Endoplasmic Reticulum in Rice Endosperm Cells 4

5 Yihua Wang,a,1 Feng Liu,c,1 Yulong Ren,b,1 Yunlong Wang,a Xi Liu,a Wuhua Long,a Di 6 Wang,a Jianping Zhu,a Xiaopin Zhu,a Ruonan Jing,a Mingming Wu,a Yuanyuan Hao,a 7 Ling Jiang,a Chunming Wang,a Haiyang Wang,b Yiqun Bao,c and Jianmin Wana,b,2 8

9 a State Key Laboratory for Crop Genetics and Germplasm Enhancement, Jiangsu Plant Gene 10 Engineering Research Center, Nanjing Agricultural University, Nanjing 210095, P.R. China 11 b National Key Facility for Crop Resources and Genetic Improvement, Institute of Crop 12 Science, Chinese Academy of Agricultural Sciences, Beijing 100081, P.R. China c College of 13 Life Sciences, Nanjing Agricultural University, Nanjing 210095, P.R. China 14 1 These authors contributed equally to this work.15 2 Address correspondence to [email protected] or [email protected]. 16

17 Short title: GOT1B Regulates Protein Export from ER 18

19 One sentence summary: GOT1B regulates COPII-mediated protein export from the ER exit 20 sites (ERESs) in developing rice endosperm cells. 21

22 The author responsible for distribution of materials integral to the findings presented in this 23 article in accordance with the policy described in the Instructions for Authors 24 (www.plantcell.org) is: Jianmin Wan ([email protected] or [email protected]). 25

26 ABSTRACT 27 Coat protein complex II (COPII) mediates the first step of anterograde transport of newly 28 synthesized proteins from the endoplasmic reticulum (ER) to other endomembrane 29 compartments in eukaryotes. A group of evolutionarily conserved proteins (Sar1, Sec23, 30 Sec24, Sec13 and Sec31) constitutes the basic COPII coat machinery; however, the details of 31 how the COPII coat assembly is regulated remain unclear. Here, we report a protein transport 32 mutant of rice (Oryza sativa), named glutelin precursor accumulation4 (gpa4), which 33 accumulates 57-kDa glutelin precursors, and forms two types of ER-derived abnormal 34 structures. GPA4 encodes an evolutionarily conserved membrane protein GOT1B (also known 35 as Glup2), homologous to the Saccharomyces cerevisiae GOT1p. The rice GOT1B protein 36 co-localizes with Arabidopsis thaliana Sar1b at Golgi-associated ER exit sites (ERESs) when 37 they are co-expressed in Nicotiana benthamiana. Moreover, GOT1B physically interacts with 38 rice Sec23 and both proteins are present in the same complex(es) with rice Sar1b. The 39 distribution of rice Sar1 in the endomembrane system, its association with rice Sec23c and the 40 ERES organization pattern are significantly altered in the gpa4 mutant. Taken together, our 41 results suggest that GOT1B plays an important role in mediating COPII vesicle formation at 42 ERESs, thus facilitating anterograde transport of secretory proteins in plant cells. 43

44

45

Plant Cell Advance Publication. Published on November 1, 2016, doi:10.1105/tpc.16.00717

©2016 American Society of Plant Biologists. All Rights Reserved

- 2 -

INTRODUCTION 46

COPII-mediated anterograde transport of newly synthesized proteins from the ER to 47

the Golgi apparatus is a vital cellular process in all eukaryotes so far analyzed 48

(D’Arcangelo et al., 2013; Venditti et al., 2014). Numerous studies of yeast and 49

mammalian cells have suggested a model in which five conserved proteins (Sar1, 50

Sec23, Sec24, Sec13 and Sec31) constitute the basic COPII coat machinery that can 51

fulfill the essential function of vesicle formation (Miller and Barlowe, 2010). The 52

assembly of COPII coat occurs on the ER membrane in a step-wise fashion and is 53

initiated by the small GTPase Sar1 (Secretion-associated and ras-superfamily 54

related1), which is activated by the guanine nucleotide exchange factor Sec12, an 55

ER-localized integral membrane protein (Barlowe and Schekman, 1993). The GTP 56

binding of Sar1 causes a conformational change that exposes its N-terminal 57

amphipathic α-helix, which inserts into the ER membrane to initiate vesicle formation. 58

Membrane-bound activated Sar1 then recruits the heterodimeric cargo adaptor 59

platform Sec23/Sec24 through direct interaction with Sec23, forming the pre-budding 60

complexes. Sec24 discriminates cargo molecules for incorporation into COPII 61

vesicles by recognizing specific ER export signals on diverse proteins (Miller et al., 62

2002, 2003). The membrane-bound inner coat complex Sar1-Sec23-Sec24 in turn 63

recruits the Sec13-Sec31 heterotetramer, which forms the cage-like outer layer of the 64

COPII coat to drive ER membrane curvature and release of the vesicles (Aridor et al., 65

1998; Giraudo et al., 2003; Stagg et al., 2006). Downstream events, including 66

hydrolysis of Sar1 in the completed coat, catalyzed by Sec23 and the outer coat, lead 67

to uncoating of the transport vesicles and recycling of the COPII components (Bi et 68

al., 2002; 2007). 69

In addition to the above five COPII proteins that constitute the minimal COPII 70

coat machinery, several accessory factors that are responsible for modulating coat 71

protein recruitment and COPII vesicle formation at ERESs have been identified, 72

including Sec16, Sec12, Sed4, phosphatidylinositol 4-phosphate (PI4P), p125A and 73

ALG-2 (D’Arcangelo et al., 2013). Another potential regulator of COPII vesicle 74

formation in yeast is GOT1p (Golgi transport1), which is not essential for yeast 75

- 3 -

growth, but its deletion significantly affects the transport efficiency between the ER 76

and the Golgi compartments in vitro (Conchon et al., 1999). GOT1p is efficiently 77

packaged into in vitro-generated COPII vesicles; however, efforts to demonstrate 78

physical interaction between GOT1p and COPII coat components have failed 79

(Lorente-Rodríguez et al., 2009). Thus, the exact role of GOT1p in the regulation of 80

COPII vesicle-mediated transport remains elusive. 81

Increasing evidence has shown that COPII vesicles also mediate protein export 82

from the ER in plants (Marti et al., 2010). Many of the major molecular players 83

involved in COPII-mediated ER-Golgi trafficking have homologues in plants and 84

seem to play similar roles as their yeast and mammalian counterparts. For example, 85

transient expression of a dominant negative Sar1 (Arabidopsis thaliana Sar1 H74L) 86

mutant in tobacco and Arabidopsis cultured cells leads to retention of two Golgi 87

membrane proteins and a vacuolar storage protein in the ER, indicating a role for Sar1 88

in protein exit from the ER (Takeuchi et al. 2000). A partial loss-of-function mutation 89

in Arabidopsis Sec24A affects the recruitment of Sec24A to ERESs, resulting in the 90

formation of aberrant tubular clusters of ER and Golgi membranes, suggesting that 91

COPII coat proteins are important for maintaining ER and Golgi membrane integrity 92

in relation to ER protein export in plants (Faso et al., 2009). In addition, analysis of an 93

Arabidopsis Sec16A loss-of-function mutant demonstrated that Sec16A is involved in 94

the dynamic association of COPII coat components on the ER as Sec24 and Sec13 95

were found to cycle on and off the ERES at a much faster rate than in wild-type cells 96

(Takagi et al., 2013). Through live-cell imaging analyses, the Arabidopsis COPII 97

components (Sec13, Sec23, Sec24, and Sec31) have been found in punctate structures 98

which are associated with the ER and move with the Golgi stacks when expressed in 99

highly vacuolated leaf epidermal cells (Stefano et al., 2006; Hanton et al., 2007, 2009; 100

Sieben et al., 2008; Wei and Wang, 2008; Faso et al., 2009; Takagi et al., 2013; 101

Tanaka et al., 2013). These COPII coat protein-labeled punctate structures are 102

commonly indicated as ERESs. Notably, Arabidopsis Sar1 has been found at the 103

ERESs but also over the ER network to a variable degree that may depend on the 104

specific Sar1 isoform (Hanton et al., 2008). In rice (Oryza sativa), simultaneous 105

- 4 -

knockdown of three Sar1 isoforms prevents vacuolar storage proteins from exiting the 106

ER in developing endosperm, suggesting an involvement of COPII vesicles in the 107

early secretory pathway in monocotyledonous plants (Tian et al., 2013). Despite great 108

efforts and advances, our knowledge of the highly regulated process of COPII vesicle 109

formation and its regulation is still limited in plants. 110

Plants generally accumulate large amounts of storage proteins in the seeds, which 111

provide nutrition for seed germination and seedling development. In rice, three types 112

of major storage proteins accumulate in the endosperm including glutelins, prolamins, 113

and α-globulin. The prolamins are retained in the ER lumen after synthesis and are 114

pinched off to form spherical protein bodies I (PBI) (Bechtel and Juliano, 1980; 115

Tanaka et al., 1980; Yamagata and Tanaka, 1986). Glutelins are initially synthesized 116

on the RER as 57-kDa precursors and then transported to the protein storage vacuoles 117

(PSV; also called protein body II [PBII]) through the Golgi apparatus and the dense 118

vesicle (DV)-mediated post-Golgi trafficking pathway (Krishnan et al., 1986; 119

Takemoto et al., 2002; Liu et al., 2013, Ren et al., 2014). The α-globulin is deposited 120

together with glutelins in PBIIs. Only those proglutelins arriving at the PBII/PSV can 121

be cleaved into the mature 40-kDa acidic and 20-kDa basic subunits (Wang et al., 122

2009; Kumamaru et al., 2010). Any defects in the proglutelin trafficking process 123

before reaching the PBII can lead to over-accumulation of the 57-kDa precursor 124

proteins (referred to as the 57H phenotype) in the seeds. Through the studies of 57H 125

mutants, several key factors involved in post-Golgi trafficking of storage proteins 126

have been characterized (Wang et al., 2010; Fukuda et al., 2011, 2013; Liu et al., 2013; 127

Ren et al., 2014). However, how these storage proteins are first exported from the ER 128

remains largely unknown. 129

In this study, we report the functional characterization of the rice gpa4 mutant, 130

which over-accumulates proglutelins in the mature seeds. We show that GPA4 131

encodes an evolutionarily conserved membrane protein GOT1B, homologous to the 132

Saccharomyces cerevisiae GOT1p, a protein known to be involved in vesicular 133

trafficking. When expressed in N. benthamiana, rice GOT1B co-localizes with 134

ArabidopsisSar1b at the ERESs. Yeast two-hybrid hunting identified rice Sec23, a key 135

- 5 -

component of the minimal COPII coat machinery, as an interacting partner of GOT1B. 136

Through a series of biochemical and cellular studies, we concluded that GOT1B is 137

associated with Sec23c and Sar1b in protein complexes in vivo and plays an 138

important role in the proper assembly of the COPII pre-budding complex at the ERES 139

sites, thus affecting anterograde transport of secretory proteins (from ER to Golgi) in 140

plant cells. Further, we present evidence that this mechanism is likely to be conserved 141

across the eukaryotic kingdom. 142

143

144

- 6 -

RESULTS 145

The gpa4-1 Mutant Has a Defect in Vacuolar Protein Trafficking 146

As part of our continuing efforts to dissect the vacuolar sorting mechanisms of seed 147

storage proteins in rice, we isolated two allelic 57H mutants named gpa4-1 (in the 148

indica variety 9311 background) and gpa4-2 (in the japonica variety Kinmaze 149

background). Phenotypic characterization was performed with gpa4-1 (which carries 150

a loss-of-function mutation, see below). In contrast to the transparent wild-type seeds, 151

gpa4-1 seeds appeared floury (Figure 1A). Scanning electron microscopy (SEM) 152

analysis revealed that the gpa4-1 endosperm comprised round and loosely packaged 153

compound starch granules instead of the tightly packaged, crystal-like structures 154

found in the wild type (Figure 1B and 1C). Meanwhile, the 1,000-grain weight was 155

significantly reduced in the gpa4-1 mutant (Figure 1D; Supplemental Table 1). 156

Interestingly, compared with the wild type, gpa4-1 accumulated a higher amount of 157

57-kDa proglutelins, accompanied by a significant reduction of the 40-kDa acidic and 158

20-kDa basic subunits of the mature glutelins as well as the 26-kDa α-globulin. 159

Prolamins of 16-kDa and 13-kDa were both notably decreased as well (Figure 1E and 160

1F). Immunoblots with isoform-specific antibodies revealed increased accumulation 161

of proglutelins for the major glutelin subfamilies (GluA and GluB). Moreover, the 162

precursor of vacuole-localized VPE1 was also greatly elevated in gpa4-1 (Figure 1G; 163

Wang et al., 2009). These results suggest that gpa4-1 is defective in the vacuolar 164

trafficking pathway. 165

In the wild-type seeds, most of the storage proteins started to accumulate from 166

about 6 d after flowering (DAF), but the storage proteins became detectable in gpa4-1 167

only at about 9 DAF (Supplemental Figure 1). The expression levels of the 168

representative genes encoding major storage proteins were all lower in the 12 DAF 169

endosperm of gpa4-1 compared to that of the wild type (Supplemental Figure 2), 170

which is consistent with a lower protein content in the gpa4-1 mature seeds 171

(Supplemental Table 1). These results suggest that the gpa4-1 mutant is also defective 172

in storage protein biosynthesis. 173

- 7 -

174

The gpa4-1 Mutant Shows Defects in Protein Export from the ER in Developing 175

Endosperm Cells 176

- 8 -

As live-cell imaging is not feasible in developing seeds, we compared storage protein 177

trafficking in the subaleurone layers of the gpa4-1 mutant to that of wild type. 178

Semi-thin sections (0.5 μm) of 12 DAF endosperm were subjected to coomassie 179

brilliant blue (CBB) staining. Two types of protein bodies were readily observed in 180

the wild type: dark-stained irregular-shaped PBIIs (contain glutelins and α-globulin) 181

and light-stained round-shaped PBIs (contain prolamins) (Figure 2A). In gpa4-1, the 182

section area of the corresponding dark-stained structures was much smaller than that 183

in 9311, and the mutant had many fewer light-stained spherical structures of normal 184

size (~1-2 µm in the wild type) (Figure 2A and 2B). This observation was further 185

supported by immunofluorescence assays with specific antibodies against prolamins 186

and glutelin acidic subunits (Figure 2G and 2H), suggesting that the gpa4-1 mutation 187

affects the formation of both types of protein bodies. 188

Notably, in addition to the typical PBIs and PBIIs, novel structures with a glutelin 189

core and a prolamin periphery were observed in the developing mutant endosperm 190

(Figure 2C and 2D). Moreover, α-globulin was also detected in the cores (Figure 2E 191

and 2F). As prolamins, glutelins, and α-globulin are all co-translationally transported 192

into their only co-localization site, the RER lumen, we deduced that the abnormal 193

structures might reflect a defect in ER export of storage proteins in rice endosperm. 194

To trace the origin and the formation of these novel structures, transmission 195

electron microscopy (TEM) and immunogold-labeling assays were adopted for 196

subcellular observation. In 12 DAF wild-type endosperm, individual irregular-shaped 197

PBIIs and spherical PBIs were readily observed (Figure 3A), whereas novel structures 198

were found only in gpa4-1 (Figure 3B). These structures were bounded by and 199

attached to the RER network, indicating that they were ER-derived (Figure 3B to 3E). 200

In 9 DAF endosperm, most of these structures had just a small electron-dense core 201

(Figure 3B). Only a few larger ones had protein aggregates in the peripheral regions 202

(Figure 3C). The structures continued to be filled with storage proteins as seed 203

development progressed and they finally grew into the typical structures of 1-2 µm in 204

diameter with an electron-dense core surrounded by large amounts of protein 205

aggregates with low electron density (Figure 3D). At 12 DAF in gpa4-1 endosperm, 206

- 9 -

numerous PBI-like structures with an average diameter of 336.8 nm (± 54.2; n = 20 207

cells) were observed. These structures were bounded by and linked to the RER 208

membranes as well, indicating an ER origin (Figure 3F). 209

- 10 -

Immunogold labeling analysis showed that in the first novel structure, the core 210

contained glutelins whereas its periphery contained prolamins (Figure 3G and 3H), 211

consistent with the immunofluorescence observations (Figure 2D). The second novel 212

- 11 -

structure contained prolamins like PBI (Figure 3I). Together, these observations 213

suggest that the export of all three types of storage proteins from the ER was 214

compromised, resulting in protein retention in the ER lumen and subsequent 215

formation of two types of abnormal structures. Consistent with the above results, 216

centrifugation-based fractionation assay showed that gpa4-1 accumulated more 217

storage proteins and VPE1 precursor in the P13 fraction (enriched in ER membranes) 218

compared with the wild type (Supplemental Figure 3). Moreover, chaperone proteins 219

like Bip1, PDIL1-1, and Hsp90 accumulated and the expression of all the ER 220

stress-related genes analyzed was significantly higher in 12 DAF endosperm of the 221

gpa4-1 mutant. 222

223

GPA4 Encodes a Conserved Membrane Protein Homologous to Yeast Got1p 224

The gpa4-1 mutant was isolated from a 60Co-irradiated population of indica cultivar 225

9311. Genetic analysis revealed that the mutant phenotype was inherited as a single 226

nuclear recessive mutation (Supplemental Table 2). Through map-based cloning, the 227

GPA4 locus was delineated to a 49-kb genomic region (Figure 4A). Sequence analysis 228

revealed that a 108 bp-fragment was deleted in the coding region of Os03g0209400. 229

Only the first 10 amino acids might be correctly translated in gpa4-1. In gpa4-2, a 230

single nucleotide substitution in the 3rd exon of Os03g0209400 caused the 231

replacement of the highly conserved Gly-47 with Asp. Thus, gpa4-1 most likely 232

represents a null mutant of Os03g0209400, while gpa4-2 is likely a partial 233

loss-of-function mutant (Figure 4B). Complementation tests with the entire coding 234

region of Os03g0209400 driven by the Ubiquitin promoter showed complete rescue 235

of the mutant phenotype, including the floury endosperm appearance, storage protein 236

composition, and storage protein deposit pattern in the subaleurone cells of 237

developing endosperm (Figure 4C to 4F). Therefore, we conclude that Os03g0209400 238

is the underlying gene for GPA4. Notably, a recent study reported that Os03g0209400, 239

which encodes GOT1B, is also the underlying gene for the glup2 mutation (Fukuda et 240

al., 2016). For simplicity, we term this gene GOT1B hereafter. 241

- 12 -

242

RT-qPCR analysis revealed that the endogenous GOT1B was expressed in all 243

tissues examined, with relatively higher expression in the endosperm and young 244

- 13 -

panicles (Figure 4G). During endosperm development, the expression of GOT1B was 245

lower at the early stage, peaked at ~15 DAF, and then decreased at 18 DAF, which 246

was correlated with the accumulation of storage proteins (Figure 4H). The rice 247

- 14 -

genome has two other genes (Os10g0337600 and Os02g0602800) homologous to 248

GOT1B (Figure 5A). The Os10g0337600 protein shares 91% sequence similarity with 249

GOT1B. Unexpectedly, instead of compensating for the loss of GOT1B, the 250

expression of Os10g0337600 was greatly down-regulated in gpa4-1 developing 251

endosperm (Figure 4I). 252

GOT1B was predicted to encode a polypeptide of 140 amino acid residues with a 253

calculated molecular mass of 15.8-kDa and four transmembrane domains (TMDs). 254

Phylogenic analysis showed that GOT1B is conserved in eukaryotes and homologous 255

to yeast GOT1p and human GOT1 (hGOT1A and hGOT1B) (Figure 5A and 5B). To 256

analyze the membrane association of GOT1B, cDNA sequence of GOT1B without 257

any tags was subcloned into a binary vector and transiently expressed in N. 258

benthamiana leaf epidermal cells. We used tonoplast-localized rice Tip3-1 as a 259

positive control (Takahashi et al., 2004). After centrifuging cell homogenates at 260

100,000g, both GOT1B and Tip3-1 could be efficiently pelleted, and could not be 261

extracted with sodium chloride or sodium carbonate, but could be solubilized by 262

Triton X-100, confirming their membrane-inserted nature (Figure 5C). To determine 263

the topology of GOT1B, a protease digestion assay was performed using the 264

microsomal pellets prepared from N. benthamiana leaves transiently expressing 265

GFP-GOT1B and GOT1B-GFP. Regardless of the presence or absence of a detergent, 266

the N- and C-terminal GFP tags were completely digested (Figure 5D and 5E), 267

suggesting that both termini of GOT1B are cytoplasmically exposed (Figure 5F). 268

269

GOT1B Is Localized to the Golgi-associated ER Exit Sites To determine the 270

subcellular localization of GOT1B, two fusion constructs (GFP-GOT1B and 271

GOT1B-GFP) under the control of GOT1B native promoter were transformed into the 272

gpa4-2 mutant. Strikingly, only the GFP-GOT1B construct showed rescue of the 273

mutant phenotype (Supplemental Figure 4). From these results, we concluded that the 274

GFP-GOT1B fusion protein is biologically functional in vivo and, thus, should be 275

present at its correct subcellular localization. Then we observed the fluorescence of 276

- 15 -

GFP-GOT1B in the roots of the complemented rice lines. The GFP signal showed a 277

punctate pattern rather than the ER-like tubular structures (Supplemental Figure 5A). 278

When expressed in N. benthamiana leaf epidermal cells, GFP-GOT1B was localized 279

- 16 -

in dynamically moving punctate structures (Supplemental Movie 1), but faint signals 280

in the ER networks were observed in cells with higher expression levels 281

(Supplemental Figure 5B and 5C). To determine the nature of these punctate 282

structures, GFP-GOT1B was co-expressed with several fluorescent markers 283

characteristic for the ER (mRFP-HDEL; for monomeric red fluorescence protein), 284

ERES (AtSar1b-mRFP, Hanton et al., 2008), cis-Golgi (GmMan1-mRFP, Ren et al., 285

2014), trans-Golgi (ST-mRFP, Saint-Jore et al., 2002), and the trans-Golgi networks 286

(mRFP-SYP61, Ren et al., 2014) in N. benthamiana leaf epidermal cells (Figure 6A 287

to 6E). Confocal microscopy analysis revealed strong correlation between 288

GFP-GOT1B and the ERES marker signals (rs = 0.776) (Figure 6B; French et al., 289

