cis-Golgi proteins accumulate near the ER exit sites and act as the scaffold for Golgi regeneration after brefeldin A treatment in tobacco BY-2 cells

Ito, Yoko; Uemura, Tomohiro; Shoda, Keiko; Fujimoto, Masaru; Ueda, Takashi; Nakano, Akihiko

doi:10.1091/mbc.e12-01-0034

Cited by 86 publications

(100 citation statements)

References 69 publications

(112 reference statements)

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“…1E). The observation on the association of AtSar1a punctate with the Golgi apparatus is consistent with previous studies using superresolution microscopy that showed that ERES are surrounded by the Golgi apparatus and that ERES shows more numbers than the Golgi (15,23). In contrast, most of the AtSar1c-GFP-labeled punctae were not Golgi-associated under superresolution microscopy.…”

Section: Resultssupporting

confidence: 91%

“…In mammals, ERES are frequently associated with the ER-Golgi intermediate compartment (ERGIC). The presence of ERGIC in higher plant cells remains elusive but a recent study suggests that the SYP31 compartment may represent a scaffold to build the Golgi stack, similar to the ERGIC in mammals (15). COPII components have been used as markers to study ERES in plants with various working models on the spatial relationship between ERES and Golgi (16).…”

Section: Resultsmentioning

confidence: 99%

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Unique COPII component AtSar1a/AtSec23a pair is required for the distinct function of protein ER export in Arabidopsis thaliana

Zeng

Chung

et al. 2015

Proc. Natl. Acad. Sci. U.S.A.

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Secretory proteins traffic from endoplasmic reticulum (ER) to Golgi via the coat protein complex II (COPII) vesicle, which consists of five cytosolic components (Sar1,. In eukaryotes, COPII transport has diversified due to gene duplication, creating multiple COPII paralogs. Evidence has accumulated, revealing the functional heterogeneity of COPII paralogs in protein ER export. Sar1B, the small GTPase of COPII machinery, seems to be specialized for large cargo secretion in mammals. Arabidopsis contains five Sar1 and seven Sec23 homologs, and AtSar1a was previously shown to exhibit different effects on α-amylase secretion. However, mechanisms underlying the functional diversity of Sar1 paralogs remain unclear in higher organisms. Here, we show that the Arabidopsis Sar1 homolog AtSar1a exhibits distinct localization in plant cells. Transgenic Arabidopsis plants expressing dominant-negative AtSar1a exhibit distinct effects on ER cargo export. Mutagenesis analysis identified a single amino acid, Cys84, as being responsible for the functional diversity of AtSar1a. Structure homology modeling and interaction studies revealed that Cys84 is crucial for the specific interaction of AtSar1a with AtSec23a, a distinct Arabidopsis Sec23 homolog. Structure modeling and coimmunoprecipitation further identified a corresponding amino acid, Cys484, on AtSec23a as being essential for the specific pair formation. At the cellular level, the Cys484 mutation affects the distinct function of AtSec23a on vacuolar cargo trafficking. Additionally, dominant-negative AtSar1a affects the ER export of the transcription factor bZIP28 under ER stress. We have demonstrated a unique plant pair of COPII machinery function in ER export and the mechanism underlying the functional diversity of COPII paralogs in eukaryotes.coat protein complex II | Sar1 | Sec23 | ER export | functional diversity

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Section: Resultssupporting

confidence: 91%

Section: Resultsmentioning

confidence: 99%

Unique COPII component AtSar1a/AtSec23a pair is required for the distinct function of protein ER export in Arabidopsis thaliana

Zeng

Chung

et al. 2015

Proc. Natl. Acad. Sci. U.S.A.