2008), and relative weaker correlation with the Golgi markers (rs = 0.532 and 0.524 290

for cis-Golgi and trans-Golgi, respectively) (Figure 6C and 6D). Therefore, 291

GFP-GOT1B is mainly localized at the ERESs and is associated with Golgi stacks. 292

This localization pattern suggests the presence of sorting signals in GOT1B 293

terminal regions. To identify the possible signals, we generated a series of N- and 294

C-terminal deletion and site-directed mutagenesis constructs and examined their 295

localizations in N. benthamiana leaf epidermal cells (Supplemental Figure 6A). GFP 296

fusions of three N-terminal mutant constructs (ΔN2-10, ΔN5-10, and V2A F4A,) 297

were mainly localized to the ER tubule networks except the construct ΔN5-10 298

(Supplemental Figure 6B to 6D). Similarly, GFP fusions of three C-terminal mutant 299

constructs (ΔC125-140, ΔC125-133, and V138G V140G) were fully retained in the 300

ER except ΔC125-133 (Supplemental Figure 6E to 6G). Thus, GOT1B protein 301

possesses sorting signals at both termini. The N-terminal VSF and the C-terminal 302

RGKRVPV residues are essential for its proper localization. 303

Previous studies have demonstrated that Golgi markers and COPII components 304

are sensitive to Brefeldin A (BFA) treatment, which inhibits COPI-mediated 305

retrograde transport and ultimately disassembles the Golgi apparatus. Upon BFA 306

treatment, the distribution of COPII components is significantly changed; Nt-Sar1 is 307

redirected to the ER, while At-Sec13 and At-Sec24 are released into the cytosol 308

- 17 -

(Brandizzi et al., 2002; daSilva et al., 2004; Yang et al, 2005; Hanton et al., 2009). 309

We observed that upon BFA treatment, the fluorescence of GmMan1-mRFP (a 310

cis-Golgi marker) was completely redirected to the ER as expected. Interestingly, the 311

punctate-localized GFP-GOT1B gradually changed to a typical ER pattern within 312

40-45 min (Figure 6F), indicating that GFP-GOT1B is also sensitive to BFA 313

treatment, like COPII components and Golgi markers. This observation lent further 314

support to the notion that GOT1B might play a role in COPII-mediated ER-Golgi 315

protein transport. 316

317

GOT1B Directly Interacts with the COPII Component Sec23 318

COPII-mediated vesicle trafficking is essential for ER-Golgi anterograde protein 319

transport in all eukaryotes so far analyzed (Marti et al., 2010; Miller and Barlowe, 320

2010; D'Arcangelo et al., 2013; Venditti et al., 2014). The phenotypic characterization 321

and the specific subcellular localization suggest a possible relationship between 322

GOT1B and the COPII system. Thus, we performed a yeast two-hybrid (Y2H) study 323

between GOT1B and the five basic components of COPII coat as well as Sec12 and 324

Sec16. We found that GOT1B could interact with Sec23c, but not other COPII 325

components (Figure 7A and Supplemental Figure 7A). As GOT1B encodes an integral 326

membrane protein, we next used a split-ubiquitin based yeast two-hybrid system to 327

verify this interaction (Johnsson and Varshavsky, 1994). In this assay, GOT1B clearly 328

interacted with both Sec23b and Sec23c. The interaction between GOT1B and Sec23a 329

could not be clearly determined because of the self-activation activity of pBT3-N- 330

GOT1B (Supplemental Figure 7B). In the subsequent in vivo bimolecular 331

fluorescence complementation (BiFC) assay in N. benthamiana leaf epidermal cells, 332

GOT1B was found to interact with all three Sec23 isoforms (Figure 7B and 333

Supplemental Figure 7C). 334

As Sec23c had the highest expression level in endosperm (Supplemental Figure 335

7E), we focused on verifying the GOT1B -Sec23c interaction in vivo. We raised 336

specific antibodies against these proteins (Supplemental Figure 8) and used them in 337

- 18 -

co-immunoprecipitation (Co-IP) assay with total extract of developing endosperm 338

(Figure 7C). In wild type, Sec23c protein was immunoprecipitated by the anti- 339

GOT1B antibodies, while in the gpa4-1 mutant, no Sec23c protein was pulled down 340

- 19 -

by the same antibodies (Supplemental Figure 7D). The yeast GOT1p and human 341

GOT1 could also interact with their corresponding Sec23 partner in the Y2H assay. 342

Further, the GOT1 proteins from all three species (human, rice, and yeast) could 343

interact with rice Sec23c (Supplemental Figure 7F). In addition, yeast GOT1 could 344

rescue the mutant phenotypes of gpa4-2 (Supplemental Figure 9). These observations 345

suggest that GOT1B performs a highly conserved role in eukaryotes. 346

To further confirm that GOT1B is involved in the COPII system, we performed 347

Co-IP in the 12 DAF endosperm extract of wild type using anti-Sar1b antibodies. 348

Interestingly, both Sec23c and GOT1B were co-immunoprecipitated (Figure 7D), 349

indicating that these three proteins were present in the same complex(es) in vivo. 350

Notably, the migration of the Sec23c immunoprecipitated by anti- GOT1B and 351

anti-Sar1b antibodies was a little slower than that in the total extracts (Figure 7C and 352

7D), suggesting that Sec23c might be subject to post-translational modification and 353

that the modified Sec23c might be the preferred binding partner for GOT1B and 354

Sar1b. Immunoblot analysis with anti-phosphorylation antibodies showed that the 355

larger band was a phosphorylated form of Sec23c in both IP samples (Figure 7E). 356

This result is consistent with the earlier finding that yeast Sec23p is a phosphoprotein 357

(Lord et al., 2011). 358

359

The Distribution Patterns of Sar1 and ERESs Are Affected in the gpa4-1 Mutant 360

Previous studies have suggested that yeast GOT1p likely participates in the budding 361

step of COPII vesicles (Lorente-Rodríguez et al., 2009). To examine the possible 362

defects of COPII vesicle formation in the gpa4 mutant, we first prepared the 363

microsomal and soluble fractions from endosperm of wild type and gpa4-1. Although 364

the amounts of membrane-associated fractions of endogenous Sec12b, Sar1b, Sar1c, 365

and Sec23c showed no significant difference between the wild type and gpa4-1 366

(Figure 8A and 8B), the distribution of the Sar1 proteins in the endomembrane system 367

was affected; more Sar1b and Sar1c accumulated in the P13 fraction of the gpa4-1 368

mutant compared with the wild type (Figure 8C and Supplemental Table 3), while the 369

- 20 -

distribution of Sec23c showed no obvious change. Previous studies have shown that 370

Sar1 is mainly localized to the ERESs in plant cells (Hanton et al., 2008). The altered 371

distribution of Sar1 proteins in endomembrane system might affect the formation or 372

- 21 -

distribution of ERESs. To directly test this, the ERES maker AtSar1b-GFP was 373

transformed into wild type and the gpa4-2 mutant. Expression of AtSar1b-GFP in rice 374

did not notably affect rice growth and development (Supplemental Figure 10 and 375

Supplemental Table 4). In wild-type root cells, most of the fluorescence of 376

AtSar1b-GFP was dispersed throughout the cytoplasm, with only some sporadic 377

punctate ERES structures. In the gpa4-1 mutant, AtSar1b-GFP showed a typical, more 378

concentrated punctate pattern (Figure 8D). These results suggest that more rice Sar1 379

proteins might be associated with the ERESs, which is consistent with the above 380

fractionation assay result. Further, co-IP assays showed that less Sec23c, but more 381

proglutelin protein was pulled down by anti-Sar1b antibodies in the gpa4-1 mutant 382

than that in the wild type (Figure 8E). These observations together support the notion 383

that GOT1B plays an important role in the formation of COPII vesicles at the ERESs 384

and proper sorting of proglutelins from the ER to the Golgi. 385

386

387

- 22 -

DISCUSSION 388

gpa4 Is Defective in Storage Protein Exit from the ER 389

In this study, we isolated a rice glutelin precursor accumulation mutant named gpa4-1, 390

which is allelic with the recently reported glup2/got1b mutant (Fukuda et al., 2016). 391

Our cytological, immunocytochemical, and biochemical studies showed that export of 392

storage proteins from the ER is significantly repressed, resulting in the retention of 393

these proteins in the ER lumen in gpa4-1 endosperm cells and formation of two novel 394

types of ER-derived abnormal structures. These structures are quite different to those 395

observed in previously reported 57H mutants in which the 57-kDa proglutelins are 396

over-accumulated. The esp2 mutant, resulted from the knockout of PDIL1-1, develops 397

large amounts of ER-derived small PBI-like vesicles containing cross-linked glutelins 398

and prolamins in developing endosperm (Kumamaru et al., 2002). The w379/glup3 399

mutants, both resulted from mutation of VPE1, develop round-shaped PBII (Wang et 400

al., 2009; Kumamaru et al, 2010). While the other three mutants defective in 401

post-Golgi trafficking, gpa1/glup4/osrab5a, gpa2/glup6/osvps9a, and gpa3, all 402

develop large amounts of protein granules and paramural bodies (PMB) in the 403

apoplast (Wang et al., 2010; Fukuda et al., 2011, 2013; Liu et al., 2013; Ren et al., 404

2014). Moreover, PDIL1-1 functions in the ER lumen, and VPE1 plays a role in 405

PSV/PBII, while GPA1, GPA2, and GPA3 form a complex that is present in the 406

trans-Golgi networks and prevacuolar compartments. The localizations of these 407

proteins are quite different from that of GOT1B. Thus, gpa4 represents a novel type 408

of 57H mutant in rice. 409

Notably, the first type of abnormal structure in gpa4-1 was very similar to the 410

MAG bodies observed in the Arabidopsis mag2, mag4, and mag5 mutants (Li et al., 411

2006; Takahashi et al., 2010; Takagi et al., 2013). Each of these MAG bodies contains 412

an electron dense core (composed of 2S albumin) and a peripheral matrix region 413

(composed of 12S globulin). In Arabidopsis, MAG2 interacts with two ER-localized 414

t-SNAREs (target-soluble NSF [N-ethylmaleimide-sensitive fusion protein] 415

attachment protein receptor), Sec20 and Ufe1 (Li et al., 2006). MAG4 is a 416

- 23 -

Golgi-localized tethering factor which has domains homologous to those found in 417

bovine vesicular transport factor p115 (Takahashi et al., 2010). MAG5 is the ortholog 418

of the Saccharomyces cerevisiae and Homo sapiens Sec16, which is localized to the 419

cup-shaped ERESs and regulates COPII turnover (Takagi et al., 2013). These three 420

factors all function in protein export from ER and are related to the COPII vesicles. 421

The high phenotypic similarity between gpa4-1 and the mag mutants suggests that the 422

protein trafficking defect in gpa4-1 is likely associated with the COPII system. 423

Consistent with this notion, simultaneous knockdown of rice Sar1a/b/c results in 424

almost the same phenotype as observed in the gpa4-1 mutant (Tian et al., 2013). In 425

addition, the blocking of large amounts of storage proteins in the ER lumen may 426

affect the normal function of ER, which probably in turn affects the biogenesis of 427

PBIs, resulting in the formation of the second type of small PBI-like structures 428

(immature PBIs) in the gpa4-1 mutant. 429

430

GOT1B Encodes a Golgi-associated ERES-localized Membrane Protein 431

Cloning and characterization of GPA4 revealed that it encodes GOT1B, which is 432

homologous to the yeast and human GOT1 with four TMDs. Both termini face to the 433

cytosol. The structure and topology of GOT1B is highly conserved relative to the 434

yeast GOT1p (Conchon et al., 1999; Lorente-Rodríguez et al., 2009). However, 435

earlier studies have reported conflicting subcellular localization of yeast GOT1p. 436

Conchon et al. (1999) demonstrated that both GOT1p and human GOT1A (hGOT1A) 437

show a punctate pattern overlapping with the cis-Golgi apparatus. Further subcellular 438

fractionation assays confirmed their cis-Golgi localization. Notably, a faint ER-like 439

staining was also observed for hGOT1A, in addition to the punctate pattern. However, 440

Huh et al. (2003) showed that a C-terminally GFP-tagged GOT1p (GOT1p-GFP) is 441

localized to the ER. In a recent study, it was proposed that GOT1p may cycle between 442

the ER and the Golgi compartments (Lorente-Rodríguez et al., 2009). In this study, 443

we showed that the biologically functional GFP-GOT1B fusion protein indeed 444

exhibited a typical punctate localization pattern in the root cells of the complemented 445

- 24 -

transgenic lines. This fusion protein is predominantly localized at the 446

AtSar1b-mRFP-labeled ERESs with faint signals in the ER when transiently 447

expressed in N. benthamiana leaf epidermal cells (Figure 6 and Supplemental Figure 448

5), and still shows relatively high correspondence (rs > 0.5) with Golgi markers. Thus, 449

our result seems to support the ER-Golgi secretory unit model, in which ERESs are 450

associated with mobile Golgi stacks (daSilva et al., 2004). The interaction between 451

GOT1B and Sec23c and their coexistence with Sar1b further support this localization 452

pattern. Based on these results, we conclude that GOT1B is predominantly localized 453

at the Golgi-associated ERESs, and likely plays a role in COPII-mediated anterograde 454

protein transport from the ER to the Golgi. 455

456

GOT1B likely Participates in Regulating the Assembly of COPII Pre-budding 457

Complexes in vivo 458

Yeast Got1p was initially identified in a synthetic lethal screen with sft2Δ and was 459

proposed to be involved in the fusion of uncoated COPII vesicles to the Golgi 460

(Conchon et al., 1999). However, later studies found the trafficking defects of the 461

original got1p strain could be due to additional mutation(s) in the mutant background 462

(Lorente-Rodríguez et al., 2009). GOT1 was also isolated as a strong suppressor of 463

thermosensitive allele of yip1-2 (Lorente-Rodríguez et al., 2009). Yip1p is an 464

evolutionarily conserved, essential 35.5-kDa integral Golgi membrane protein 465

functioning in COPII budding in the membrane scission stage (Matern et al., 2000; 466

Heidtman et al., 2005). Meanwhile, multicopy GOT1 is a suppressor of genes 467

involved in vesicle formation rather than those participating in vesicle tethering, 468

fusing, and retrograde transport. Moreover, in vitro assays showed that GOT1p can be 469

packaged into COPII vesicles (Lorente-Rodríguez et al., 2009). These results together 470

suggest that GOT1p likely participates in the assembly or budding stage of COPII 471

vesicles. 472

In this study, using a combination of Y2H, BiFC and co-IP assays, we showed 473

that GOT1B specifically interacts with rice Sec23 isoforms (Figure 7A to 7C). We 474

- 25 -

also showed that the yeast, human counterparts of GOT1B can physically interact 475

with their corresponding Sec23 proteins (Supplemental Figure 7F). Our co-IP assays 476

further showed that Sar1b, GOT1B, and Sec23c are present in the same complex(es) 477

in vivo (Figure 7D). These observations together suggest that GOT1B likely functions 478

before the budding of COPII vesicles, as Sar1 hydrolyzes its bound GTP and 479

dissociates from the membrane once the COPII vesicle is released. The altered 480

fractionation pattern of the pre-budding complex components (Sar1b and Sar1c) and 481

the lower amount of modified Sec23c protein immunoprecipitated by anti-Sar1b 482

antibodies in the gpa4 mutant (Figure 8A to 8C and 8E) also support the notion that 483

GOT1B functions in COPII vesicle formation, probably participating in the regulation 484

of the formation or stability control of the pre-budding complex of the COPII coat. In 485

further support of this, we observed distinct patterns of ERESs in the wild type and 486

gpa4 (Figure 8D). The dispersed distribution of ERESs in wild type might be due to 487

the rapid recycling of COPII vesicles between the ER and the Golgi apparatus, while 488

in the mutant, the recycling of COPII vesicles is likely disrupted, causing blockage of 489

COPII components as well as proglutelins (cargos) in the ERESs. 490

Based on the above results, we propose a speculative model for GOT1B in COPII 491

coat assembly. As GOT1B itself is localized to the ERESs, it may work together with 492

Sar1 to facilitate the recruitment of the Sec23/Sec24 heterodimer to form the 493

pre-budding complexes in which cargos have been preloaded. Then the Sec13/Sec31 494

heterotetramer is recruited to form the outer coat of the COPII vesicles before vesicle 495

budding and subsequent fusion with the cis-Golgi apparatus (Figure 8F). In the 496

gpa4-1 mutant, the absence of GOT1B protein may reduce the binding strength or 497

efficiency between Sar1 and the Sec23/Sec24 heterodimer, resulting in the instability 498

of the pre-budding complexes and defective COPII vesicle formation. The assembly 499

deficiency of COPII vesicles may in turn affect the recycling of COPII coat components, 500

leading to blockage of COPII coat components in the ERESs. 501

The COPII system is highly conserved in eukaryotes for anterograde protein 502

transport, and defects in this system cause many types of diseases in human (Miller et 503

al., 2013). Our results reveal the in vivo function of GOT1B in regulating 504

- 26 -

COPII-mediated secretory protein trafficking and provide evidence that GOT1B 505

might function in regulating the formation or stability of the COPII pre-budding 506

complexes. However, earlier studies have shown that COPII vesicle budding can be 507

reconstituted in vitro in the absence of Got1p (Matsuoka et al., 1998); thus, it is 508

possible that GOT1B may function as a modulator to facilitate COPII coat formation 509

rather than being a stoichiometric subunit of the COPII coat. Notably, a recent study 510

reported that prolamin mRNA sorting is defective in the glup2/got1B mutant and that 511

GOT1B is required for localization of prolamin and α-globulin RNAs to the protein 512

body-ER and for efficient export of proglutelin and α-globulin proteins from the ER 513

to the Golgi apparatus (Fukuda et al., 2016). The identification and functional studies 514

of GOT1B now pave the way for further investigating the detailed biophysical 515

mechanisms of COPII vesicle formation and its regulation in eukaryotes. 516

517

518

- 27 -

METHODS 519

Plant Materials and Growth Conditions 520

Two allelic gpa4 mutants, named gpa4-1 and gpa4-2, were isolated in this study. 521

gpa4-1 was isolated from a 60Co-irradiated M2 population of the indica rice (Oryza 522

sativa) cultivar 9311. gpa4-2 was isolated from an MNU-treated M2 population of the 523

japonica rice cultivar Kinmaze. Both mutants were backcrossed at least three times 524

with their corresponding wild type to remove other mutation sites. All plants were 525

grown in paddy fields during normal growing seasons or in a greenhouse. 526

Protein Extraction from Rice Seeds and Immunoblot Analysis 527

Total protein extraction and immunoblot assays were performed as described 528

previously (Wang et al., 2010; Liu et al., 2013; Ren et al., 2014). 529

Map-based Cloning 530

To map the GPA4 locus, an F2 population derived from the cross between the gpa4-1 531

mutant (indica) and a japonica variety Nipponbare was developed. In this population, 532

total proteins were extracted form one half of an individual F2 seed and resolved by 533

SDS-PAGE gel to monitor the accumulation of proglutelins. Meanwhile, the other 534

half of the identified mutant seed with embryo was grown for DNA isolation. In total, 535

1155 recessive individuals were used for fine mapping of GPA4. The primers used in 536

fine mapping are listed in Supplemental Table 5. 537

Microscopic Observation 538

The immunofluorescence analyses, scanning electron microscopy, transmission 539

electron microscopy, and subsequent immunogold labeling experiments were 540

performed as described previously (Wang et al., 2010; Liu et al., 2013; Ren et al., 541

2014). 542

Phylogenetic Analysis 543

Homologs of rice GOT1B were identified using the BLASTP search program of the 544

- 28 -

National Center for Biotechnology Information (http://www.ncbi.nlm.nih.gov). The 545

phylogenetic tree was constructed using MEGA 5.0 (http://www.megasoftware.net), 546

based on the neighbor-joining method with the following parameters: p-distance 547

model, pairwise deletion and bootstrap (1000 replicates; random seed). 548

Antibodies 549

Synthetic peptides of GOT1B (Os03g0209400, TSFLDRYRGKRVPV), GluA1 550

(Os01g0762500, RRGSPRECRFDR), GluB1 (Os02g0249800, SQSQKFRDEHQK), 551

α-globulin (Os05g0499100, CEGSSSEQGYYGEGS), 10-kDa prolamin 552

(Os03g0766100, Pro10, TLAMGTMDPCRQ), 13-kDa prolamin-a (Os07g0206400, 553

Pro13a, RFDPLSQSYRQY), 13-kDa prolamin-b (Os07g0219300, Pro13b, 554

QLRNNQVLQQLR), 16-kDa prolamin (Os06g0507200, Pro16, EQSRRLQLSSCQ), 555

PDIL1-1 (Os11g0199200, CKAESAPAEPLKDEL), Sar1c (Os06g0225000, 556

PTQHPTSEELSIGRC), and Tip3-1 (Os10g0492600, RPGRRFTVGRSEDAC) were 557

synthesized. Recombinant proteins of Sec12b (Os11g0610700, 1-227AA), Sar1b 558

(Os01g0338000, 1-193AA), Sec23c (Os11g0433500, 1-366AA), Bip1 559

(Os02g0115900, 461-665AA), and VPE1 (Os04g0537900, 24-497AA) were 560

bacterially produced in pET-32a and purified. The synthetic peptides or recombinant 561

proteins were injected to rabbits or mice to generate corresponding polyclonal 562

antibodies or monoclonal antibody at Yingji Biotech Co. LTD 563

(http://www.immunogen.com.cn/). The anti-EF-1α antibodies were purchased from 564

Agrisera (As111633, lot 1209). The Anti-Hsp90 antibodies were purchased from BGI 565

(AbM51099-31-PU, lot 2012022301). Antibodies of phosphorylation were purchased 566

from Abcam (ab17464, lot GR276547-1). The anti-GFP antibodies were purchased 567

from Roche (11814460001, lot 14717400). All the antibodies were used in 1:1000 568

dilutions in immunoblot analyses. 569

570

Yeast Two-Hybrid Assay 571

The cDNA of GOT1B was cloned into pGBT9, while the coding regions of the COPII 572

- 29 -

components were cloned into pGADT7 by Clontech In-Fusion HD® Cloning Kit 573

(639650). Various combinations of plasmids were co-transformed into the yeast strain 574

AH109 for interaction study, following the manufacturer’s instructions. 575

The split ubiquitin based DUAL hunter starter kit was purchased from 576

Dualsystems Biotech (P01601-P01609). The cDNA of GOT1B was cloned into 577

pBT3-N, while the coding regions of the rice Sec23 isoforms were cloned into 578

pPR3-N. Corresponding plasmids were co-transformed into the yeast strain NMY51 579

following the manufacturer’s instructions. Primers used in this assay are listed in 580

Supplemental Table 5. 581

RT-qPCR Analysis 582

Total RNA was isolated using the RNA prep pure plant kit (TIANGEN, Beijing, 583

China). The first-strand cDNA was synthesized using Oligo (dT)18 as the primer, and 584

PrimeScript Reverse Transcriptase (TaKaRa, Dalian, China) for reverse transcription. 585

Rice Ubiquitin (UBQ) was used as an internal control. Real-time PCR analysis was 586

performed using an ABI 7500 real-time PCR system with the SYBR Green Mix 587

(Bio-Rad, Hercules, CA, USA) and three biological repeats (three plants grown 588

separately). Primers used in this assay are listed in Supplemental Table 5. 589

Subcellular Fractionation 590

The wild-type and the gpa4-1 developing endosperm were used for fractionation as 591

described previously with some modifications (Tamura et al., 2005). At 12 DAF, 592

developing endosperm was homogenized in a mortar on ice in a triple volume of 593

buffer A (100 mM HEPES-KOH, pH 7.5, 0.3 M Sucrose, 5 mM EGTA, 5 mM MgCl2, 594

and protease inhibitor [complete cocktail tablets; Roche]). The homogenate was 595

filtered through cheesecloth and centrifuged at 50g for 20 min to remove starch. The 596

supernatant was further centrifuged at 2000g for 20 min at 4oC to obtain the 597

supernatant (S2) and pellet fractions (P2). Then the S2 fraction was further 598

centrifuged at 1,3000g and 100,000g to obtain the P13, P100, and S100 fractions for 599

immunoblot analysis. 600

- 30 -

To perform subcellular fractionation, N. benthamiana leaves (~3 g) transiently 601

expressing GOT1B were homogenized in 10 mL of the above buffer. The homogenate 602

was filtered and centrifuged at 2000g for 20 min at 4oC to remove the cell debris. The 603

supernatant was ultracentrifuged at 100,000g for 1 h at 4oC to obtain the microsomal 604

pellet. Then the microsomal pellets were resuspended in 150 µL of each solution of 605

buffer A, high salt-buffer (1 M NaCl, 100 mM HEPES-KOH, pH 7.5, 0.3 M sucrose, 606

5 mM EGTA, and 5mM EDTA), alkaline buffer (0.1 M Na2CO3, pH 11, 0.3 M 607

sucrose, 5 mM EGTA, and 5mM EDTA), and Triton X-100 buffer (1% [v/v] Triton 608

X-100, 100 mM HEPES-KOH, pH 7.5, 0.3 M sucrose, 5 mM EGTA, and 5mM 609

EDTA). After incubation for 20 min on ice, these supernatants were ultracentrifuged 610

at 100,000g for 1 h at 4oC to obtain the supernatant and pellet fractions for 611

immunoblot analysis. 612

To determine the membrane topology of GOT1B, the microsomal pellets were 613

resuspended in buffer A in the presence or absence of 1% (v/v) Triton X-100 and then 614

were incubated with 10 ng/µL proteinase K (Roche) for 15 min on ice. The reactions 615

were terminated by adding equal volume of 2 × SDS-PAGE loading buffer and then 616

were subjected to immunoblot analysis. 617

Transient Expression Analysis in N. benthamiana 618

For transient expression analysis in N. benthamiana leaf epidermal cells, the coding 619

region of GOT1B was amplified and inserted into the binary vector 620

pCAMBIA1305GFP to produce the GFP-GOT1B (BglII site) or GOT1B-GFP 621

(XbaI-BamHI sites) fusion constructs. For BiFC assay, the coding sequences of 622

GOT1B and rice Sec23 isoforms were cloned into pYN1 and pYC1 vectors (kind gift 623

of Dr. John A. Lindbo, OARDC, The Ohio State University, Wooster, OH, USA) to 624

produce YN-GOT1B and YC-Sec23a/b/c, respectively. All the constructs were 625

introduced into the Agrobacterium strain EHA105 and then used to infiltrate N. 626

benthamiana leaves, as described previously (Waadt et al., 2008). Confocal imaging 627

was performed using a Zeiss LSM780 laser scanning confocal microscope. Image 628

analysis was performed using Image J software. 629

- 31 -

Co-immunoprecipitation 630

Developing endosperm was homogenized and solubilized in triple volumes of NB1 631

buffer (50 mM Tris-MES, pH 7.5, 0.5 M sucrose, 1 mM MgCl2, 10 mM EDTA, 5 632

mM DTT, 0.2% (v/v) Nonidet P-40, 10 mM NaF, and complete proteinase inhibitors) 633

and then centrifuged at 20,000g for 20 min at 4oC to remove the cell debris and fatty 634

acids. 1 mL of total extract was pre-incubated with 20 µL of Protein-A-agarose beads 635

(Roche, 11134515001). The extracts were incubated with the corresponding 636

antibodies or the same amount of IgG from rabbit serum (Sigma, I5006) for 3 h and 637

then incubated with Protein-A-agarose beads for additional 2 h. After extensive 638

washing, the agarose beads were centrifuged at 500g and boiled in the 5 × 639

SDS-PAGE sample buffer for subsequent immunoblot analysis. For phosphorylation 640

assay, the transblotted PVDF membrane was cut into two halves along the marker 641

lane. Then the left half was incubated with anti-phosphorylation antibodies, while the 642

right half was incubated with anti-OsSec23c antibodies. 643

Accession Numbers 644

Sequence data from this article can be found in the GenBank/EMBL databases under 645

the following accession numbers: GOT1B (Os03g0209400), Sec12b (Os11g0610700), 646

Sar1a (Os01g0254000), Sar1b (Os01g0338000), Sar1c (Os06g0225000), Sar1d 647

(Os12g0560300), Sec23a (Os01g0321700), Sec23b (Os08g0474700), Sec23c 648

(Os11g0433500), Sec24 (Os11g0482100), Sec13a (Os02g0135800), Sec13b 649

(Os03g0831800), Sec13c (Os07g0246300), Sec31 (Os07g0657200). The accession 650

numbers for proteins in the phylogentice analysis are SbGOT1, XP_003617250.1; 651

ZmGOT1-2, NP_001150565.1; ZmGOT1-1, NP_001141744.1; HvGOT1, 652

BAJ99406.1; GOT1B, NP_001049334.1; Os10g0337600, BAH00874.1; SiGOT1, 653

XP_004985256.1; AtGOT1, NP_186968.2; At5g01430, NP_190511.1; BrGOT1, 654

XP_009130652.1; GsGOT1, KHN46642.1; MtGOT1, XP_003617250.1; At1g05785, 655

NP_683279.1; Os02g0602800, NP_001047360.1; GOT1p, NP_014020.1; hGOT1B, 656

NP_057156; DmGOT1A, NP_727945.1; DmGOT1B, NP_001014746.1; DrGOT1A, 657

XP_001336385.1; MmGOT1, NP_080956.1; hGOT1A, NP_940849; PtGOT1, 658

- 32 -

XP_009439600.1; OaGOT1, XP_012042315.1; SsGOT1, XP_003130159.1. 659

660

Supplemental Data 661

The following materials are available in the online version of this article. 662

Supplemental Figure 1. Time-Course Analysis of Storage Proteins during 663

Endosperm Development of the Wild-Type 9311 and the gpa4-1 Mutant. 664

Supplemental Figure 2. RT-qPCR Assay of the Expression of Representative 665

Genes Coding for Storage Proteins in 12 DAF Endosperm. 666

Supplemental Figure 3. Immunoblot Analyses Showing Defective Export of 667

Storage Proteins from the ER in gpa4-1. 668

Supplemental Figure 4. Rescue of the gpa4-2 Mutant Phenotype by the 669

GFP-GOT1B Fusion Construct. 670

Supplemental Figure 5. Localization Pattern of GFP-GOT1B Fusion Protein. 671

Supplemental Figure 6. Both the N- and C-termini Are Essential for the Proper 672

Localization of GOT1B Protein. 673

Supplemental Figure 7. Interaction between GOT1B and Sec23. 674

Supplemental Figure 8. Immunoblot Analyses Showing the Specificity of 675

Antibodies. 676

Supplemental Figure 9. Rescue of the gpa4-2 Mutant Phenotypes by Yeast 677

GOT1. 678

Supplemental Figure 10. The Seeds of Transgenic Rice Lines Expressing 679

AtSar1b-GFP Show No Difference from Their Corresponding Recipient Plants. 680

Supplemental Table 1. Comparison of Important Agronomic Traits between Wild 681

Type and gpa4 Mutants. 682

Supplemental Table 2. Segregation of Mutant Phenotype in Reciprocal Crosses 683

between the Wild Type and the gpa4-1 Mutant. 684

Supplemental Table 3. The Distribution of COPII-Related Proteins in the 685

Endomembrane System. 686

Supplemental Table 4. Comparison of Important Agronomic Traits between 687

- 33 -

AtSar1b-GFP Transgenic Lines and Their Corresponding Recipient Plants. 688

Supplemental Table 5. Primers Used in This Study. 689

690

Supplemental Data set 1. Text file of the alignment used for the phylogenetic 691

analysis in Figure 5A. 692

Supplemental Movie 1. Time-Lapse Microscopy of Tobacco Leaf Epidermal Cells 693

Expressing GFP-GOT1B. 694

695

ACKNOWLEDGEMENTS 696

This work was supported by grants from the National Natural Science Foundation of 697

China (Grants 31330054, 31371598, and 31401360), a project from the ministry of 698

Agriculture of China for Transgenic Research (Grants 2014ZX0800925B, 699

2014ZX08009-003, and 2014ZX08001006), and the Fundamental Research Funds for 700

Excellent Young Scientists of ICS-CAAS (Grant to YR, 2014JB04-009; 701

1610092015003-08). This work was also supported by Key Laboratory of Biology, 702

Genetics and Breeding of Japonica Rice in Mid-lower Yangtze River, Ministry of 703

Agriculture, P. R. China, and Jiangsu Collaborative Innovation Center for Modern 704

Crop Production. We thank Dr. Jinxing Lin and Dr. Xiaojuan Li (Beijing Forestry 705

University), Dr. Xiaohua Wang and Dr. Jingjing Xing (Institute of Botany, the 706

Chinese Academy of Sciences) for kind help with fluorescence observation. We also 707

thank Dr. Shuhua Yang (China Agricultural University) for kindly providing the split 708

ubiquitin based Y2H hybrid vectors.709

710

AUTHOR CONTRIBUTIONS 711

J.W., H.W., Y.B. and Y.H.W. designed the research. X.L., W.L., and D.W. screened the712

mutant materials. F.L., Y.R, and Y.L.W. performed immunofluorescence and 713

immunogold labeling experiments. Y.H.W., F.L. and J.Z. performed the Co-IP assays. 714

X.Z. and R.J. performed vector constructions. Y.H.W., F.L., M.W., L.J., and C.W.715

- 34 -

performed other experiments. J.W., H.W., Y.H.W. and F.L. analyzed the data and716

wrote the article. Y.H.W., F.L. and Y.R. contributed equally to this work. 717

718

Figure Legends 719

Figure 1. Phenotypic Analysis of the gpa4-1 Mutant. 720

(A) Transverse sections of representative wild-type (Indica variety 9311) and gpa4-1721

mutant dry seeds. Bar = 1 mm. 722

(B) and (C) Scanning electron microscopy (SEM) images of transverse sections of723

wild-type (B) and gpa4-1 mutant (C) seeds. Bars = 10 μm. 724

(D) 1,000-grain weight of wild type and gpa4-1. Values are mean ± SD. **P < 0.01 (n725

= 3, Student’s t test). 726

(E) SDS-PAGE profiles of total proteins of dry seeds from the wild type and the727

gpa4-1 mutant. pGlu, 57-kDa proglutelins; αGlu, 40-kDa glutelin acidic subunits; 728

α-Glb, 26-kDa α-globulin; βGlu, 20-kDa glutelin basic subunits; Pro, prolamins. 729

(F) Immunoblot analysis of seed storage proteins using anti-glutelin and730

anti-α-globulin antibodies. Blue triangles indicate the 57-kDa proglutelins. Hollow 731

arrows denote the glutelin acidic subunits (black) and basic subunits (red) in (F) and 732

(G). 733

(G) Immunoblot analysis of the major glutelin subfamily proteins (i.e. GluA and734

GluB) and VPE1. Arrows indicate different forms of VPE1. pV, VPE1 precursor; iV, 735

intermediate VPE1; mV, mature VPE1. EF-1α was used as a loading control in (F) 736

and (G). 737

738

Figure 2. Light and Immunofluorescence Microscopy of Protein Bodies in the 739

Subaleurone Cells of the Wild Type and the gpa4-1 Mutant. 740

(A) and (B) Sections of 12 DAF endosperm of wild type (A) and gpa4-1 (B) stained741

with coomassie brilliant blue (CBB). Red and white triangles indicate the dark-stained 742

glutelin-containing structures (PBIIs in wild type) and the light-stained 743

prolamin-containing structures (PBIs in wild type), respectively. SG, starch grains. 744

Bars = 10 μm. 745

- 35 -

(C) to (F) Immunofluorescence microscopy images of storage proteins in wild-type 746

(C and E) and gpa4-1 (D and F) seeds. Secondary antibodies conjugated with Alexa 747

fluor 488 (green) and Alexa fluor 555 (red) were used to trace the antigens recognized 748

by the anti-glutelin and anti-prolamin antibodies, respectively, in (C) and (D). Similar 749

reactions were performed with anti-α-globulin antibodies instead of anti-glutelin 750

antibodies in (E) and (F). White arrows in (D) and (F) indicate the novel structures. 751

The insets in (D) and (F) are the enlarged images of the corresponding boxed areas. 752

Bars = 10 μm. 753

(G) and (H) Measurement of the diameters of PBIIs (G) and the number of PBIs with754

normal size per 100 µm2 (H). Values are mean ± SD. **P < 0.01 (n = 84 for wild type 755

and 56 for gpa4-1 in [G]; n = 4 [total 470 PBIs] for wild type and 5 [total 334 PBIs] 756

for gpa4-1 in [H]. Student’s t test). 757

758

Figure 3. Ultrastructure of Subaleurone Cells of Developing Endosperm of the 759

Wild Type and gpa4-1 Mutant. 760

(A) Two types of protein bodies were observed in wild-type endosperm. Bar = 2 μm.761

(B) The first type of novel structure was observed from 9 DAF in endosperm of the762

gpa4-1 mutant. Stars represent this type of novel structure in (B) to (E). Bar = 1 μm. 763

(C) Enlarged image of the boxed area in (B). Triangles indicate protein aggregates in764

the periphery of the first type of novel structure. Bar = 200 nm. 765

(D) The first type of novel structure in 12 DAF endosperm cells. Bar = 1 μm.766

(E) The first type of novel structure is directly linked with the ER. Bar = 1 μm.767

(F) The second type of novel structure (red triangles), in 12 DAF endosperm cells.768

Bar = 500 nm. 769

(G) to (I) Immunoelectron microscopy localization of glutelins and prolamins in770

subaleurone cells of developing wild-type endosperm (G) and the gpa4-1 mutant ([H] 771

and [I]). (G) Glutelins and prolamins are accumulated separately in the wild type. (H) 772

The first type of novel structure contains a glutelin (6 nm gold, blue arrows) core and 773

a prolamin (15 nm gold, red arrows) periphery. (I) The second type of novel structure 774

contains prolamins (15 nm gold, red arrows). Bars = 500 nm in (G) and (H); 200 nm 775

- 36 -

in (I). 776

777

Figure 4. Map-based Cloning and Expression Analysis of GOT1B. 778

(A) Fine mapping of the GPA4 locus. The molecular markers and the number of779

recombinants are shown. 780

(B) Gene structure and the mutation site in Os03g0209400. Os03g0209400 comprises781

6 exons (closed boxes) and 5 introns (lines). ATG and TGA represent the start and 782

stop codon, respectively. A 108-bp fragment deletion and a nucleotide substitution 783

occurred in the coding region of Os03g0209400 in gpa4-1 and gpa4-2, respectively. 784

(C) to (F) The Os03g0209400 cDNA under the control of Ubiquitin promoter rescues785

the grain appearance (C), the storage protein composition pattern (D), and the storage 786

protein trafficking defects ([E] and [F]) of the gpa4-2 mutant. L1 to L4 denote the 787

grains from four independent T1 transgenic lines. Stars represent the abnormal 788

structure with a glutelin core and a prolamin periphery in (E). Bars = 2 μm in (E) and 789

(F). 790

(G) RT-qPCR assay showing that GOT1B is expressed in various wild-type tissues791

examined, with the highest expression in panicles before heading. S, shoot; E, 792

endosperm; L, leaf; R, root; SL, seedling; LS, leaf sheath; P, panicle before heading. 793

EF-1α was used as an internal control in (G) to (I). For each RNA sample, three 794

technical replicates were performed. Values are mean ± SD. 795

(H) RT-qPCR assay showing that GOT1B is expressed throughout endosperm796

development. The expression of GOT1B in gpa4-1 was much lower compared with 797

that in the wild type. For each RNA sample, three technical replicates were performed. 798

Values are mean ± SD. 799

(I) The expression of GOT1B and its homologs in 12 DAF endosperm cells. For each800

RNA sample, three technical replicates were performed. Values are mean ± SD. 801

802

Figure 5. Phylogenic Tree and Topology Analysis of the GOT1B Protein. 803

(A) Phylogenic tree of the GOT1B protein and its homologs in eukaryotes. The804

phylogenic tree was constructed using MEGA version 5.0. Sb, Sorghum biocolor; Zm, 805

- 37 -

Zea mays; Hv, Hordeum vulgare; Os, Oryza sativa; Si, Setaria italica; At, Arabidopsis 806

thaliana; Br, Brassica rapa; Gs, Glycine soja; Mt, Medicago truncatula; H, human 807

sapiens; Dm, Drosophila melanogaster; Mm, Mus musculus; Pt, Pan troglodytes; Oa, 808

Ovis aries; Ss, Sus scrofa. The sequence alignment used for this analysis is available 809

as Supplemental Data set 1. 810

(B) Sequence alignment of GOT1B and its homologous proteins. Red lines indicate811

the four transmembrane domains predicted by TMHMM Server v. 2.0 812

(http://www.cbs.dtu.dk/services /TMHMM). 813

(C) Membrane association of GOT1B protein expressed in N. benthamiana. GOT1B814

was expressed in tobacco leaf epidermal cells. 100,000g membrane pellets were 815

prepared and extracted with indicated buffers before centrifugation and analysis of the 816

pellets (P100) and supernatants (S100) by immunoblot. Triangle indicates the GPA4 817

protein band. Arrow indicates the Tip3-1 protein band. 818

(D) and (E) Protease protection assays. Membrane preparations containing the819

GOT1B protein tagged at either the C- (D) or N-terminus (E), as indicated, were 820

digested with proteinase K in the presence or absence of detergent, and then analyzed 821

by immunoblot. 822

(F) The proposed topology of GOT1B protein. TMD, transmembrane domain.823

824

Figure 6. Subcellular Localization of GOT1B in the Leaf Epidermal Cells of N. 825

benthamiana. 826

(A) to (E) Confocal microscopy images showing that GFP-GOT1B generates punctate827

signals in the cytosol and its distribution is obviously distinct from that of marker 828

proteins characteristic for the ER (mRFP-HDEL [A]) and the trans-Golgi networks 829

(mRFP-SYP61 [E]), but is partially localized with the marker proteins characteristic 830

for ER exit sites (AtSar1b-mRFP [B]), cis-Golgi (GmMan1-mRFP [C]), and 831

trans-Golgi apparatus (ST-mRFP [D]). PSC coefficients (rs) between GFP-GOT1B 832

and each marker are shown in the right panel. Values are mean ± SD. n = 3. Bars = 10 833

μm in (A) to (E). 834

(F) BFA treatment (100 μg/mL) of leaf epidermal cells coexpressing GFP-GOT1B835

- 38 -

and GmMan1-mRFP. The localization pattern of GFP-GOT1B and GmMan1-mRFP 836

gradually changed from punctate patterns (0-5 min) to typical ER patterns (40-45 837

min). Bars = 10 μm. 838

839

Figure 7. GOT1B Physically Interacts with Sec23 Proteins. 840

(A) Y2H assay showing that GOT1B interacts with Sec23c. The bait plasmid841

(pGBKT7-Lam or pGBKT7-53) was co-transformed into the AH109 yeast strain with 842

the prey plasmid (pGADT7-T) to serve as negative and positive controls, respectively. 843

(B) BiFC assay showing that GOT1B can interact with three Sec23 isoforms in leaf844

epidermal cells of N. benthamiana. The Golgi-localized membrane proteins COG3 845

and COG8 (a pair of interacting proteins) were used as the negative control (Tan et al., 846

1996). Bars = 10 μm. 847

(C) Co-IP assay showing that Sec23c can be immunoprecipitated by anti-GOT1B848

polyclonal antibodies in total extract of developing endosperm. Immunoblots with 849

anti-PDIL1-1 and anti-Sec12b antibodies showing no ER lumenal and membrane 850

protein contamination in the IP samples. Red arrows indicate the corresponding 851

protein bands. Triangles indicate the heavy chain of rabbit IgG protein. T, total extract; 852

IP, immunoprecipitation; IB, immunoblot. 853

(D) Co-IP assay showing that both Sec23c and GOT1B can be immunoprecipitated by854

anti-OsSar1b antibodies in total extract of developing endosperm. 855

(E) Immunoblot analysis of the IP samples with anti-phosphorylation antibodies (left)856

and anti-Sec23c antibodies (right), respectively. M, protein markers. 857

858

Figure 8. Mutation of GOT1B Affects the Distribution of COPII Coat 859

Components and ERESs. 860

(A) Immunoblot analysis showing the distribution of COPII coat components in the861

various membrane fractions in wild type and gpa4-1. P2, pellet obtained following the 862

centrifugation at 2,000g; P13, pellet obtained following the centrifugation at 13,000g. 863

P100, pellet obtained following centrifugation at 100,000g; S100, supernatant 864

obtained following centrifugation at 100,000g. 865

- 39 -

(B) Quantitative analysis of the ratio of the signal intensity of membrane fractions 866

compared with total proteins (P2 + P13 + P100/Total, Total = P2 + P13 + P100 + 867

S100) in the immunoblot shown in (A). Three independent experiments were 868

performed. Values are mean ± SD. 869

(C) Quantitative analysis of the ratio of signal intensity of each protein in P13 870

compared with total protein in the immunoblot shown in (A). **P < 0.01 (n = 3 871

independent experiments, Student’s t test). 872

(D) Fluorescence observation of the ERES status (marked by AtSar1b-GFP) in root 873

cells of wild type and the gpa4-2 mutant. Bars = 10 µm. 874

(E) In vivo co-IP assay showing that reduced amounts of Sec23c were precipitated in 875

gpa4-1 mutant compared to wild type. Immunoblots with Anti-PDIL1-1 and 876

anti-Sec12b antibodies showing no ER lumenal and membrane protein contamination 877

in the IP samples. 878

(F) A working model depicting the function of GOT1B in the formation of COPII 879

vesicles. GOT1B participates in COPII coat formation at the ERESs via interaction 880

with Sec23c. The heterodimer of Sec23/Sec24 is recruited by GOT1B and Sar1 881

cooperatively to form the pre-budding complexes in which proglutelin cargos are 882

loaded. Then, the heterotetrimer of Sec13/Sec31 is recruited to form the outer coat of 883

the COPII vesicles before vesicle budding and subsequent fusion with the cis-Golgi 884

apparatus. 885

886

887

Parsed CitationsAridor, M., Weissman, J., Bannykh, S., Nuoffer, C., and Balch, W.E. (1998). Cargo selection by the COPII budding machinery duringexport from the ER. J. Cell Biol. 141: 61-70.