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“…Golgi stacks in tobacco cells are formed in the order from cis-to trans-cisternae and that the presence of scaffold at cis-most side, which we named Golgi entry core compartment (GECCO), plays a role of receiving cargo from the ER (Ito et al, 2012(Ito et al, , 2017. Furthermore, computational simulation has implicated self-organizing properties of Golgi cisternae during reassembly processes (Tachikawa and Mochizuki, 2017).…”

Section: Discussionmentioning

confidence: 99%

“…To further investigate the anomalies of the Golgi morphology, the arrangement of cis and trans cisternae in Golgi stacks was examined in the wild-type and #46-3 plants stably expressing ST-mRFP, a trans-Golgi marker (sialyl transferase from rat) (Boevink et al, 1998;Ito et al, 2012;, in addition to ERD2-GFP. As shown in Fig.…”

Section: Localization Analysis Of Cis-and Trans-golgi In the #46-3 Mumentioning

confidence: 99%

A Missense Mutation in the NSF Gene Causes Abnormal Golgi Morphology in Arabidopsis thaliana

Tanabashi

Shoda

Saito

et al. 2018

Cell Struct. Funct.

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The Golgi apparatus is a key station of glycosylation and membrane traffic. It consists of stacked cisternae in most eukaryotes. However, the mechanisms how the Golgi stacks are formed and maintained are still obscure. The model plant Arabidopsis thaliana provides a nice system to observe Golgi structures by light microscopy, because the Golgi in A. thaliana is in the form of mini-stacks that are distributed throughout the cytoplasm. To obtain a clue to understand the molecular basis of Golgi morphology, we took a forward-genetic approach to isolate A. thaliana mutants that show abnormal structures of the Golgi under a confocal microscope. In the present report, we describe characterization of one of such mutants, named #46-3. The #46-3 mutant showed pleiotropic Golgi phenotypes. The Golgi size was in majority smaller than the wild type, but varied from very small ones, sometimes without clear association of cis and trans cisternae, to abnormally large ones under a confocal microscope.At the ultrastructual level by electron microscopy, queer-shaped large Golgi stacks were occasionally observed. By positional mapping, genome sequencing, and complementation and allelism tests, we linked the mutant phenotype to the missense mutation D374N in the NSF gene, encoding the N-ethylmaleimide-sensitive factor (NSF), a key component of membrane fusion. This residue is near the ATP-binding site of NSF, which is very well conserved in eukaryotes, suggesting that the biochemical function of NSF is important for maintaining the normal morphology of the Golgi.3

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“…However, with improved resolution, it looks more likely that small structures containing a cis-Golgi marker move around and grow over time before entering the maturation phase. We usually use Suppressor of Erd2 Deletion (Sed5; the counterpart of SYP31/SYP32 of plants and syntaxin5 of mammals) as a cis-Golgi marker, but considering the findings we have made in tobacco BY2 cells (Ito et al, 2012), the yeast Sed5 compartment may represent both a sorting platform like the ERGIC as well as the first enzymatic station of the glycosylation factory (see also below). (5) Is a hug-andkiss mechanism specific to yeast?…”

Section: Akihiko Nakano: a Common Mechanism For Er-to-golgi Traffic: mentioning

confidence: 99%

Vesicles versus Tubes: Is Endoplasmic Reticulum-Golgi Transport in Plants Fundamentally Different from Other Eukaryotes?

et al. 2015

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cis-Golgi proteins accumulate near the ER exit sites and act as the scaffold for Golgi regeneration after brefeldin A treatment in tobacco BY-2 cells

Cited by 86 publications

References 69 publications

Unique COPII component AtSar1a/AtSec23a pair is required for the distinct function of protein ER export in Arabidopsis thaliana

Unique COPII component AtSar1a/AtSec23a pair is required for the distinct function of protein ER export in Arabidopsis thaliana

A Missense Mutation in the <i>NSF</i> Gene Causes Abnormal Golgi Morphology in <i>Arabidopsis thaliana</i>

Vesicles versus Tubes: Is Endoplasmic Reticulum-Golgi Transport in Plants Fundamentally Different from Other Eukaryotes?

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