Pubmed: Author and TitleCrossRef: Author and TitleGoogle Scholar: Author Only Title Only Author and Title

Barlowe, C., and Schekman, R. (1993). SEC12 encodes a guanine-nucleotide-exchange factor essential for transport vesiclebudding from the ER. Nature 365: 347-349.


Bechtel, D.B., and Juliano, B.O. (1980). Formation of protein bodies in the starchy endosperm of rice (Oryza sativa L.): a re-investigation. Ann. Bot. 45: 503-509.


Bi, X., Corpina, R.A., and Goldberg, J. (2002). Structure of the Sec23/24-Sar1 pre-budding complex of the COPII vesicle coat.Nature 419: 271-277.


Bi, X., Mancias, J.D., and Goldberg, J. (2007). Insights into COPII coat nucleation from the structure of Sec23.Sar1 complexed withthe active fragment of Sec31. Dev. Cell 13: 635-645.


Brandizzi, F., Snapp, E., Roberts, A., Lippincott-Schwartz, J., and Hawe, C. (2002). Membrane protein transport between the ER andGolgi in tobacco leaves is energy dependent but cytoskeleton independent: evidence from selective photobleaching. Plan Cell14: 1293-1309


Conchon, S., Cao, X., Barlowe, C., and R.B.?elham, H. (1999). Got1p and Sft2p: membrane proteins involved in traffic to the Golgicomplex. EMBO J. 18: 3934-3946.


D'Arcangelo, J.G., Stahmer, K.R., and Miller, E.A. (2013). Vesicle-mediated export from the ER: COPII coat function and regulation.Biochim. Biophys. Acta. 1833: 2464-2472.


daSilva, L.L., Snapp, E.L., Denecke, J., Lippincott-Schwartz, J., Hawes, C., and Brandizzi, F. (2004). Endoplasmic reticulum exportsites and Golgi bodies behave as single mobile secretory units in plant cells. Plant Cell 16: 1753-1771.


Faso, C., Chen, Y., Tamura, K. Held, M., Zemelis, S. Marti, L., Saravanan, R. Hummel, E., Kung, L., Miller, E., Hawes, C., andBrandizzi, F. (2009). A missense mutation in the Arabidopsis COPII coat protein Sec24A induces the formation of clusters of theEndoplasmic Reticulum and Golgi apparatus. Plant Cell 21: 3655-3671.


French, A.P., Mills, S., Swarup, R., Bennett, M.J., and Pridmore, T.P. (2008). Colocalization of fluorescent markers in confocalmicroscope images of plant cells. Nat. Protoc. 3: 619-628.


Fromme, J.C., Orci, L., and Schekman, R. (2008). Coordination of COPII vesicle trafficking by Sec23. Trends Cell Biol. 18: 330-336.Pubmed: Author and TitleCrossRef: Author and TitleGoogle Scholar: Author Only Title Only Author and Title

Fukuda, M., Kawagoe, Y., Murakami, T., Washida, H., Sugino, A., Nagamine, A., Okita,T.W., Ogawa, M., and Kumamaru, T. (2016) Thedual roles of the Golgi Transport 1 (GOT1B): RNA localization to the cortical Endoplasmic Reticulum and the export of proglutelinand a-globulin from the cortical-ER to the Golgi. Plant Cell Physiol. doi: 10.1093/pcp/pcw154

Pubmed: Author and Title

http://www.ncbi.nlm.nih.gov/pubmed?term=Aridor%2C M%2E%2C Weissman%2C J%2E%2C Bannykh%2C S%2E%2C Nuoffer%2C C%2E%2C and Balch%2C W%2EE%2E %281998%29%2E Cargo selection by the COPII budding machinery during export from the ER%2E J%2E Cell Biol%2E 141%3A 61%2D70%2E&dopt=abstract

http://search.crossref.org/?page=1&rows=2&q=Aridor, M., Weissman, J., Bannykh, S., Nuoffer, C., and Balch, W.E. (1998). Cargo selection by the COPII budding machinery during export from the ER. J. Cell Biol. 141: 61-70.

http://scholar.google.com/scholar?as_q=&num=10&as_occt=any&as_sauthors=Aridor,&hl=en&c2coff=1

http://scholar.google.com/scholar?as_q=Cargo selection by the COPII budding machinery during export from the ER&num=10&btnG=Search+Scholar&as_epq=&as_oq=&as_eq=&as_occt=any&as_publication=&as_yhi=&as_allsubj=all&hl=en&lr=&c2coff=1

http://scholar.google.com/scholar?as_q=Cargo selection by the COPII budding machinery during export from the ER&num=10&btnG=Search+Scholar&as_occt=any&as_sauthors=Aridor,&as_ylo=1998&as_allsubj=all&hl=en&c2coff=1

http://www.ncbi.nlm.nih.gov/pubmed?term=Barlowe%2C C%2E%2C and Schekman%2C R%2E %281993%29%2E SEC12 encodes a guanine%2Dnucleotide%2Dexchange factor essential for transport vesicle budding from the ER%2E Nature 365%3A 347%2D349%2E&dopt=abstract

http://search.crossref.org/?page=1&rows=2&q=Barlowe, C., and Schekman, R. (1993). SEC12 encodes a guanine-nucleotide-exchange factor essential for transport vesicle budding from the ER. Nature 365: 347-349.

http://scholar.google.com/scholar?as_q=&num=10&as_occt=any&as_sauthors=Barlowe,&hl=en&c2coff=1

http://scholar.google.com/scholar?as_q=SEC12 encodes a guanine-nucleotide-exchange factor essential for transport vesicle budding from the ER&num=10&btnG=Search+Scholar&as_epq=&as_oq=&as_eq=&as_occt=any&as_publication=&as_yhi=&as_allsubj=all&hl=en&lr=&c2coff=1

http://scholar.google.com/scholar?as_q=SEC12 encodes a guanine-nucleotide-exchange factor essential for transport vesicle budding from the ER&num=10&btnG=Search+Scholar&as_occt=any&as_sauthors=Barlowe,&as_ylo=1993&as_allsubj=all&hl=en&c2coff=1

http://www.ncbi.nlm.nih.gov/pubmed?term=Bechtel%2C D%2EB%2E%2C and Juliano%2C B%2EO%2E %281980%29%2E Formation of protein bodies in the starchy endosperm of rice %28Oryza sativa L%2E%29%3A a re%2Dinvestigation%2E Ann%2E Bot%2E 45%3A 503%2D509%2E&dopt=abstract

http://search.crossref.org/?page=1&rows=2&q=Bechtel, D.B., and Juliano, B.O. (1980). Formation of protein bodies in the starchy endosperm of rice (Oryza sativa L.): a re-investigation. Ann. Bot. 45: 503-509.

http://scholar.google.com/scholar?as_q=&num=10&as_occt=any&as_sauthors=Bechtel,&hl=en&c2coff=1

http://scholar.google.com/scholar?as_q=Formation of protein bodies in the starchy endosperm of rice (Oryza sativa L&num=10&btnG=Search+Scholar&as_epq=&as_oq=&as_eq=&as_occt=any&as_publication=&as_yhi=&as_allsubj=all&hl=en&lr=&c2coff=1

http://scholar.google.com/scholar?as_q=Formation of protein bodies in the starchy endosperm of rice (Oryza sativa L&num=10&btnG=Search+Scholar&as_occt=any&as_sauthors=Bechtel,&as_ylo=1980&as_allsubj=all&hl=en&c2coff=1

http://www.ncbi.nlm.nih.gov/pubmed?term=Bi%2C X%2E%2C Corpina%2C R%2EA%2E%2C and Goldberg%2C J%2E %282002%29%2E Structure of the Sec23%2F24%2DSar1 pre%2Dbudding complex of the COPII vesicle coat%2E Nature 419%3A 271%2D277%2E&dopt=abstract

http://search.crossref.org/?page=1&rows=2&q=Bi, X., Corpina, R.A., and Goldberg, J. (2002). Structure of the Sec23/24-Sar1 pre-budding complex of the COPII vesicle coat. Nature 419: 271-277.

http://scholar.google.com/scholar?as_q=&num=10&as_occt=any&as_sauthors=Bi,&hl=en&c2coff=1

http://scholar.google.com/scholar?as_q=Structure of the Sec23/24-Sar1 pre-budding complex of the COPII vesicle coat&num=10&btnG=Search+Scholar&as_epq=&as_oq=&as_eq=&as_occt=any&as_publication=&as_yhi=&as_allsubj=all&hl=en&lr=&c2coff=1

http://scholar.google.com/scholar?as_q=Structure of the Sec23/24-Sar1 pre-budding complex of the COPII vesicle coat&num=10&btnG=Search+Scholar&as_occt=any&as_sauthors=Bi,&as_ylo=2002&as_allsubj=all&hl=en&c2coff=1

http://www.ncbi.nlm.nih.gov/pubmed?term=Bi%2C X%2E%2C Mancias%2C J%2ED%2E%2C and Goldberg%2C J%2E %282007%29%2E Insights into COPII coat nucleation from the structure of Sec23%2ESar1 complexed with the active fragment of Sec31%2E Dev%2E Cell 13%3A 635%2D645%2E&dopt=abstract

http://search.crossref.org/?page=1&rows=2&q=Bi, X., Mancias, J.D., and Goldberg, J. (2007). Insights into COPII coat nucleation from the structure of Sec23.Sar1 complexed with the active fragment of Sec31. Dev. Cell 13: 635-645.

http://scholar.google.com/scholar?as_q=&num=10&as_occt=any&as_sauthors=Bi,&hl=en&c2coff=1

http://scholar.google.com/scholar?as_q=Insights into COPII coat nucleation from the structure of Sec23&num=10&btnG=Search+Scholar&as_epq=&as_oq=&as_eq=&as_occt=any&as_publication=&as_yhi=&as_allsubj=all&hl=en&lr=&c2coff=1

http://scholar.google.com/scholar?as_q=Insights into COPII coat nucleation from the structure of Sec23&num=10&btnG=Search+Scholar&as_occt=any&as_sauthors=Bi,&as_ylo=2007&as_allsubj=all&hl=en&c2coff=1

http://www.ncbi.nlm.nih.gov/pubmed?term=Brandizzi%2C F%2E%2C Snapp%2C E%2E%2C Roberts%2C A%2E%2C Lippincott%2DSchwartz%2C J%2E%2C and Hawe%2C C%2E %282002%29%2E Membrane protein transport between the ER and Golgi in tobacco leaves is energy dependent but cytoskeleton independent%3A evidence from selective photobleaching%2E Plan Cell 14%3A 1293%2D1309&dopt=abstract

http://search.crossref.org/?page=1&rows=2&q=Brandizzi, F., Snapp, E., Roberts, A., Lippincott-Schwartz, J., and Hawe, C. (2002). Membrane protein transport between the ER and Golgi in tobacco leaves is energy dependent but cytoskeleton independent: evidence from selective photobleaching. Plan Cell 14: 1293-1309

http://scholar.google.com/scholar?as_q=&num=10&as_occt=any&as_sauthors=Brandizzi,&hl=en&c2coff=1

http://scholar.google.com/scholar?as_q=Membrane protein transport between the ER and Golgi in tobacco leaves is energy dependent but cytoskeleton independent: evidence from selective photobleaching&num=10&btnG=Search+Scholar&as_epq=&as_oq=&as_eq=&as_occt=any&as_publication=&as_yhi=&as_allsubj=all&hl=en&lr=&c2coff=1

http://scholar.google.com/scholar?as_q=Membrane protein transport between the ER and Golgi in tobacco leaves is energy dependent but cytoskeleton independent: evidence from selective photobleaching&num=10&btnG=Search+Scholar&as_occt=any&as_sauthors=Brandizzi,&as_ylo=2002&as_allsubj=all&hl=en&c2coff=1

http://www.ncbi.nlm.nih.gov/pubmed?term=Conchon%2C S%2E%2C Cao%2C X%2E%2C Barlowe%2C C%2E%2C and R%2EB%2E%3Felham%2C H%2E %281999%29%2E Got1p and Sft2p%3A membrane proteins involved in traffic to the Golgi complex%2E EMBO J%2E 18%3A 3934%2D3946%2E&dopt=abstract

http://search.crossref.org/?page=1&rows=2&q=Conchon, S., Cao, X., Barlowe, C., and R.B.?elham, H. (1999). Got1p and Sft2p: membrane proteins involved in traffic to the Golgi complex. EMBO J. 18: 3934-3946.

http://scholar.google.com/scholar?as_q=&num=10&as_occt=any&as_sauthors=Conchon,&hl=en&c2coff=1

http://scholar.google.com/scholar?as_q=Got1p and Sft2p: membrane proteins involved in traffic to the Golgi complex&num=10&btnG=Search+Scholar&as_epq=&as_oq=&as_eq=&as_occt=any&as_publication=&as_yhi=&as_allsubj=all&hl=en&lr=&c2coff=1

http://scholar.google.com/scholar?as_q=Got1p and Sft2p: membrane proteins involved in traffic to the Golgi complex&num=10&btnG=Search+Scholar&as_occt=any&as_sauthors=Conchon,&as_ylo=1999&as_allsubj=all&hl=en&c2coff=1

http://www.ncbi.nlm.nih.gov/pubmed?term=D%27Arcangelo%2C J%2EG%2E%2C Stahmer%2C K%2ER%2E%2C and Miller%2C E%2EA%2E %282013%29%2E Vesicle%2Dmediated export from the ER%3A COPII coat function and regulation%2E Biochim%2E Biophys%2E Acta%2E 1833%3A 2464%2D2472%2E&dopt=abstract

http://search.crossref.org/?page=1&rows=2&q=D'Arcangelo, J.G., Stahmer, K.R., and Miller, E.A. (2013). Vesicle-mediated export from the ER: COPII coat function and regulation. Biochim. Biophys. Acta. 1833: 2464-2472.

http://scholar.google.com/scholar?as_q=&num=10&as_occt=any&as_sauthors=D'Arcangelo,&hl=en&c2coff=1

http://scholar.google.com/scholar?as_q=Vesicle-mediated export from the ER: COPII coat function and regulation&num=10&btnG=Search+Scholar&as_epq=&as_oq=&as_eq=&as_occt=any&as_publication=&as_yhi=&as_allsubj=all&hl=en&lr=&c2coff=1

http://scholar.google.com/scholar?as_q=Vesicle-mediated export from the ER: COPII coat function and regulation&num=10&btnG=Search+Scholar&as_occt=any&as_sauthors=D'Arcangelo,&as_ylo=2013&as_allsubj=all&hl=en&c2coff=1

http://www.ncbi.nlm.nih.gov/pubmed?term=daSilva%2C L%2EL%2E%2C Snapp%2C E%2EL%2E%2C Denecke%2C J%2E%2C Lippincott%2DSchwartz%2C J%2E%2C Hawes%2C C%2E%2C and Brandizzi%2C F%2E %282004%29%2E Endoplasmic reticulum export sites and Golgi bodies behave as single mobile secretory units in plant cells%2E Plant Cell 16%3A 1753%2D1771%2E&dopt=abstract

http://search.crossref.org/?page=1&rows=2&q=daSilva, L.L., Snapp, E.L., Denecke, J., Lippincott-Schwartz, J., Hawes, C., and Brandizzi, F. (2004). Endoplasmic reticulum export sites and Golgi bodies behave as single mobile secretory units in plant cells. Plant Cell 16: 1753-1771.

http://scholar.google.com/scholar?as_q=&num=10&as_occt=any&as_sauthors=daSilva,&hl=en&c2coff=1

http://scholar.google.com/scholar?as_q=Endoplasmic reticulum export sites and Golgi bodies behave as single mobile secretory units in plant cells&num=10&btnG=Search+Scholar&as_epq=&as_oq=&as_eq=&as_occt=any&as_publication=&as_yhi=&as_allsubj=all&hl=en&lr=&c2coff=1

http://scholar.google.com/scholar?as_q=Endoplasmic reticulum export sites and Golgi bodies behave as single mobile secretory units in plant cells&num=10&btnG=Search+Scholar&as_occt=any&as_sauthors=daSilva,&as_ylo=2004&as_allsubj=all&hl=en&c2coff=1

http://www.ncbi.nlm.nih.gov/pubmed?term=Faso%2C C%2E%2C Chen%2C Y%2E%2C Tamura%2C K%2E Held%2C M%2E%2C Zemelis%2C S%2E Marti%2C L%2E%2C Saravanan%2C R%2E Hummel%2C E%2E%2C Kung%2C L%2E%2C Miller%2C E%2E%2C Hawes%2C C%2E%2C and Brandizzi%2C F%2E %282009%29%2E A missense mutation in the Arabidopsis COPII coat protein Sec24A induces the formation of clusters of the Endoplasmic Reticulum and Golgi apparatus%2E Plant Cell 21%3A 3655%2D3671%2E&dopt=abstract

http://search.crossref.org/?page=1&rows=2&q=Faso, C., Chen, Y., Tamura, K. Held, M., Zemelis, S. Marti, L., Saravanan, R. Hummel, E., Kung, L., Miller, E., Hawes, C., and Brandizzi, F. (2009). A missense mutation in the Arabidopsis COPII coat protein Sec24A induces the formation of clusters of the Endoplasmic Reticulum and Golgi apparatus. Plant Cell 21: 3655-3671.

http://scholar.google.com/scholar?as_q=&num=10&as_occt=any&as_sauthors=Faso,&hl=en&c2coff=1

http://scholar.google.com/scholar?as_q=A missense mutation in the Arabidopsis COPII coat protein Sec24A induces the formation of clusters of the Endoplasmic Reticulum and Golgi apparatus&num=10&btnG=Search+Scholar&as_epq=&as_oq=&as_eq=&as_occt=any&as_publication=&as_yhi=&as_allsubj=all&hl=en&lr=&c2coff=1

http://scholar.google.com/scholar?as_q=A missense mutation in the Arabidopsis COPII coat protein Sec24A induces the formation of clusters of the Endoplasmic Reticulum and Golgi apparatus&num=10&btnG=Search+Scholar&as_occt=any&as_sauthors=Faso,&as_ylo=2009&as_allsubj=all&hl=en&c2coff=1

http://www.ncbi.nlm.nih.gov/pubmed?term=French%2C A%2EP%2E%2C Mills%2C S%2E%2C Swarup%2C R%2E%2C Bennett%2C M%2EJ%2E%2C and Pridmore%2C T%2EP%2E %282008%29%2E Colocalization of fluorescent markers in confocal microscope images of plant cells%2E Nat%2E Protoc%2E 3%3A 619%2D628%2E&dopt=abstract

http://search.crossref.org/?page=1&rows=2&q=French, A.P., Mills, S., Swarup, R., Bennett, M.J., and Pridmore, T.P. (2008). Colocalization of fluorescent markers in confocal microscope images of plant cells. Nat. Protoc. 3: 619-628.

http://scholar.google.com/scholar?as_q=&num=10&as_occt=any&as_sauthors=French,&hl=en&c2coff=1

http://scholar.google.com/scholar?as_q=Colocalization of fluorescent markers in confocal microscope images of plant cells&num=10&btnG=Search+Scholar&as_epq=&as_oq=&as_eq=&as_occt=any&as_publication=&as_yhi=&as_allsubj=all&hl=en&lr=&c2coff=1

http://scholar.google.com/scholar?as_q=Colocalization of fluorescent markers in confocal microscope images of plant cells&num=10&btnG=Search+Scholar&as_occt=any&as_sauthors=French,&as_ylo=2008&as_allsubj=all&hl=en&c2coff=1

http://www.ncbi.nlm.nih.gov/pubmed?term=Fromme%2C J%2EC%2E%2C Orci%2C L%2E%2C and Schekman%2C R%2E %282008%29%2E Coordination of COPII vesicle trafficking by Sec23%2E Trends Cell Biol%2E 18%3A 330%2D336%2E&dopt=abstract

http://search.crossref.org/?page=1&rows=2&q=Fromme, J.C., Orci, L., and Schekman, R. (2008). Coordination of COPII vesicle trafficking by Sec23. Trends Cell Biol. 18: 330-336.

http://scholar.google.com/scholar?as_q=&num=10&as_occt=any&as_sauthors=Fromme,&hl=en&c2coff=1

http://scholar.google.com/scholar?as_q=Coordination of COPII vesicle trafficking by Sec23&num=10&btnG=Search+Scholar&as_epq=&as_oq=&as_eq=&as_occt=any&as_publication=&as_yhi=&as_allsubj=all&hl=en&lr=&c2coff=1

http://scholar.google.com/scholar?as_q=Coordination of COPII vesicle trafficking by Sec23&num=10&btnG=Search+Scholar&as_occt=any&as_sauthors=Fromme,&as_ylo=2008&as_allsubj=all&hl=en&c2coff=1

http://www.ncbi.nlm.nih.gov/pubmed?term=Fukuda%2C M%2E%2C Kawagoe%2C Y%2E%2C Murakami%2C T%2E%2C Washida%2C H%2E%2C Sugino%2C A%2E%2C Nagamine%2C A%2E%2C Okita%2CT%2EW%2E%2C Ogawa%2C M%2E%2C and Kumamaru%2C T%2E %282016%29 The dual roles of the Golgi Transport 1 %28GOT1B%29%3A RNA localization to the cortical Endoplasmic Reticulum and the export of proglutelin and a%2Dglobulin from the cortical%2DER to the Golgi%2E Plant Cell Physiol%2E doi%3A 10%2E1093%2Fpcp%2Fpcw154&dopt=abstract

CrossRef: Author and TitleGoogle Scholar: Author Only Title Only Author and Title

Fukuda, M., Satoh-Cruz, M., Wen, L., Crofts, A.J., Sugino, A., Washida, H., Okita, T.W., Ogawa, M., Kawagoe, Y., Maeshima, M., andKumamaru, T. (2011). The small GTPase Rab5a is essential for intracellular transport of proglutelin from the Golgi apparatus to theprotein storage vacuole and endosomal membrane organization in developing rice endosperm. Plant Physiol. 157: 632-644.


Fukuda, M., Wen, L., Satoh-Cruz, M., Kawagoe, Y., Nagamura, Y., Okita, T.W., Washida, H., Sugino, A., Ishino, S., Ishino, Y., Ogawa,M., Sunada, M., Ueda, T., and Kumamaru, T. (2013). A guanine nucleotide exchange factor for Rab5 proteins is essential forintracellular transport of the proglutelin from the Golgi apparatus to the protein storage vacuole in rice endosperm. Plant Physiol.162: 663-674.


Giraudo, C.G., and Maccioni, H.J. (2003). Endoplasmic reticulum export of glycosyltransferases depends on interaction of acytoplasmic dibasic motif with Sar1. Mol. Biol. Cell. 14: 3753-3766.


Hanton, S.L., Chatre, L., Matheson, L.A., Rossi, M., Held, M.A., Brandizzi, F. (2008). Plant Sar1 isoforms with near-identical proteinsequences exhibit different localisations and effects on secretion. Plant Mol. Biol. 67: 283-294.


Hanton, S.L., Chatre, L., Renna, L., Matheson, L.A., and Brandizzi, F. (2007). De novo formation of plant endoplasmic reticulumexport sites is membrane cargo induced and signal mediated. Plant Physiol. 143: 1640-1650.


Hanton, S.L., Matheson, L.A., Chatre, L., and Brandizzi, F. (2009). Dynamic organization of COPII coat proteins at endoplasmicreticulum export sites in plant cells. Plant J. 57: 963-974.


Heidtman, M., Chen, C.Z., Collins, R.N., and Barlowe, C. (2005). Yos1p is a novel subunit of the Yip1p-Yif1p complex and is requiredfor transport between the endoplasmic reticulum and the Golgi complex. Mol. Biol. Cell 16: 1673-1683.


Huh, W.K., Falvo, J.V., Gerke, L.C., Carroll, A.S., Howson, R.W., Weissman, J.S., and O'Shea, E.K. (2003). Global analysis of proteinlocalization in budding yeast. Nature 425: 686-691.


Johnsson, N., and Varshavsky, A. (1994). Split ubiquitin as a sensor of protein interactions in vivo. Proc. Natl. Acad. Sci. USA 91:10340-10344.


Krishnan, H.B., Franceschi, V.R., and Okita, T.W. (1986). Immunochemical studies on the role of the Golgi complex in protein-bodyformation in rice seeds. Planta 169: 471-480.


Li, L., Shimada, T., Takahashi, H., Ueda, H., Fukao, Y., Kondo, M., Nishimura, M., Hara-Nishimura, I. (2006). MAIGO2 is involved inexit of seed storage proteins from the endoplasmic reticulum in Arabidopsis thaliana. Plant Cell 18: 3535-3547.


Liu, F., Ren, Y., Wang, Y., Peng, C., Zhou, K., Lv, J., Guo, X., Zhang, X., Zhong, M., Zhao, S.. Jiang, L., Wang, H., Bao, Y., and Wan, J.(2013). OsVPS9A functions cooperatively with OsRAB5A to regulate post-Golgi dense vesicle-mediated storage protein traffickingto protein storage vacuole in rice endosperm cells. Mol. Plant 6: 1918-1932.


Lord, C., Bhandari, D., Menon, S., Ghassemian, M., Nycz, D., Hay, J., Ghosh, P., Ferro-Novick, S. (2011). Sequential interactions

http://search.crossref.org/?page=1&rows=2&q=Fukuda, M., Kawagoe, Y., Murakami, T., Washida, H., Sugino, A., Nagamine, A., Okita,T.W., Ogawa, M., and Kumamaru, T. (2016) The dual roles of the Golgi Transport 1 (GOT1B): RNA localization to the cortical Endoplasmic Reticulum and the export of proglutelin and a-globulin from the cortical-ER to the Golgi. Plant Cell Physiol. doi: 10.1093/pcp/pcw154

http://scholar.google.com/scholar?as_q=&num=10&as_occt=any&as_sauthors=Fukuda,&hl=en&c2coff=1

http://scholar.google.com/scholar?as_q=The dual roles of the Golgi Transport 1 (GOT1B): RNA localization to the cortical Endoplasmic Reticulum and the export of proglutelin and a-globulin from the cortical-ER to the Golgi.&num=10&btnG=Search+Scholar&as_epq=&as_oq=&as_eq=&as_occt=any&as_publication=&as_yhi=&as_allsubj=all&hl=en&lr=&c2coff=1

http://scholar.google.com/scholar?as_q=The dual roles of the Golgi Transport 1 (GOT1B): RNA localization to the cortical Endoplasmic Reticulum and the export of proglutelin and a-globulin from the cortical-ER to the Golgi.&num=10&btnG=Search+Scholar&as_occt=any&as_sauthors=Fukuda,&as_ylo=2016&as_allsubj=all&hl=en&c2coff=1

http://www.ncbi.nlm.nih.gov/pubmed?term=Fukuda%2C M%2E%2C Satoh%2DCruz%2C M%2E%2C Wen%2C L%2E%2C Crofts%2C A%2EJ%2E%2C Sugino%2C A%2E%2C Washida%2C H%2E%2C Okita%2C T%2EW%2E%2C Ogawa%2C M%2E%2C Kawagoe%2C Y%2E%2C Maeshima%2C M%2E%2C and Kumamaru%2C T%2E %282011%29%2E The small GTPase Rab5a is essential for intracellular transport of proglutelin from the Golgi apparatus to the protein storage vacuole and endosomal membrane organization in developing rice endosperm%2E Plant Physiol%2E 157%3A 632%2D644%2E&dopt=abstract

http://search.crossref.org/?page=1&rows=2&q=Fukuda, M., Satoh-Cruz, M., Wen, L., Crofts, A.J., Sugino, A., Washida, H., Okita, T.W., Ogawa, M., Kawagoe, Y., Maeshima, M., and Kumamaru, T. (2011). The small GTPase Rab5a is essential for intracellular transport of proglutelin from the Golgi apparatus to the protein storage vacuole and endosomal membrane organization in developing rice endosperm. Plant Physiol. 157: 632-644.


http://scholar.google.com/scholar?as_q=The small GTPase Rab5a is essential for intracellular transport of proglutelin from the Golgi apparatus to the protein storage vacuole and endosomal membrane organization in developing rice endosperm&num=10&btnG=Search+Scholar&as_epq=&as_oq=&as_eq=&as_occt=any&as_publication=&as_yhi=&as_allsubj=all&hl=en&lr=&c2coff=1

http://scholar.google.com/scholar?as_q=The small GTPase Rab5a is essential for intracellular transport of proglutelin from the Golgi apparatus to the protein storage vacuole and endosomal membrane organization in developing rice endosperm&num=10&btnG=Search+Scholar&as_occt=any&as_sauthors=Fukuda,&as_ylo=2011&as_allsubj=all&hl=en&c2coff=1

http://www.ncbi.nlm.nih.gov/pubmed?term=Fukuda%2C M%2E%2C Wen%2C L%2E%2C Satoh%2DCruz%2C M%2E%2C Kawagoe%2C Y%2E%2C Nagamura%2C Y%2E%2C Okita%2C T%2EW%2E%2C Washida%2C H%2E%2C Sugino%2C A%2E%2C Ishino%2C S%2E%2C Ishino%2C Y%2E%2C Ogawa%2C M%2E%2C Sunada%2C M%2E%2C Ueda%2C T%2E%2C and Kumamaru%2C T%2E %282013%29%2E A guanine nucleotide exchange factor for Rab5 proteins is essential for intracellular transport of the proglutelin from the Golgi apparatus to the protein storage vacuole in rice endosperm%2E Plant Physiol%2E 162%3A 663%2D674%2E&dopt=abstract

http://search.crossref.org/?page=1&rows=2&q=Fukuda, M., Wen, L., Satoh-Cruz, M., Kawagoe, Y., Nagamura, Y., Okita, T.W., Washida, H., Sugino, A., Ishino, S., Ishino, Y., Ogawa, M., Sunada, M., Ueda, T., and Kumamaru, T. (2013). A guanine nucleotide exchange factor for Rab5 proteins is essential for intracellular transport of the proglutelin from the Golgi apparatus to the protein storage vacuole in rice endosperm. Plant Physiol. 162: 663-674.


http://scholar.google.com/scholar?as_q=A guanine nucleotide exchange factor for Rab5 proteins is essential for intracellular transport of the proglutelin from the Golgi apparatus to the protein storage vacuole in rice endosperm&num=10&btnG=Search+Scholar&as_epq=&as_oq=&as_eq=&as_occt=any&as_publication=&as_yhi=&as_allsubj=all&hl=en&lr=&c2coff=1

http://scholar.google.com/scholar?as_q=A guanine nucleotide exchange factor for Rab5 proteins is essential for intracellular transport of the proglutelin from the Golgi apparatus to the protein storage vacuole in rice endosperm&num=10&btnG=Search+Scholar&as_occt=any&as_sauthors=Fukuda,&as_ylo=2013&as_allsubj=all&hl=en&c2coff=1

http://www.ncbi.nlm.nih.gov/pubmed?term=Giraudo%2C C%2EG%2E%2C and Maccioni%2C H%2EJ%2E %282003%29%2E Endoplasmic reticulum export of glycosyltransferases depends on interaction of a cytoplasmic dibasic motif with Sar1%2E Mol%2E Biol%2E Cell%2E 14%3A 3753%2D3766%2E&dopt=abstract

http://search.crossref.org/?page=1&rows=2&q=Giraudo, C.G., and Maccioni, H.J. (2003). Endoplasmic reticulum export of glycosyltransferases depends on interaction of a cytoplasmic dibasic motif with Sar1. Mol. Biol. Cell. 14: 3753-3766.

http://scholar.google.com/scholar?as_q=&num=10&as_occt=any&as_sauthors=Giraudo,&hl=en&c2coff=1

http://scholar.google.com/scholar?as_q=Endoplasmic reticulum export of glycosyltransferases depends on interaction of a cytoplasmic dibasic motif with Sar1&num=10&btnG=Search+Scholar&as_epq=&as_oq=&as_eq=&as_occt=any&as_publication=&as_yhi=&as_allsubj=all&hl=en&lr=&c2coff=1

http://scholar.google.com/scholar?as_q=Endoplasmic reticulum export of glycosyltransferases depends on interaction of a cytoplasmic dibasic motif with Sar1&num=10&btnG=Search+Scholar&as_occt=any&as_sauthors=Giraudo,&as_ylo=2003&as_allsubj=all&hl=en&c2coff=1

http://www.ncbi.nlm.nih.gov/pubmed?term=Hanton%2C S%2EL%2E%2C Chatre%2C L%2E%2C Matheson%2C L%2EA%2E%2C Rossi%2C M%2E%2C Held%2C M%2EA%2E%2C Brandizzi%2C F%2E %282008%29%2E Plant Sar1 isoforms with near%2Didentical protein sequences exhibit different localisations and effects on secretion%2E Plant Mol%2E Biol%2E 67%3A 283%2D294%2E&dopt=abstract

http://search.crossref.org/?page=1&rows=2&q=Hanton, S.L., Chatre, L., Matheson, L.A., Rossi, M., Held, M.A., Brandizzi, F. (2008). Plant Sar1 isoforms with near-identical protein sequences exhibit different localisations and effects on secretion. Plant Mol. Biol. 67: 283-294.

http://scholar.google.com/scholar?as_q=&num=10&as_occt=any&as_sauthors=Hanton,&hl=en&c2coff=1

http://scholar.google.com/scholar?as_q=Plant Sar1 isoforms with near-identical protein sequences exhibit different localisations and effects on secretion&num=10&btnG=Search+Scholar&as_epq=&as_oq=&as_eq=&as_occt=any&as_publication=&as_yhi=&as_allsubj=all&hl=en&lr=&c2coff=1

http://scholar.google.com/scholar?as_q=Plant Sar1 isoforms with near-identical protein sequences exhibit different localisations and effects on secretion&num=10&btnG=Search+Scholar&as_occt=any&as_sauthors=Hanton,&as_ylo=2008&as_allsubj=all&hl=en&c2coff=1

http://www.ncbi.nlm.nih.gov/pubmed?term=Hanton%2C S%2EL%2E%2C Chatre%2C L%2E%2C Renna%2C L%2E%2C Matheson%2C L%2EA%2E%2C and Brandizzi%2C F%2E %282007%29%2E De novo formation of plant endoplasmic reticulum export sites is membrane cargo induced and signal mediated%2E Plant Physiol%2E 143%3A 1640%2D1650%2E&dopt=abstract

http://search.crossref.org/?page=1&rows=2&q=Hanton, S.L., Chatre, L., Renna, L., Matheson, L.A., and Brandizzi, F. (2007). De novo formation of plant endoplasmic reticulum export sites is membrane cargo induced and signal mediated. Plant Physiol. 143: 1640-1650.


http://scholar.google.com/scholar?as_q=De novo formation of plant endoplasmic reticulum export sites is membrane cargo induced and signal mediated&num=10&btnG=Search+Scholar&as_epq=&as_oq=&as_eq=&as_occt=any&as_publication=&as_yhi=&as_allsubj=all&hl=en&lr=&c2coff=1

http://scholar.google.com/scholar?as_q=De novo formation of plant endoplasmic reticulum export sites is membrane cargo induced and signal mediated&num=10&btnG=Search+Scholar&as_occt=any&as_sauthors=Hanton,&as_ylo=2007&as_allsubj=all&hl=en&c2coff=1

http://www.ncbi.nlm.nih.gov/pubmed?term=Hanton%2C S%2EL%2E%2C Matheson%2C L%2EA%2E%2C Chatre%2C L%2E%2C and Brandizzi%2C F%2E %282009%29%2E Dynamic organization of COPII coat proteins at endoplasmic reticulum export sites in plant cells%2E Plant J%2E 57%3A 963%2D974%2E&dopt=abstract

http://search.crossref.org/?page=1&rows=2&q=Hanton, S.L., Matheson, L.A., Chatre, L., and Brandizzi, F. (2009). Dynamic organization of COPII coat proteins at endoplasmic reticulum export sites in plant cells. Plant J. 57: 963-974.


http://scholar.google.com/scholar?as_q=Dynamic organization of COPII coat proteins at endoplasmic reticulum export sites in plant cells&num=10&btnG=Search+Scholar&as_epq=&as_oq=&as_eq=&as_occt=any&as_publication=&as_yhi=&as_allsubj=all&hl=en&lr=&c2coff=1

http://scholar.google.com/scholar?as_q=Dynamic organization of COPII coat proteins at endoplasmic reticulum export sites in plant cells&num=10&btnG=Search+Scholar&as_occt=any&as_sauthors=Hanton,&as_ylo=2009&as_allsubj=all&hl=en&c2coff=1

http://www.ncbi.nlm.nih.gov/pubmed?term=Heidtman%2C M%2E%2C Chen%2C C%2EZ%2E%2C Collins%2C R%2EN%2E%2C and Barlowe%2C C%2E %282005%29%2E Yos1p is a novel subunit of the Yip1p%2DYif1p complex and is required for transport between the endoplasmic reticulum and the Golgi complex%2E Mol%2E Biol%2E Cell 16%3A 1673%2D1683%2E&dopt=abstract

http://search.crossref.org/?page=1&rows=2&q=Heidtman, M., Chen, C.Z., Collins, R.N., and Barlowe, C. (2005). Yos1p is a novel subunit of the Yip1p-Yif1p complex and is required for transport between the endoplasmic reticulum and the Golgi complex. Mol. Biol. Cell 16: 1673-1683.

http://scholar.google.com/scholar?as_q=&num=10&as_occt=any&as_sauthors=Heidtman,&hl=en&c2coff=1

http://scholar.google.com/scholar?as_q=Yos1p is a novel subunit of the Yip1p-Yif1p complex and is required for transport between the endoplasmic reticulum and the Golgi complex&num=10&btnG=Search+Scholar&as_epq=&as_oq=&as_eq=&as_occt=any&as_publication=&as_yhi=&as_allsubj=all&hl=en&lr=&c2coff=1

http://scholar.google.com/scholar?as_q=Yos1p is a novel subunit of the Yip1p-Yif1p complex and is required for transport between the endoplasmic reticulum and the Golgi complex&num=10&btnG=Search+Scholar&as_occt=any&as_sauthors=Heidtman,&as_ylo=2005&as_allsubj=all&hl=en&c2coff=1

http://www.ncbi.nlm.nih.gov/pubmed?term=Huh%2C W%2EK%2E%2C Falvo%2C J%2EV%2E%2C Gerke%2C L%2EC%2E%2C Carroll%2C A%2ES%2E%2C Howson%2C R%2EW%2E%2C Weissman%2C J%2ES%2E%2C and O%27Shea%2C E%2EK%2E %282003%29%2E Global analysis of protein localization in budding yeast%2E Nature 425%3A 686%2D691%2E&dopt=abstract

http://search.crossref.org/?page=1&rows=2&q=Huh, W.K., Falvo, J.V., Gerke, L.C., Carroll, A.S., Howson, R.W., Weissman, J.S., and O'Shea, E.K. (2003). Global analysis of protein localization in budding yeast. Nature 425: 686-691.

http://scholar.google.com/scholar?as_q=&num=10&as_occt=any&as_sauthors=Huh,&hl=en&c2coff=1

http://scholar.google.com/scholar?as_q=Global analysis of protein localization in budding yeast&num=10&btnG=Search+Scholar&as_epq=&as_oq=&as_eq=&as_occt=any&as_publication=&as_yhi=&as_allsubj=all&hl=en&lr=&c2coff=1

http://scholar.google.com/scholar?as_q=Global analysis of protein localization in budding yeast&num=10&btnG=Search+Scholar&as_occt=any&as_sauthors=Huh,&as_ylo=2003&as_allsubj=all&hl=en&c2coff=1

http://www.ncbi.nlm.nih.gov/pubmed?term=Johnsson%2C N%2E%2C and Varshavsky%2C A%2E %281994%29%2E Split ubiquitin as a sensor of protein interactions in vivo%2E Proc%2E Natl%2E Acad%2E Sci%2E USA 91%3A 10340%2D10344%2E&dopt=abstract

http://search.crossref.org/?page=1&rows=2&q=Johnsson, N., and Varshavsky, A. (1994). Split ubiquitin as a sensor of protein interactions in vivo. Proc. Natl. Acad. Sci. USA 91: 10340-10344.

http://scholar.google.com/scholar?as_q=&num=10&as_occt=any&as_sauthors=Johnsson,&hl=en&c2coff=1

http://scholar.google.com/scholar?as_q=Split ubiquitin as a sensor of protein interactions in vivo&num=10&btnG=Search+Scholar&as_epq=&as_oq=&as_eq=&as_occt=any&as_publication=&as_yhi=&as_allsubj=all&hl=en&lr=&c2coff=1

http://scholar.google.com/scholar?as_q=Split ubiquitin as a sensor of protein interactions in vivo&num=10&btnG=Search+Scholar&as_occt=any&as_sauthors=Johnsson,&as_ylo=1994&as_allsubj=all&hl=en&c2coff=1

http://www.ncbi.nlm.nih.gov/pubmed?term=Krishnan%2C H%2EB%2E%2C Franceschi%2C V%2ER%2E%2C and Okita%2C T%2EW%2E %281986%29%2E Immunochemical studies on the role of the Golgi complex in protein%2Dbody formation in rice seeds%2E Planta 169%3A 471%2D480%2E&dopt=abstract

http://search.crossref.org/?page=1&rows=2&q=Krishnan, H.B., Franceschi, V.R., and Okita, T.W. (1986). Immunochemical studies on the role of the Golgi complex in protein-body formation in rice seeds. Planta 169: 471-480.

http://scholar.google.com/scholar?as_q=&num=10&as_occt=any&as_sauthors=Krishnan,&hl=en&c2coff=1

http://scholar.google.com/scholar?as_q=Immunochemical studies on the role of the Golgi complex in protein-body formation in rice seeds&num=10&btnG=Search+Scholar&as_epq=&as_oq=&as_eq=&as_occt=any&as_publication=&as_yhi=&as_allsubj=all&hl=en&lr=&c2coff=1

http://scholar.google.com/scholar?as_q=Immunochemical studies on the role of the Golgi complex in protein-body formation in rice seeds&num=10&btnG=Search+Scholar&as_occt=any&as_sauthors=Krishnan,&as_ylo=1986&as_allsubj=all&hl=en&c2coff=1

http://www.ncbi.nlm.nih.gov/pubmed?term=Li%2C L%2E%2C Shimada%2C T%2E%2C Takahashi%2C H%2E%2C Ueda%2C H%2E%2C Fukao%2C Y%2E%2C Kondo%2C M%2E%2C Nishimura%2C M%2E%2C Hara%2DNishimura%2C I%2E %282006%29%2E MAIGO2 is involved in exit of seed storage proteins from the endoplasmic reticulum in Arabidopsis thaliana%2E Plant Cell 18%3A 3535%2D3547%2E&dopt=abstract

http://search.crossref.org/?page=1&rows=2&q=Li, L., Shimada, T., Takahashi, H., Ueda, H., Fukao, Y., Kondo, M., Nishimura, M., Hara-Nishimura, I. (2006). MAIGO2 is involved in exit of seed storage proteins from the endoplasmic reticulum in Arabidopsis thaliana. Plant Cell 18: 3535-3547.

http://scholar.google.com/scholar?as_q=&num=10&as_occt=any&as_sauthors=Li,&hl=en&c2coff=1

http://scholar.google.com/scholar?as_q=MAIGO2 is involved in exit of seed storage proteins from the endoplasmic reticulum in Arabidopsis thaliana&num=10&btnG=Search+Scholar&as_epq=&as_oq=&as_eq=&as_occt=any&as_publication=&as_yhi=&as_allsubj=all&hl=en&lr=&c2coff=1

http://scholar.google.com/scholar?as_q=MAIGO2 is involved in exit of seed storage proteins from the endoplasmic reticulum in Arabidopsis thaliana&num=10&btnG=Search+Scholar&as_occt=any&as_sauthors=Li,&as_ylo=2006&as_allsubj=all&hl=en&c2coff=1

http://www.ncbi.nlm.nih.gov/pubmed?term=Liu%2C F%2E%2C Ren%2C Y%2E%2C Wang%2C Y%2E%2C Peng%2C C%2E%2C Zhou%2C K%2E%2C Lv%2C J%2E%2C Guo%2C X%2E%2C Zhang%2C X%2E%2C Zhong%2C M%2E%2C Zhao%2C S%2E%2E Jiang%2C L%2E%2C Wang%2C H%2E%2C Bao%2C Y%2E%2C and Wan%2C J%2E %282013%29%2E OsVPS9A functions cooperatively with OsRAB5A to regulate post%2DGolgi dense vesicle%2Dmediated storage protein trafficking to protein storage vacuole in rice endosperm cells%2E Mol%2E Plant 6%3A 1918%2D1932%2E&dopt=abstract

http://search.crossref.org/?page=1&rows=2&q=Liu, F., Ren, Y., Wang, Y., Peng, C., Zhou, K., Lv, J., Guo, X., Zhang, X., Zhong, M., Zhao, S.. Jiang, L., Wang, H., Bao, Y., and Wan, J. (2013). OsVPS9A functions cooperatively with OsRAB5A to regulate post-Golgi dense vesicle-mediated storage protein trafficking to protein storage vacuole in rice endosperm cells. Mol. Plant 6: 1918-1932.

http://scholar.google.com/scholar?as_q=&num=10&as_occt=any&as_sauthors=Liu,&hl=en&c2coff=1

http://scholar.google.com/scholar?as_q=OsVPS9A functions cooperatively with OsRAB5A to regulate post-Golgi dense vesicle-mediated storage protein trafficking to protein storage vacuole in rice endosperm cells&num=10&btnG=Search+Scholar&as_epq=&as_oq=&as_eq=&as_occt=any&as_publication=&as_yhi=&as_allsubj=all&hl=en&lr=&c2coff=1

http://scholar.google.com/scholar?as_q=OsVPS9A functions cooperatively with OsRAB5A to regulate post-Golgi dense vesicle-mediated storage protein trafficking to protein storage vacuole in rice endosperm cells&num=10&btnG=Search+Scholar&as_occt=any&as_sauthors=Liu,&as_ylo=2013&as_allsubj=all&hl=en&c2coff=1

with Sec23 control the direction of vesicle traffic. Nature 473: 181-186.Pubmed: Author and TitleCrossRef: Author and TitleGoogle Scholar: Author Only Title Only Author and Title

Lorente-Rodríguez, A., Heidtman, M., and Barlowe, C. (2009). Multicopy suppressor analysis of thermosensitive YIP1 allelesimplicates GOT1 in transport from the ER. J. Cell Sci. 122: 1540-1550.


Marti, L., Fornaciari, S., Renna, L., Stefano, G., and Brandizzi, F. (2010). COPII-mediated traffic in plants. Trends Plant Sci. 15: 522-528.


Matern, H., Yang, X., Andrulis, E., Sternglanz, R., Trepte, H.H., and Gallwitz, D. (2000). A novel Golgi membrane protein is part of aGTPase-binding protein complex involved in vesicle targeting. EMBO J. 19: 4485-4492.


Matsuoka, K., Orci, L., Amherdt, M., Bednarek, S.Y., Hamamoto, S., Schekman, R., and Yeung, T. (1998). COPII-coated vesicleformation reconstituted with purified coat proteins and chemically defined liposomes. Cell 93: 263-275.


Miller, E., Antonny, B., Hamamoto, S., and Schekman, R. (2002). Cargo selection into COPII vesicles is driven by the Sec24psubunit. EMBO J. 21: 6105-6113.


Miller, E.A., Beilharz, T.H., Malkus, P.N., Lee, M.C.S., Hamamoto, S., Orci, L., and Schekman, R. (2003). Multiple cargo binding siteson the COPII subunit Sec24p ensure capture of diverse membrane proteins into transport vesicles. Cell 114: 497-509.


Miller, M.A., and Schekman, R. (2013). COPII - a flexible vesicle formation system. Curr. Opin. Cell Biol. 25: 420-427.Pubmed: Author and TitleCrossRef: Author and TitleGoogle Scholar: Author Only Title Only Author and Title

Miller, E.A., and Barlowe, C. (2010). Regulation of coat assembly—sorting things out at the ER. Curr. Opin. Cell Biol. 22: 447-453.Pubmed: Author and TitleCrossRef: Author and TitleGoogle Scholar: Author Only Title Only Author and Title

Ren, Y., Wang, Y., Liu, F., Zhou, K., Ding, Y., Zhou, F., Wang, Y., Liu, K., Gan, L., Ma, W., Han, X., Zhang, X., Guo, X., Wu, F., Cheng,Z., Wang, J., Lei, C., Lin, Q., Jiang, L., Wu, C., Bao, Y., Wang, H., and Wan, J. (2014). GLUTELIN PRECURSOR ACCUMULATION3encodes a regulator of post-Golgi vesicular traffic essential for vacuolar protein sorting in rice endosperm. Plant Cell 26: 410-425.


Saint-Jore, C.M., Evins, J., Batoko, H., Brandizzi, F., Moore, I., and Hawes, C. (2002). Redistribution of membrane proteins betweenthe Golgi apparatus and endoplasmic reticulum in plants is reversible and not dependent on cytoskeletal networks. Plant J. 29:661-678.


Saint-Jore-Dupas, C., Nebenführ, A., Boulaflous, A., Follet-Gueye, M.L., Plasson, C., Hawes, C., Driouich, A., Faye, L., and Gomord,V. (2006). Plant N-glycan processing enzymes employ different targeting mechanisms for their spatial arrangement along thesecretory pathway. Plant Cell 18: 3182-3200.


Sieben, C., Mikosch, M., Brandizzi, F., and Homann, U. (2008). Interaction of the K(+)-channel KAT1 with the coat protein complex IIcoat component Sec24 depends on a di-acidic endoplasmic reticulum export motif. Plant J. 56: 997-1006.


Stagg, S.M., Gurkan, C., Fowler, D.M., LaPointe, P., Foss, T.R., Potter, C.S., Carragher, B., and Balch, W.E. (2006). Structure of theSec13/31 COPII coat cage. Nature 439: 234-238.

http://www.ncbi.nlm.nih.gov/pubmed?term=Lord%2C C%2E%2C Bhandari%2C D%2E%2C Menon%2C S%2E%2C Ghassemian%2C M%2E%2C Nycz%2C D%2E%2C Hay%2C J%2E%2C Ghosh%2C P%2E%2C Ferro%2DNovick%2C S%2E %282011%29%2E Sequential interactions with Sec23 control the direction of vesicle traffic%2E Nature 473%3A 181%2D186%2E&dopt=abstract

http://search.crossref.org/?page=1&rows=2&q=Lord, C., Bhandari, D., Menon, S., Ghassemian, M., Nycz, D., Hay, J., Ghosh, P., Ferro-Novick, S. (2011). Sequential interactions with Sec23 control the direction of vesicle traffic. Nature 473: 181-186.

http://scholar.google.com/scholar?as_q=&num=10&as_occt=any&as_sauthors=Lord,&hl=en&c2coff=1

http://scholar.google.com/scholar?as_q=Sequential interactions with Sec23 control the direction of vesicle traffic&num=10&btnG=Search+Scholar&as_epq=&as_oq=&as_eq=&as_occt=any&as_publication=&as_yhi=&as_allsubj=all&hl=en&lr=&c2coff=1

http://scholar.google.com/scholar?as_q=Sequential interactions with Sec23 control the direction of vesicle traffic&num=10&btnG=Search+Scholar&as_occt=any&as_sauthors=Lord,&as_ylo=2011&as_allsubj=all&hl=en&c2coff=1

http://www.ncbi.nlm.nih.gov/pubmed?term=Lorente%2DRodr�guez%2C A%2E%2C Heidtman%2C M%2E%2C and Barlowe%2C C%2E %282009%29%2E Multicopy suppressor analysis of thermosensitive YIP1 alleles implicates GOT1 in transport from the ER%2E J%2E Cell Sci%2E 122%3A 1540%2D1550%2E&dopt=abstract

http://search.crossref.org/?page=1&rows=2&q=Lorente-Rodr�guez, A., Heidtman, M., and Barlowe, C. (2009). Multicopy suppressor analysis of thermosensitive YIP1 alleles implicates GOT1 in transport from the ER. J. Cell Sci. 122: 1540-1550.

http://scholar.google.com/scholar?as_q=&num=10&as_occt=any&as_sauthors=Lorente-Rodr�guez,&hl=en&c2coff=1

http://scholar.google.com/scholar?as_q=Multicopy suppressor analysis of thermosensitive YIP1 alleles implicates GOT1 in transport from the ER&num=10&btnG=Search+Scholar&as_epq=&as_oq=&as_eq=&as_occt=any&as_publication=&as_yhi=&as_allsubj=all&hl=en&lr=&c2coff=1

http://scholar.google.com/scholar?as_q=Multicopy suppressor analysis of thermosensitive YIP1 alleles implicates GOT1 in transport from the ER&num=10&btnG=Search+Scholar&as_occt=any&as_sauthors=Lorente-Rodr�guez,&as_ylo=2009&as_allsubj=all&hl=en&c2coff=1

http://www.ncbi.nlm.nih.gov/pubmed?term=Marti%2C L%2E%2C Fornaciari%2C S%2E%2C Renna%2C L%2E%2C Stefano%2C G%2E%2C and Brandizzi%2C F%2E %282010%29%2E COPII%2Dmediated traffic in plants%2E Trends Plant Sci%2E 15%3A 522%2D528%2E&dopt=abstract

http://search.crossref.org/?page=1&rows=2&q=Marti, L., Fornaciari, S., Renna, L., Stefano, G., and Brandizzi, F. (2010). COPII-mediated traffic in plants. Trends Plant Sci. 15: 522-528.

http://scholar.google.com/scholar?as_q=&num=10&as_occt=any&as_sauthors=Marti,&hl=en&c2coff=1

http://scholar.google.com/scholar?as_q=COPII-mediated traffic in plants&num=10&btnG=Search+Scholar&as_epq=&as_oq=&as_eq=&as_occt=any&as_publication=&as_yhi=&as_allsubj=all&hl=en&lr=&c2coff=1

http://scholar.google.com/scholar?as_q=COPII-mediated traffic in plants&num=10&btnG=Search+Scholar&as_occt=any&as_sauthors=Marti,&as_ylo=2010&as_allsubj=all&hl=en&c2coff=1

http://www.ncbi.nlm.nih.gov/pubmed?term=Matern%2C H%2E%2C Yang%2C X%2E%2C Andrulis%2C E%2E%2C Sternglanz%2C R%2E%2C Trepte%2C H%2EH%2E%2C and Gallwitz%2C D%2E %282000%29%2E A novel Golgi membrane protein is part of a GTPase%2Dbinding protein complex involved in vesicle targeting%2E EMBO J%2E 19%3A 4485%2D4492%2E&dopt=abstract

http://search.crossref.org/?page=1&rows=2&q=Matern, H., Yang, X., Andrulis, E., Sternglanz, R., Trepte, H.H., and Gallwitz, D. (2000). A novel Golgi membrane protein is part of a GTPase-binding protein complex involved in vesicle targeting. EMBO J. 19: 4485-4492.

http://scholar.google.com/scholar?as_q=&num=10&as_occt=any&as_sauthors=Matern,&hl=en&c2coff=1

http://scholar.google.com/scholar?as_q=A novel Golgi membrane protein is part of a GTPase-binding protein complex involved in vesicle targeting&num=10&btnG=Search+Scholar&as_epq=&as_oq=&as_eq=&as_occt=any&as_publication=&as_yhi=&as_allsubj=all&hl=en&lr=&c2coff=1

http://scholar.google.com/scholar?as_q=A novel Golgi membrane protein is part of a GTPase-binding protein complex involved in vesicle targeting&num=10&btnG=Search+Scholar&as_occt=any&as_sauthors=Matern,&as_ylo=2000&as_allsubj=all&hl=en&c2coff=1

http://www.ncbi.nlm.nih.gov/pubmed?term=Matsuoka%2C K%2E%2C Orci%2C L%2E%2C Amherdt%2C M%2E%2C Bednarek%2C S%2EY%2E%2C Hamamoto%2C S%2E%2C Schekman%2C R%2E%2C and Yeung%2C T%2E %281998%29%2E COPII%2Dcoated vesicle formation reconstituted with purified coat proteins and chemically defined liposomes%2E Cell 93%3A 263%2D275%2E&dopt=abstract

http://search.crossref.org/?page=1&rows=2&q=Matsuoka, K., Orci, L., Amherdt, M., Bednarek, S.Y., Hamamoto, S., Schekman, R., and Yeung, T. (1998). COPII-coated vesicle formation reconstituted with purified coat proteins and chemically defined liposomes. Cell 93: 263-275.

http://scholar.google.com/scholar?as_q=&num=10&as_occt=any&as_sauthors=Matsuoka,&hl=en&c2coff=1

http://scholar.google.com/scholar?as_q=COPII-coated vesicle formation reconstituted with purified coat proteins and chemically defined liposomes&num=10&btnG=Search+Scholar&as_epq=&as_oq=&as_eq=&as_occt=any&as_publication=&as_yhi=&as_allsubj=all&hl=en&lr=&c2coff=1

http://scholar.google.com/scholar?as_q=COPII-coated vesicle formation reconstituted with purified coat proteins and chemically defined liposomes&num=10&btnG=Search+Scholar&as_occt=any&as_sauthors=Matsuoka,&as_ylo=1998&as_allsubj=all&hl=en&c2coff=1

http://www.ncbi.nlm.nih.gov/pubmed?term=Miller%2C E%2E%2C Antonny%2C B%2E%2C Hamamoto%2C S%2E%2C and Schekman%2C R%2E %282002%29%2E Cargo selection into COPII vesicles is driven by the Sec24p subunit%2E EMBO J%2E 21%3A 6105%2D6113%2E&dopt=abstract

http://search.crossref.org/?page=1&rows=2&q=Miller, E., Antonny, B., Hamamoto, S., and Schekman, R. (2002). Cargo selection into COPII vesicles is driven by the Sec24p subunit. EMBO J. 21: 6105-6113.

http://scholar.google.com/scholar?as_q=&num=10&as_occt=any&as_sauthors=Miller,&hl=en&c2coff=1

http://scholar.google.com/scholar?as_q=Cargo selection into COPII vesicles is driven by the Sec24p subunit&num=10&btnG=Search+Scholar&as_epq=&as_oq=&as_eq=&as_occt=any&as_publication=&as_yhi=&as_allsubj=all&hl=en&lr=&c2coff=1

http://scholar.google.com/scholar?as_q=Cargo selection into COPII vesicles is driven by the Sec24p subunit&num=10&btnG=Search+Scholar&as_occt=any&as_sauthors=Miller,&as_ylo=2002&as_allsubj=all&hl=en&c2coff=1

http://www.ncbi.nlm.nih.gov/pubmed?term=Miller%2C E%2EA%2E%2C Beilharz%2C T%2EH%2E%2C Malkus%2C P%2EN%2E%2C Lee%2C M%2EC%2ES%2E%2C Hamamoto%2C S%2E%2C Orci%2C L%2E%2C and Schekman%2C R%2E %282003%29%2E Multiple cargo binding sites on the COPII subunit Sec24p ensure capture of diverse membrane proteins into transport vesicles%2E Cell 114%3A 497%2D509%2E&dopt=abstract

http://search.crossref.org/?page=1&rows=2&q=Miller, E.A., Beilharz, T.H., Malkus, P.N., Lee, M.C.S., Hamamoto, S., Orci, L., and Schekman, R. (2003). Multiple cargo binding sites on the COPII subunit Sec24p ensure capture of diverse membrane proteins into transport vesicles. Cell 114: 497-509.


http://scholar.google.com/scholar?as_q=Multiple cargo binding sites on the COPII subunit Sec24p ensure capture of diverse membrane proteins into transport vesicles&num=10&btnG=Search+Scholar&as_epq=&as_oq=&as_eq=&as_occt=any&as_publication=&as_yhi=&as_allsubj=all&hl=en&lr=&c2coff=1

http://scholar.google.com/scholar?as_q=Multiple cargo binding sites on the COPII subunit Sec24p ensure capture of diverse membrane proteins into transport vesicles&num=10&btnG=Search+Scholar&as_occt=any&as_sauthors=Miller,&as_ylo=2003&as_allsubj=all&hl=en&c2coff=1

http://www.ncbi.nlm.nih.gov/pubmed?term=Miller%2C M%2EA%2E%2C and Schekman%2C R%2E %282013%29%2E COPII %2D a flexible vesicle formation system%2E Curr%2E Opin%2E Cell Biol%2E 25%3A 420%2D427%2E&dopt=abstract

http://search.crossref.org/?page=1&rows=2&q=Miller, M.A., and Schekman, R. (2013). COPII - a flexible vesicle formation system. Curr. Opin. Cell Biol. 25: 420-427.


http://scholar.google.com/scholar?as_q=COPII - a flexible vesicle formation system&num=10&btnG=Search+Scholar&as_epq=&as_oq=&as_eq=&as_occt=any&as_publication=&as_yhi=&as_allsubj=all&hl=en&lr=&c2coff=1

http://scholar.google.com/scholar?as_q=COPII - a flexible vesicle formation system&num=10&btnG=Search+Scholar&as_occt=any&as_sauthors=Miller,&as_ylo=2013&as_allsubj=all&hl=en&c2coff=1

http://www.ncbi.nlm.nih.gov/pubmed?term=Miller%2C E%2EA%2E%2C and Barlowe%2C C%2E %282010%29%2E Regulation of coat assembly?sorting things out at the ER%2E Curr%2E Opin%2E Cell Biol%2E 22%3A 447%2D453%2E&dopt=abstract

http://search.crossref.org/?page=1&rows=2&q=Miller, E.A., and Barlowe, C. (2010). Regulation of coat assembly?sorting things out at the ER. Curr. Opin. Cell Biol. 22: 447-453.


http://scholar.google.com/scholar?as_q=Regulation of coat assembly?sorting things out at the ER&num=10&btnG=Search+Scholar&as_epq=&as_oq=&as_eq=&as_occt=any&as_publication=&as_yhi=&as_allsubj=all&hl=en&lr=&c2coff=1

http://scholar.google.com/scholar?as_q=Regulation of coat assembly?sorting things out at the ER&num=10&btnG=Search+Scholar&as_occt=any&as_sauthors=Miller,&as_ylo=2010&as_allsubj=all&hl=en&c2coff=1

http://www.ncbi.nlm.nih.gov/pubmed?term=Ren%2C Y%2E%2C Wang%2C Y%2E%2C Liu%2C F%2E%2C Zhou%2C K%2E%2C Ding%2C Y%2E%2C Zhou%2C F%2E%2C Wang%2C Y%2E%2C Liu%2C K%2E%2C Gan%2C L%2E%2C Ma%2C W%2E%2C Han%2C X%2E%2C Zhang%2C X%2E%2C Guo%2C X%2E%2C Wu%2C F%2E%2C Cheng%2C Z%2E%2C Wang%2C J%2E%2C Lei%2C C%2E%2C Lin%2C Q%2E%2C Jiang%2C L%2E%2C Wu%2C C%2E%2C Bao%2C Y%2E%2C Wang%2C H%2E%2C and Wan%2C J%2E %282014%29%2E GLUTELIN PRECURSOR ACCUMULATION3 encodes a regulator of post%2DGolgi vesicular traffic essential for vacuolar protein sorting in rice endosperm%2E Plant Cell 26%3A 410%2D425%2E&dopt=abstract

http://search.crossref.org/?page=1&rows=2&q=Ren, Y., Wang, Y., Liu, F., Zhou, K., Ding, Y., Zhou, F., Wang, Y., Liu, K., Gan, L., Ma, W., Han, X., Zhang, X., Guo, X., Wu, F., Cheng, Z., Wang, J., Lei, C., Lin, Q., Jiang, L., Wu, C., Bao, Y., Wang, H., and Wan, J. (2014). GLUTELIN PRECURSOR ACCUMULATION3 encodes a regulator of post-Golgi vesicular traffic essential for vacuolar protein sorting in rice endosperm. Plant Cell 26: 410-425.

http://scholar.google.com/scholar?as_q=&num=10&as_occt=any&as_sauthors=Ren,&hl=en&c2coff=1

http://scholar.google.com/scholar?as_q=GLUTELIN PRECURSOR ACCUMULATION3 encodes a regulator of post-Golgi vesicular traffic essential for vacuolar protein sorting in rice endosperm&num=10&btnG=Search+Scholar&as_epq=&as_oq=&as_eq=&as_occt=any&as_publication=&as_yhi=&as_allsubj=all&hl=en&lr=&c2coff=1

http://scholar.google.com/scholar?as_q=GLUTELIN PRECURSOR ACCUMULATION3 encodes a regulator of post-Golgi vesicular traffic essential for vacuolar protein sorting in rice endosperm&num=10&btnG=Search+Scholar&as_occt=any&as_sauthors=Ren,&as_ylo=2014&as_allsubj=all&hl=en&c2coff=1

http://www.ncbi.nlm.nih.gov/pubmed?term=Saint%2DJore%2C C%2EM%2E%2C Evins%2C J%2E%2C Batoko%2C H%2E%2C Brandizzi%2C F%2E%2C Moore%2C I%2E%2C and Hawes%2C C%2E %282002%29%2E Redistribution of membrane proteins between the Golgi apparatus and endoplasmic reticulum in plants is reversible and not dependent on cytoskeletal networks%2E Plant J%2E 29%3A 661%2D678%2E&dopt=abstract

http://search.crossref.org/?page=1&rows=2&q=Saint-Jore, C.M., Evins, J., Batoko, H., Brandizzi, F., Moore, I., and Hawes, C. (2002). Redistribution of membrane proteins between the Golgi apparatus and endoplasmic reticulum in plants is reversible and not dependent on cytoskeletal networks. Plant J. 29: 661-678.

http://scholar.google.com/scholar?as_q=&num=10&as_occt=any&as_sauthors=Saint-Jore,&hl=en&c2coff=1

http://scholar.google.com/scholar?as_q=Redistribution of membrane proteins between the Golgi apparatus and endoplasmic reticulum in plants is reversible and not dependent on cytoskeletal networks&num=10&btnG=Search+Scholar&as_epq=&as_oq=&as_eq=&as_occt=any&as_publication=&as_yhi=&as_allsubj=all&hl=en&lr=&c2coff=1

http://scholar.google.com/scholar?as_q=Redistribution of membrane proteins between the Golgi apparatus and endoplasmic reticulum in plants is reversible and not dependent on cytoskeletal networks&num=10&btnG=Search+Scholar&as_occt=any&as_sauthors=Saint-Jore,&as_ylo=2002&as_allsubj=all&hl=en&c2coff=1

http://www.ncbi.nlm.nih.gov/pubmed?term=Saint%2DJore%2DDupas%2C C%2E%2C Nebenf�hr%2C A%2E%2C Boulaflous%2C A%2E%2C Follet%2DGueye%2C M%2EL%2E%2C Plasson%2C C%2E%2C Hawes%2C C%2E%2C Driouich%2C A%2E%2C Faye%2C L%2E%2C and Gomord%2C V%2E %282006%29%2E Plant N%2Dglycan processing enzymes employ different targeting mechanisms for their spatial arrangement along the secretory pathway%2E Plant Cell 18%3A 3182%2D3200%2E&dopt=abstract

http://search.crossref.org/?page=1&rows=2&q=Saint-Jore-Dupas, C., Nebenf�hr, A., Boulaflous, A., Follet-Gueye, M.L., Plasson, C., Hawes, C., Driouich, A., Faye, L., and Gomord, V. (2006). Plant N-glycan processing enzymes employ different targeting mechanisms for their spatial arrangement along the secretory pathway. Plant Cell 18: 3182-3200.

http://scholar.google.com/scholar?as_q=&num=10&as_occt=any&as_sauthors=Saint-Jore-Dupas,&hl=en&c2coff=1

http://scholar.google.com/scholar?as_q=Plant N-glycan processing enzymes employ different targeting mechanisms for their spatial arrangement along the secretory pathway&num=10&btnG=Search+Scholar&as_epq=&as_oq=&as_eq=&as_occt=any&as_publication=&as_yhi=&as_allsubj=all&hl=en&lr=&c2coff=1

http://scholar.google.com/scholar?as_q=Plant N-glycan processing enzymes employ different targeting mechanisms for their spatial arrangement along the secretory pathway&num=10&btnG=Search+Scholar&as_occt=any&as_sauthors=Saint-Jore-Dupas,&as_ylo=2006&as_allsubj=all&hl=en&c2coff=1

http://www.ncbi.nlm.nih.gov/pubmed?term=Sieben%2C C%2E%2C Mikosch%2C M%2E%2C Brandizzi%2C F%2E%2C and Homann%2C U%2E %282008%29%2E Interaction of the K%28%2B%29%2Dchannel KAT1 with the coat protein complex II coat component Sec24 depends on a di%2Dacidic endoplasmic reticulum export motif%2E Plant J%2E 56%3A 997%2D1006%2E&dopt=abstract

http://search.crossref.org/?page=1&rows=2&q=Sieben, C., Mikosch, M., Brandizzi, F., and Homann, U. (2008). Interaction of the K(+)-channel KAT1 with the coat protein complex II coat component Sec24 depends on a di-acidic endoplasmic reticulum export motif. Plant J. 56: 997-1006.

http://scholar.google.com/scholar?as_q=&num=10&as_occt=any&as_sauthors=Sieben,&hl=en&c2coff=1

http://scholar.google.com/scholar?as_q=Interaction of the K(+)-channel KAT1 with the coat protein complex II coat component Sec24 depends on a di-acidic endoplasmic reticulum export motif&num=10&btnG=Search+Scholar&as_epq=&as_oq=&as_eq=&as_occt=any&as_publication=&as_yhi=&as_allsubj=all&hl=en&lr=&c2coff=1

http://scholar.google.com/scholar?as_q=Interaction of the K(+)-channel KAT1 with the coat protein complex II coat component Sec24 depends on a di-acidic endoplasmic reticulum export motif&num=10&btnG=Search+Scholar&as_occt=any&as_sauthors=Sieben,&as_ylo=2008&as_allsubj=all&hl=en&c2coff=1


Stefano, G., Renna, L., Chatre, L., Hanton, S.L., Moreau, P., Hawes, C., and Brandizzi, F. (2006). In tobacco leaf epidermal cells, theintegrity of protein export from the endoplasmic reticulumand of ER export sites depends on active COPI machinery. Plant J. 46:95-110.


Takagi, J., Renna, L., Takahashi, H., Koumoto, Y., Tamura, K., Stefano, G., Fukao, Y., Kondo, M., Nishimura, M., Shimada, T.,Brandizzi, F., and Hara-Nishimura, I. (2013). MAIGO5 functions in protein export from Golgi-associated Endoplasmic Reticulum Exitsites in Arabidopsis. Plant Cell 25: 4658-4675.


Takahashi, H., Rai, M., Kitagawa, T., Morita, S., Masumura, T., and Tanaka, K. (2004). Differential localization of tonoplast intrinsicproteins on the membrane of protein body type II and aleurone grain in rice seeds. Biosci. Biotechnol. Biochem. 68: 1728-1736.


Takahashi, H., Saito, Y., Kitagawa, T., Morita, S., Masumura, T., and Tanaka, K. (2005). A novel vesicle derived directly fromendoplasmic reticulum is involved in the transport of vacuolar storage proteins in rice endosperm. Plant Cell Physiol. 46: 245-249.


Takahashi, H., Tamura, K., Takagi, J., Koumoto, Y., Hara-Nishimura, I., and Shimada, T. (2010). MAG4/Atp115 is a Golgi-localizedtethering factor that mediates efficient anterograde transport in Arabidopsis. Plant Cell Physiol. 51: 1777-1787.


Takemoto. Y., Coughlan, S,J., Okita, T.W., Satoh, H., Ogawa, M., and Kumamaru, T. (2002). The rice mutant esp2 greatlyaccumulates the glutelin precursor and deletes the protein disulfide isomerase. Plant Physiol. 128: 1212-1222.


Takeuchi, M., Ueda, T., Sato, K., Abe, H., Nagata, T., and Nakano A. (2000). A dominant negative mutant of Sar1 GTPase inhibitsprotein transport from the endoplasmic reticulum to the Golgi apparatus in tobacco and Arabidopsis cultured cells. Plant J. 23: 517-525


Tamura, K., Shimada, T., Kondo, M., Nishimura, M., and Hara-Nishimura, I. (2005). KATAMARI1/MURUS3 is a novel Golgi membraneprotein that is required for endomembrane organization in Arabidopsis. Plant Cell 17: 1764-1776.


Tan, X., Cao, K., Liu, F., Li, Y., Li, P., Gao, C., Ding, Y., Lan, Z., Shi, Z., Rui, Q., Feng, Y., Liu, Y., Zhao, Y., Wu, C., Zhang, Q., Li, Y.,Jiang, L., and Bao, Y. (2016). Arabidopsis COG complex subunits COG3 and COG8 modulate Golgi morphology, vesicle traffickinghomeostasis and are essential for pollen tube growth. PLoS Genet. 12(7): e1006140. doi:10.1371/journal.pgen.1006140


Tanaka, K., Sugimoto, T., Ogawa, M., and Kasai, Z. (1980). Isolation and characterization of 2-types of protein bodies in the riceendosperm. Agric. Biol. Chem. 44: 1633-1639.


Tanaka, Y., Nishimura, K., Kawamukai, M., Oshima, A., and Nakagawa, T. (2013) Redundant function of two Arabidopsis COPIIcomponents, AtSec24B and At-Sec24C, is essential for male and female gametogenesis. Planta 238: 561-575.


Tian, L., Dai, L.L., Yin, Z.J., Fukuda, M., Kumamaru, T., Dong, X.B., Xu, X.P., and Qu, L.Q. (2013). Small GTPase Sar1 is crucial forproglutelin and a-globulin export from the endoplasmic reticulum in rice endosperm. J. Exp. Bot. 64: 2831-2845.


http://www.ncbi.nlm.nih.gov/pubmed?term=Stagg%2C S%2EM%2E%2C Gurkan%2C C%2E%2C Fowler%2C D%2EM%2E%2C LaPointe%2C P%2E%2C Foss%2C T%2ER%2E%2C Potter%2C C%2ES%2E%2C Carragher%2C B%2E%2C and Balch%2C W%2EE%2E %282006%29%2E Structure of the Sec13%2F31 COPII coat cage%2E Nature 439%3A 234%2D238%2E&dopt=abstract

http://search.crossref.org/?page=1&rows=2&q=Stagg, S.M., Gurkan, C., Fowler, D.M., LaPointe, P., Foss, T.R., Potter, C.S., Carragher, B., and Balch, W.E. (2006). Structure of the Sec13/31 COPII coat cage. Nature 439: 234-238.

http://scholar.google.com/scholar?as_q=&num=10&as_occt=any&as_sauthors=Stagg,&hl=en&c2coff=1

http://scholar.google.com/scholar?as_q=Structure of the Sec13/31 COPII coat cage&num=10&btnG=Search+Scholar&as_epq=&as_oq=&as_eq=&as_occt=any&as_publication=&as_yhi=&as_allsubj=all&hl=en&lr=&c2coff=1

http://scholar.google.com/scholar?as_q=Structure of the Sec13/31 COPII coat cage&num=10&btnG=Search+Scholar&as_occt=any&as_sauthors=Stagg,&as_ylo=2006&as_allsubj=all&hl=en&c2coff=1

http://www.ncbi.nlm.nih.gov/pubmed?term=Stefano%2C G%2E%2C Renna%2C L%2E%2C Chatre%2C L%2E%2C Hanton%2C S%2EL%2E%2C Moreau%2C P%2E%2C Hawes%2C C%2E%2C and Brandizzi%2C F%2E %282006%29%2E In tobacco leaf epidermal cells%2C the integrity of protein export from the endoplasmic reticulumand of ER export sites depends on active COPI machinery%2E Plant J%2E 46%3A 95%2D110%2E&dopt=abstract

http://search.crossref.org/?page=1&rows=2&q=Stefano, G., Renna, L., Chatre, L., Hanton, S.L., Moreau, P., Hawes, C., and Brandizzi, F. (2006). In tobacco leaf epidermal cells, the integrity of protein export from the endoplasmic reticulumand of ER export sites depends on active COPI machinery. Plant J. 46: 95-110.

http://scholar.google.com/scholar?as_q=&num=10&as_occt=any&as_sauthors=Stefano,&hl=en&c2coff=1

http://scholar.google.com/scholar?as_q=In tobacco leaf epidermal cells, the integrity of protein export from the endoplasmic reticulumand of ER export sites depends on active COPI machinery&num=10&btnG=Search+Scholar&as_epq=&as_oq=&as_eq=&as_occt=any&as_publication=&as_yhi=&as_allsubj=all&hl=en&lr=&c2coff=1

http://scholar.google.com/scholar?as_q=In tobacco leaf epidermal cells, the integrity of protein export from the endoplasmic reticulumand of ER export sites depends on active COPI machinery&num=10&btnG=Search+Scholar&as_occt=any&as_sauthors=Stefano,&as_ylo=2006&as_allsubj=all&hl=en&c2coff=1

http://www.ncbi.nlm.nih.gov/pubmed?term=Takagi%2C J%2E%2C Renna%2C L%2E%2C Takahashi%2C H%2E%2C Koumoto%2C Y%2E%2C Tamura%2C K%2E%2C Stefano%2C G%2E%2C Fukao%2C Y%2E%2C Kondo%2C M%2E%2C Nishimura%2C M%2E%2C Shimada%2C T%2E%2C Brandizzi%2C F%2E%2C and Hara%2DNishimura%2C I%2E %282013%29%2E MAIGO5 functions in protein export from Golgi%2Dassociated Endoplasmic Reticulum Exit sites in Arabidopsis%2E Plant Cell 25%3A 4658%2D4675%2E&dopt=abstract

http://search.crossref.org/?page=1&rows=2&q=Takagi, J., Renna, L., Takahashi, H., Koumoto, Y., Tamura, K., Stefano, G., Fukao, Y., Kondo, M., Nishimura, M., Shimada, T., Brandizzi, F., and Hara-Nishimura, I. (2013). MAIGO5 functions in protein export from Golgi-associated Endoplasmic Reticulum Exit sites in Arabidopsis. Plant Cell 25: 4658-4675.

http://scholar.google.com/scholar?as_q=&num=10&as_occt=any&as_sauthors=Takagi,&hl=en&c2coff=1

http://scholar.google.com/scholar?as_q=MAIGO5 functions in protein export from Golgi-associated Endoplasmic Reticulum Exit sites in Arabidopsis&num=10&btnG=Search+Scholar&as_epq=&as_oq=&as_eq=&as_occt=any&as_publication=&as_yhi=&as_allsubj=all&hl=en&lr=&c2coff=1

http://scholar.google.com/scholar?as_q=MAIGO5 functions in protein export from Golgi-associated Endoplasmic Reticulum Exit sites in Arabidopsis&num=10&btnG=Search+Scholar&as_occt=any&as_sauthors=Takagi,&as_ylo=2013&as_allsubj=all&hl=en&c2coff=1

http://www.ncbi.nlm.nih.gov/pubmed?term=Takahashi%2C H%2E%2C Rai%2C M%2E%2C Kitagawa%2C T%2E%2C Morita%2C S%2E%2C Masumura%2C T%2E%2C and Tanaka%2C K%2E %282004%29%2E Differential localization of tonoplast intrinsic proteins on the membrane of protein body type II and aleurone grain in rice seeds%2E Biosci%2E Biotechnol%2E Biochem%2E 68%3A 1728%2D1736%2E&dopt=abstract

http://search.crossref.org/?page=1&rows=2&q=Takahashi, H., Rai, M., Kitagawa, T., Morita, S., Masumura, T., and Tanaka, K. (2004). Differential localization of tonoplast intrinsic proteins on the membrane of protein body type II and aleurone grain in rice seeds. Biosci. Biotechnol. Biochem. 68: 1728-1736.

http://scholar.google.com/scholar?as_q=&num=10&as_occt=any&as_sauthors=Takahashi,&hl=en&c2coff=1

http://scholar.google.com/scholar?as_q=Differential localization of tonoplast intrinsic proteins on the membrane of protein body type II and aleurone grain in rice seeds&num=10&btnG=Search+Scholar&as_epq=&as_oq=&as_eq=&as_occt=any&as_publication=&as_yhi=&as_allsubj=all&hl=en&lr=&c2coff=1

http://scholar.google.com/scholar?as_q=Differential localization of tonoplast intrinsic proteins on the membrane of protein body type II and aleurone grain in rice seeds&num=10&btnG=Search+Scholar&as_occt=any&as_sauthors=Takahashi,&as_ylo=2004&as_allsubj=all&hl=en&c2coff=1

http://www.ncbi.nlm.nih.gov/pubmed?term=Takahashi%2C H%2E%2C Saito%2C Y%2E%2C Kitagawa%2C T%2E%2C Morita%2C S%2E%2C Masumura%2C T%2E%2C and Tanaka%2C K%2E %282005%29%2E A novel vesicle derived directly from endoplasmic reticulum is involved in the transport of vacuolar storage proteins in rice endosperm%2E Plant Cell Physiol%2E 46%3A 245%2D249%2E&dopt=abstract

http://search.crossref.org/?page=1&rows=2&q=Takahashi, H., Saito, Y., Kitagawa, T., Morita, S., Masumura, T., and Tanaka, K. (2005). A novel vesicle derived directly from endoplasmic reticulum is involved in the transport of vacuolar storage proteins in rice endosperm. Plant Cell Physiol. 46: 245-249.


http://scholar.google.com/scholar?as_q=A novel vesicle derived directly from endoplasmic reticulum is involved in the transport of vacuolar storage proteins in rice endosperm&num=10&btnG=Search+Scholar&as_epq=&as_oq=&as_eq=&as_occt=any&as_publication=&as_yhi=&as_allsubj=all&hl=en&lr=&c2coff=1

http://scholar.google.com/scholar?as_q=A novel vesicle derived directly from endoplasmic reticulum is involved in the transport of vacuolar storage proteins in rice endosperm&num=10&btnG=Search+Scholar&as_occt=any&as_sauthors=Takahashi,&as_ylo=2005&as_allsubj=all&hl=en&c2coff=1

http://www.ncbi.nlm.nih.gov/pubmed?term=Takahashi%2C H%2E%2C Tamura%2C K%2E%2C Takagi%2C J%2E%2C Koumoto%2C Y%2E%2C Hara%2DNishimura%2C I%2E%2C and Shimada%2C T%2E %282010%29%2E MAG4%2FAtp115 is a Golgi%2Dlocalized tethering factor that mediates efficient anterograde transport in Arabidopsis%2E Plant Cell Physiol%2E 51%3A 1777%2D1787%2E&dopt=abstract

http://search.crossref.org/?page=1&rows=2&q=Takahashi, H., Tamura, K., Takagi, J., Koumoto, Y., Hara-Nishimura, I., and Shimada, T. (2010). MAG4/Atp115 is a Golgi-localized tethering factor that mediates efficient anterograde transport in Arabidopsis. Plant Cell Physiol. 51: 1777-1787.


http://scholar.google.com/scholar?as_q=MAG4/Atp115 is a Golgi-localized tethering factor that mediates efficient anterograde transport in Arabidopsis&num=10&btnG=Search+Scholar&as_epq=&as_oq=&as_eq=&as_occt=any&as_publication=&as_yhi=&as_allsubj=all&hl=en&lr=&c2coff=1

http://scholar.google.com/scholar?as_q=MAG4/Atp115 is a Golgi-localized tethering factor that mediates efficient anterograde transport in Arabidopsis&num=10&btnG=Search+Scholar&as_occt=any&as_sauthors=Takahashi,&as_ylo=2010&as_allsubj=all&hl=en&c2coff=1

http://www.ncbi.nlm.nih.gov/pubmed?term=Takemoto%2E Y%2E%2C Coughlan%2C S%2CJ%2E%2C Okita%2C T%2EW%2E%2C Satoh%2C H%2E%2C Ogawa%2C M%2E%2C and Kumamaru%2C T%2E %282002%29%2E The rice mutant esp2 greatly accumulates the glutelin precursor and deletes the protein disulfide isomerase%2E Plant Physiol%2E 128%3A 1212%2D1222%2E&dopt=abstract

http://search.crossref.org/?page=1&rows=2&q=Takemoto. Y., Coughlan, S,J., Okita, T.W., Satoh, H., Ogawa, M., and Kumamaru, T. (2002). The rice mutant esp2 greatly accumulates the glutelin precursor and deletes the protein disulfide isomerase. Plant Physiol. 128: 1212-1222.

http://scholar.google.com/scholar?as_q=&num=10&as_occt=any&as_sauthors=Takemoto.&hl=en&c2coff=1

http://scholar.google.com/scholar?as_q=The rice mutant esp2 greatly accumulates the glutelin precursor and deletes the protein disulfide isomerase&num=10&btnG=Search+Scholar&as_epq=&as_oq=&as_eq=&as_occt=any&as_publication=&as_yhi=&as_allsubj=all&hl=en&lr=&c2coff=1

http://scholar.google.com/scholar?as_q=The rice mutant esp2 greatly accumulates the glutelin precursor and deletes the protein disulfide isomerase&num=10&btnG=Search+Scholar&as_occt=any&as_sauthors=Takemoto.&as_ylo=2002&as_allsubj=all&hl=en&c2coff=1

http://www.ncbi.nlm.nih.gov/pubmed?term=Takeuchi%2C M%2E%2C Ueda%2C T%2E%2C Sato%2C K%2E%2C Abe%2C H%2E%2C Nagata%2C T%2E%2C and Nakano A%2E %282000%29%2E A dominant negative mutant of Sar1 GTPase inhibits protein transport from the endoplasmic reticulum to the Golgi apparatus in tobacco and Arabidopsis cultured cells%2E Plant J%2E 23%3A 517%2D525&dopt=abstract

http://search.crossref.org/?page=1&rows=2&q=Takeuchi, M., Ueda, T., Sato, K., Abe, H., Nagata, T., and Nakano A. (2000). A dominant negative mutant of Sar1 GTPase inhibits protein transport from the endoplasmic reticulum to the Golgi apparatus in tobacco and Arabidopsis cultured cells. Plant J. 23: 517-525

http://scholar.google.com/scholar?as_q=&num=10&as_occt=any&as_sauthors=Takeuchi,&hl=en&c2coff=1

http://scholar.google.com/scholar?as_q=A dominant negative mutant of Sar1 GTPase inhibits protein transport from the endoplasmic reticulum to the Golgi apparatus in tobacco and Arabidopsis cultured cells&num=10&btnG=Search+Scholar&as_epq=&as_oq=&as_eq=&as_occt=any&as_publication=&as_yhi=&as_allsubj=all&hl=en&lr=&c2coff=1

http://scholar.google.com/scholar?as_q=A dominant negative mutant of Sar1 GTPase inhibits protein transport from the endoplasmic reticulum to the Golgi apparatus in tobacco and Arabidopsis cultured cells&num=10&btnG=Search+Scholar&as_occt=any&as_sauthors=Takeuchi,&as_ylo=2000&as_allsubj=all&hl=en&c2coff=1

http://www.ncbi.nlm.nih.gov/pubmed?term=Tamura%2C K%2E%2C Shimada%2C T%2E%2C Kondo%2C M%2E%2C Nishimura%2C M%2E%2C and Hara%2DNishimura%2C I%2E %282005%29%2E KATAMARI1%2FMURUS3 is a novel Golgi membrane protein that is required for endomembrane organization in Arabidopsis%2E Plant Cell 17%3A 1764%2D1776%2E&dopt=abstract

http://search.crossref.org/?page=1&rows=2&q=Tamura, K., Shimada, T., Kondo, M., Nishimura, M., and Hara-Nishimura, I. (2005). KATAMARI1/MURUS3 is a novel Golgi membrane protein that is required for endomembrane organization in Arabidopsis. Plant Cell 17: 1764-1776.

http://scholar.google.com/scholar?as_q=&num=10&as_occt=any&as_sauthors=Tamura,&hl=en&c2coff=1

http://scholar.google.com/scholar?as_q=KATAMARI1/MURUS3 is a novel Golgi membrane protein that is required for endomembrane organization in Arabidopsis&num=10&btnG=Search+Scholar&as_epq=&as_oq=&as_eq=&as_occt=any&as_publication=&as_yhi=&as_allsubj=all&hl=en&lr=&c2coff=1

http://scholar.google.com/scholar?as_q=KATAMARI1/MURUS3 is a novel Golgi membrane protein that is required for endomembrane organization in Arabidopsis&num=10&btnG=Search+Scholar&as_occt=any&as_sauthors=Tamura,&as_ylo=2005&as_allsubj=all&hl=en&c2coff=1

http://www.ncbi.nlm.nih.gov/pubmed?term=Tan%2C X%2E%2C Cao%2C K%2E%2C Liu%2C F%2E%2C Li%2C Y%2E%2C Li%2C P%2E%2C Gao%2C C%2E%2C Ding%2C Y%2E%2C Lan%2C Z%2E%2C Shi%2C Z%2E%2C Rui%2C Q%2E%2C Feng%2C Y%2E%2C Liu%2C Y%2E%2C Zhao%2C Y%2E%2C Wu%2C C%2E%2C Zhang%2C Q%2E%2C Li%2C Y%2E%2C Jiang%2C L%2E%2C and Bao%2C Y%2E %282016%29%2E Arabidopsis COG complex subunits COG3 and COG8 modulate Golgi morphology%2C vesicle trafficking homeostasis and are essential for pollen tube growth%2E PLoS Genet%2E 12%287%29%3A e1006140%2E doi%3A10%2E1371%2Fjournal%2Epgen%2E1006140&dopt=abstract

http://search.crossref.org/?page=1&rows=2&q=Tan, X., Cao, K., Liu, F., Li, Y., Li, P., Gao, C., Ding, Y., Lan, Z., Shi, Z., Rui, Q., Feng, Y., Liu, Y., Zhao, Y., Wu, C., Zhang, Q., Li, Y., Jiang, L., and Bao, Y. (2016). Arabidopsis COG complex subunits COG3 and COG8 modulate Golgi morphology, vesicle trafficking homeostasis and are essential for pollen tube growth. PLoS Genet. 12(7): e1006140. doi:10.1371/journal.pgen.1006140

http://scholar.google.com/scholar?as_q=&num=10&as_occt=any&as_sauthors=Tan,&hl=en&c2coff=1

http://scholar.google.com/scholar?as_q=Arabidopsis COG complex subunits COG3 and COG8 modulate Golgi morphology, vesicle trafficking homeostasis and are essential for pollen tube growth.&num=10&btnG=Search+Scholar&as_epq=&as_oq=&as_eq=&as_occt=any&as_publication=&as_yhi=&as_allsubj=all&hl=en&lr=&c2coff=1

http://scholar.google.com/scholar?as_q=Arabidopsis COG complex subunits COG3 and COG8 modulate Golgi morphology, vesicle trafficking homeostasis and are essential for pollen tube growth.&num=10&btnG=Search+Scholar&as_occt=any&as_sauthors=Tan,&as_ylo=2016&as_allsubj=all&hl=en&c2coff=1

http://www.ncbi.nlm.nih.gov/pubmed?term=Tanaka%2C K%2E%2C Sugimoto%2C T%2E%2C Ogawa%2C M%2E%2C and Kasai%2C Z%2E %281980%29%2E Isolation and characterization of 2%2Dtypes of protein bodies in the rice endosperm%2E Agric%2E Biol%2E Chem%2E 44%3A 1633%2D1639%2E&dopt=abstract

http://search.crossref.org/?page=1&rows=2&q=Tanaka, K., Sugimoto, T., Ogawa, M., and Kasai, Z. (1980). Isolation and characterization of 2-types of protein bodies in the rice endosperm. Agric. Biol. Chem. 44: 1633-1639.

http://scholar.google.com/scholar?as_q=&num=10&as_occt=any&as_sauthors=Tanaka,&hl=en&c2coff=1

http://scholar.google.com/scholar?as_q=Isolation and characterization of 2-types of protein bodies in the rice endosperm&num=10&btnG=Search+Scholar&as_epq=&as_oq=&as_eq=&as_occt=any&as_publication=&as_yhi=&as_allsubj=all&hl=en&lr=&c2coff=1

http://scholar.google.com/scholar?as_q=Isolation and characterization of 2-types of protein bodies in the rice endosperm&num=10&btnG=Search+Scholar&as_occt=any&as_sauthors=Tanaka,&as_ylo=1980&as_allsubj=all&hl=en&c2coff=1

http://www.ncbi.nlm.nih.gov/pubmed?term=Tanaka%2C Y%2E%2C Nishimura%2C K%2E%2C Kawamukai%2C M%2E%2C Oshima%2C A%2E%2C and Nakagawa%2C T%2E %282013%29 Redundant function of two Arabidopsis COPII components%2C AtSec24B and At%2DSec24C%2C is essential for male and female gametogenesis%2E Planta 238%3A 561%2D575%2E&dopt=abstract

http://search.crossref.org/?page=1&rows=2&q=Tanaka, Y., Nishimura, K., Kawamukai, M., Oshima, A., and Nakagawa, T. (2013) Redundant function of two Arabidopsis COPII components, AtSec24B and At-Sec24C, is essential for male and female gametogenesis. Planta 238: 561-575.

http://scholar.google.com/scholar?as_q=&num=10&as_occt=any&as_sauthors=Tanaka,&hl=en&c2coff=1

http://scholar.google.com/scholar?as_q=Redundant function of two Arabidopsis COPII components, AtSec24B and At-Sec24C, is essential for male and female gametogenesis&num=10&btnG=Search+Scholar&as_epq=&as_oq=&as_eq=&as_occt=any&as_publication=&as_yhi=&as_allsubj=all&hl=en&lr=&c2coff=1

http://scholar.google.com/scholar?as_q=Redundant function of two Arabidopsis COPII components, AtSec24B and At-Sec24C, is essential for male and female gametogenesis&num=10&btnG=Search+Scholar&as_occt=any&as_sauthors=Tanaka,&as_ylo=2013&as_allsubj=all&hl=en&c2coff=1

http://www.ncbi.nlm.nih.gov/pubmed?term=Tian%2C L%2E%2C Dai%2C L%2EL%2E%2C Yin%2C Z%2EJ%2E%2C Fukuda%2C M%2E%2C Kumamaru%2C T%2E%2C Dong%2C X%2EB%2E%2C Xu%2C X%2EP%2E%2C and Qu%2C L%2EQ%2E %282013%29%2E Small GTPase Sar1 is crucial for proglutelin and a%2Dglobulin export from the endoplasmic reticulum in rice endosperm%2E J%2E Exp%2E Bot%2E 64%3A 2831%2D2845%2E&dopt=abstract

http://search.crossref.org/?page=1&rows=2&q=Tian, L., Dai, L.L., Yin, Z.J., Fukuda, M., Kumamaru, T., Dong, X.B., Xu, X.P., and Qu, L.Q. (2013). Small GTPase Sar1 is crucial for proglutelin and a-globulin export from the endoplasmic reticulum in rice endosperm. J. Exp. Bot. 64: 2831-2845.

http://scholar.google.com/scholar?as_q=&num=10&as_occt=any&as_sauthors=Tian,&hl=en&c2coff=1

http://scholar.google.com/scholar?as_q=Small GTPase Sar1 is crucial for proglutelin and a-globulin export from the endoplasmic reticulum in rice endosperm&num=10&btnG=Search+Scholar&as_epq=&as_oq=&as_eq=&as_occt=any&as_publication=&as_yhi=&as_allsubj=all&hl=en&lr=&c2coff=1

http://scholar.google.com/scholar?as_q=Small GTPase Sar1 is crucial for proglutelin and a-globulin export from the endoplasmic reticulum in rice endosperm&num=10&btnG=Search+Scholar&as_occt=any&as_sauthors=Tian,&as_ylo=2013&as_allsubj=all&hl=en&c2coff=1

Venditti, R., Wilson, C., De, and Matteis, M.A. (2014). Exiting the ER: what we know and what we don't. Trends Cell Biol. 24: 9-18.Pubmed: Author and TitleCrossRef: Author and TitleGoogle Scholar: Author Only Title Only Author and Title

Waadt, R., and Kudla, J. (2008). In planta visualization of protein interactions using bimolecular fluorescence complementation(BiFC). CSH Protoc. prot4995.


Wang, Y., Ren, Y., Liu, X., Jiang, L., Chen, L., Han, X., Jin, M., Liu, S., Liu, F., Lv, J., Zhou, K., Su, N., Bao, Y., and Wan, J. (2010).OsRab5a regulates endomembrane organization and storage protein trafficking in rice endosperm cells. Plant J. 64: 812-824.


Wang, Y., Zhu, S., Liu, S., Jiang, L., Chen, L., Ren, Y., Han, X., Liu, F., Ji, S., Liu, X., and Wan, J. (2009). The vacuolar processingenzyme OsVPE1 is required for efficient glutelin processing in rice. Plant J. 58: 606-617.


Wei, T., and Wang, A. (2008). Biogenesis of cytoplasmic membranous vesicles for plant potyvirus replication occurs at endoplasmicreticulum exit sites in a COPI- and COPII-dependent manner. J. Virol. 82: 12252-12264.


Yamagata, H., and Tanaka, K. (1986). The site of synthesis and accumulation of storage proteins. Plant Cell Physiol. 27: 135-145.Pubmed: Author and TitleCrossRef: Author and TitleGoogle Scholar: Author Only Title Only Author and Title

Yang, Y., Elamawi, R., Bubeck, J., Pepperkok, R., Ritzenthaler, C., and Robinson, D.G. (2005). Dynamics of COPII vesicles and theGolgi apparatus in cultured Nicotiana tabacum BY-2 cells provides evidence for transient association of Golgi stacks withendoplasmic reticulum exit sites. Plant cell 17: 1513-1531.


http://www.ncbi.nlm.nih.gov/pubmed?term=Venditti%2C R%2E%2C Wilson%2C C%2E%2C De%2C and Matteis%2C M%2EA%2E %282014%29%2E Exiting the ER%3A what we know and what we don%27t%2E Trends Cell Biol%2E 24%3A 9%2D18%2E&dopt=abstract

http://search.crossref.org/?page=1&rows=2&q=Venditti, R., Wilson, C., De, and Matteis, M.A. (2014). Exiting the ER: what we know and what we don't. Trends Cell Biol. 24: 9-18.

http://scholar.google.com/scholar?as_q=&num=10&as_occt=any&as_sauthors=Venditti,&hl=en&c2coff=1

http://scholar.google.com/scholar?as_q=Exiting the ER: what we know and what we don't&num=10&btnG=Search+Scholar&as_epq=&as_oq=&as_eq=&as_occt=any&as_publication=&as_yhi=&as_allsubj=all&hl=en&lr=&c2coff=1

http://scholar.google.com/scholar?as_q=Exiting the ER: what we know and what we don't&num=10&btnG=Search+Scholar&as_occt=any&as_sauthors=Venditti,&as_ylo=2014&as_allsubj=all&hl=en&c2coff=1

http://www.ncbi.nlm.nih.gov/pubmed?term=Waadt%2C R%2E%2C and Kudla%2C J%2E %282008%29%2E In planta visualization of protein interactions using bimolecular fluorescence complementation %28BiFC%29%2E CSH Protoc%2E prot4995%2E&dopt=abstract

http://search.crossref.org/?page=1&rows=2&q=Waadt, R., and Kudla, J. (2008). In planta visualization of protein interactions using bimolecular fluorescence complementation (BiFC). CSH Protoc. prot4995.

http://scholar.google.com/scholar?as_q=&num=10&as_occt=any&as_sauthors=Waadt,&hl=en&c2coff=1

http://scholar.google.com/scholar?as_q=In planta visualization of protein interactions using bimolecular fluorescence complementation (BiFC).&num=10&btnG=Search+Scholar&as_epq=&as_oq=&as_eq=&as_occt=any&as_publication=&as_yhi=&as_allsubj=all&hl=en&lr=&c2coff=1

http://scholar.google.com/scholar?as_q=In planta visualization of protein interactions using bimolecular fluorescence complementation (BiFC).&num=10&btnG=Search+Scholar&as_occt=any&as_sauthors=Waadt,&as_ylo=2008&as_allsubj=all&hl=en&c2coff=1

http://www.ncbi.nlm.nih.gov/pubmed?term=Wang%2C Y%2E%2C Ren%2C Y%2E%2C Liu%2C X%2E%2C Jiang%2C L%2E%2C Chen%2C L%2E%2C Han%2C X%2E%2C Jin%2C M%2E%2C Liu%2C S%2E%2C Liu%2C F%2E%2C Lv%2C J%2E%2C Zhou%2C K%2E%2C Su%2C N%2E%2C Bao%2C Y%2E%2C and Wan%2C J%2E %282010%29%2E OsRab5a regulates endomembrane organization and storage protein trafficking in rice endosperm cells%2E Plant J%2E 64%3A 812%2D824%2E&dopt=abstract

http://search.crossref.org/?page=1&rows=2&q=Wang, Y., Ren, Y., Liu, X., Jiang, L., Chen, L., Han, X., Jin, M., Liu, S., Liu, F., Lv, J., Zhou, K., Su, N., Bao, Y., and Wan, J. (2010). OsRab5a regulates endomembrane organization and storage protein trafficking in rice endosperm cells. Plant J. 64: 812-824.

http://scholar.google.com/scholar?as_q=&num=10&as_occt=any&as_sauthors=Wang,&hl=en&c2coff=1

http://scholar.google.com/scholar?as_q=OsRab5a regulates endomembrane organization and storage protein trafficking in rice endosperm cells&num=10&btnG=Search+Scholar&as_epq=&as_oq=&as_eq=&as_occt=any&as_publication=&as_yhi=&as_allsubj=all&hl=en&lr=&c2coff=1

http://scholar.google.com/scholar?as_q=OsRab5a regulates endomembrane organization and storage protein trafficking in rice endosperm cells&num=10&btnG=Search+Scholar&as_occt=any&as_sauthors=Wang,&as_ylo=2010&as_allsubj=all&hl=en&c2coff=1

http://www.ncbi.nlm.nih.gov/pubmed?term=Wang%2C Y%2E%2C Zhu%2C S%2E%2C Liu%2C S%2E%2C Jiang%2C L%2E%2C Chen%2C L%2E%2C Ren%2C Y%2E%2C Han%2C X%2E%2C Liu%2C F%2E%2C Ji%2C S%2E%2C Liu%2C X%2E%2C and Wan%2C J%2E %282009%29%2E The vacuolar processing enzyme OsVPE1 is required for efficient glutelin processing in rice%2E Plant J%2E 58%3A 606%2D617%2E&dopt=abstract

http://search.crossref.org/?page=1&rows=2&q=Wang, Y., Zhu, S., Liu, S., Jiang, L., Chen, L., Ren, Y., Han, X., Liu, F., Ji, S., Liu, X., and Wan, J. (2009). The vacuolar processing enzyme OsVPE1 is required for efficient glutelin processing in rice. Plant J. 58: 606-617.

http://scholar.google.com/scholar?as_q=&num=10&as_occt=any&as_sauthors=Wang,&hl=en&c2coff=1

http://scholar.google.com/scholar?as_q=The vacuolar processing enzyme OsVPE1 is required for efficient glutelin processing in rice&num=10&btnG=Search+Scholar&as_epq=&as_oq=&as_eq=&as_occt=any&as_publication=&as_yhi=&as_allsubj=all&hl=en&lr=&c2coff=1

http://scholar.google.com/scholar?as_q=The vacuolar processing enzyme OsVPE1 is required for efficient glutelin processing in rice&num=10&btnG=Search+Scholar&as_occt=any&as_sauthors=Wang,&as_ylo=2009&as_allsubj=all&hl=en&c2coff=1

http://www.ncbi.nlm.nih.gov/pubmed?term=Wei%2C T%2E%2C and Wang%2C A%2E %282008%29%2E Biogenesis of cytoplasmic membranous vesicles for plant potyvirus replication occurs at endoplasmic reticulum exit sites in a COPI%2D and COPII%2Ddependent manner%2E J%2E Virol%2E 82%3A 12252%2D12264%2E&dopt=abstract

http://search.crossref.org/?page=1&rows=2&q=Wei, T., and Wang, A. (2008). Biogenesis of cytoplasmic membranous vesicles for plant potyvirus replication occurs at endoplasmic reticulum exit sites in a COPI- and COPII-dependent manner. J. Virol. 82: 12252-12264.

http://scholar.google.com/scholar?as_q=&num=10&as_occt=any&as_sauthors=Wei,&hl=en&c2coff=1

http://scholar.google.com/scholar?as_q=Biogenesis of cytoplasmic membranous vesicles for plant potyvirus replication occurs at endoplasmic reticulum exit sites in a COPI- and COPII-dependent manner&num=10&btnG=Search+Scholar&as_epq=&as_oq=&as_eq=&as_occt=any&as_publication=&as_yhi=&as_allsubj=all&hl=en&lr=&c2coff=1

http://scholar.google.com/scholar?as_q=Biogenesis of cytoplasmic membranous vesicles for plant potyvirus replication occurs at endoplasmic reticulum exit sites in a COPI- and COPII-dependent manner&num=10&btnG=Search+Scholar&as_occt=any&as_sauthors=Wei,&as_ylo=2008&as_allsubj=all&hl=en&c2coff=1

http://www.ncbi.nlm.nih.gov/pubmed?term=Yamagata%2C H%2E%2C and Tanaka%2C K%2E %281986%29%2E The site of synthesis and accumulation of storage proteins%2E Plant Cell Physiol%2E 27%3A 135%2D145%2E&dopt=abstract

http://search.crossref.org/?page=1&rows=2&q=Yamagata, H., and Tanaka, K. (1986). The site of synthesis and accumulation of storage proteins. Plant Cell Physiol. 27: 135-145.

http://scholar.google.com/scholar?as_q=&num=10&as_occt=any&as_sauthors=Yamagata,&hl=en&c2coff=1

http://scholar.google.com/scholar?as_q=The site of synthesis and accumulation of storage proteins&num=10&btnG=Search+Scholar&as_epq=&as_oq=&as_eq=&as_occt=any&as_publication=&as_yhi=&as_allsubj=all&hl=en&lr=&c2coff=1

http://scholar.google.com/scholar?as_q=The site of synthesis and accumulation of storage proteins&num=10&btnG=Search+Scholar&as_occt=any&as_sauthors=Yamagata,&as_ylo=1986&as_allsubj=all&hl=en&c2coff=1

http://www.ncbi.nlm.nih.gov/pubmed?term=Yang%2C Y%2E%2C Elamawi%2C R%2E%2C Bubeck%2C J%2E%2C Pepperkok%2C R%2E%2C Ritzenthaler%2C C%2E%2C and Robinson%2C D%2EG%2E %282005%29%2E Dynamics of COPII vesicles and the Golgi apparatus in cultured Nicotiana tabacum BY%2D2 cells provides evidence for transient association of Golgi stacks with endoplasmic reticulum exit sites%2E Plant cell 17%3A 1513%2D1531%2E&dopt=abstract

http://search.crossref.org/?page=1&rows=2&q=Yang, Y., Elamawi, R., Bubeck, J., Pepperkok, R., Ritzenthaler, C., and Robinson, D.G. (2005). Dynamics of COPII vesicles and the Golgi apparatus in cultured Nicotiana tabacum BY-2 cells provides evidence for transient association of Golgi stacks with endoplasmic reticulum exit sites. Plant cell 17: 1513-1531.

http://scholar.google.com/scholar?as_q=&num=10&as_occt=any&as_sauthors=Yang,&hl=en&c2coff=1

http://scholar.google.com/scholar?as_q=Dynamics of COPII vesicles and the Golgi apparatus in cultured Nicotiana tabacum BY-2 cells provides evidence for transient association of Golgi stacks with endoplasmic reticulum exit sites&num=10&btnG=Search+Scholar&as_epq=&as_oq=&as_eq=&as_occt=any&as_publication=&as_yhi=&as_allsubj=all&hl=en&lr=&c2coff=1

http://scholar.google.com/scholar?as_q=Dynamics of COPII vesicles and the Golgi apparatus in cultured Nicotiana tabacum BY-2 cells provides evidence for transient association of Golgi stacks with endoplasmic reticulum exit sites&num=10&btnG=Search+Scholar&as_occt=any&as_sauthors=Yang,&as_ylo=2005&as_allsubj=all&hl=en&c2coff=1

DOI 10.1105/tpc.16.00717; originally published online November 1, 2016;Plant Cell

Yiqun Bao and Jianmin WanXiaopin Zhu, Ruonan Jing, Mingming Wu, Yuanyuan Hao, Ling Jiang, Chunming Wang, Haiyang Wang,

Yihua Wang, Feng Liu, Yulong Ren, Yunlong Wang, Xi Liu, Wuhua Long, Di Wang, Jianping Zhu,Endosperm Cells

GOLGI TRANSPORT 1B Regulates Protein Export from Endoplasmic Reticulum in Rice

This information is current as of November 17, 2020

Supplemental Data

/content/suppl/2016/12/05/tpc.16.00717.DC3.html /content/suppl/2016/12/05/tpc.16.00717.DC2.html /content/suppl/2016/11/01/tpc.16.00717.DC1.html

Permissions https://www.copyright.com/ccc/openurl.do?sid=pd_hw1532298X&issn=1532298X&WT.mc_id=pd_hw1532298X

eTOCs http://www.plantcell.org/cgi/alerts/ctmain

Sign up for eTOCs at:

CiteTrack Alerts http://www.plantcell.org/cgi/alerts/ctmain

Sign up for CiteTrack Alerts at:

Subscription Information http://www.aspb.org/publications/subscriptions.cfm

is available at:Plant Physiology and The Plant CellSubscription Information for

ADVANCING THE SCIENCE OF PLANT BIOLOGY © American Society of Plant Biologists

https://www.copyright.com/ccc/openurl.do?sid=pd_hw1532298X&issn=1532298X&WT.mc_id=pd_hw1532298X

http://www.plantcell.org/cgi/alerts/ctmain

http://www.plantcell.org/cgi/alerts/ctmain

http://www.aspb.org/publications/subscriptions.cfm

Documents

GOLGI TRANSPORT 1B Regulates Protein Export from ...€¦ · 01/11/2016 · Only those proglutelins arriving at the PBII/PSV can 122 be cleaved into the mature 40-kDa acidic and