TRAPPI tethers COPII vesicles by binding the coat subunit Sec23

Cai, Huaqing; Yu, Sidney; Menon, Shekar; Cai, Yiying; Lazarova, Darina L.; Fu, Chao; Reinisch, Karin M; Hay, Jesse; Ferro‐Novick, Susan

doi:10.1038/nature05527

Cited by 222 publications

(261 citation statements)

References 28 publications

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“…However, the mixed nature of the Vps53 C terminus surface, and of the conserved surface in particular, argues against this mechanism for the Vps53 C terminus. Several tethering complexes, including Dsl1 and TRAPPI (20,21), recognize proteins in the vesicle coat, and an intriguing possibility is that the Vps53 C terminus could interact with the retromer coat of endosome-derived vesicles, perhaps through the conserved patch.…”

Section: Resultsmentioning

confidence: 99%

Structure of a C-terminal fragment of its Vps53 subunit suggests similarity of Golgi-associated retrograde protein (GARP) complex to a family of tethering complexes

Vasan

Hutagalung

Novick

et al. 2010

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

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The Golgi-associated retrograde protein (GARP) complex is a membrane-tethering complex that functions in traffic from endosomes to the trans-Golgi network. Here we present the structure of a C-terminal fragment of the Vps53 subunit, important for binding endosome-derived vesicles, at a resolution of 2.9 Å. We show that the C terminus consists of two α-helical bundles arranged in tandem, and we identify a highly conserved surface patch, which may play a role in vesicle recognition. Mutations of the surface result in defects in membrane traffic. The fold of the Vps53 C terminus is strongly reminiscent of proteins that belong to three other tethering complexes—Dsl1, conserved oligomeric Golgi, and the exocyst—thought to share a common evolutionary origin. Thus, the structure of the Vps53 C terminus suggests that GARP belongs to this family of complexes.

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Section: Resultsmentioning

confidence: 99%

Structure of a C-terminal fragment of its Vps53 subunit suggests similarity of Golgi-associated retrograde protein (GARP) complex to a family of tethering complexes

Vasan

Hutagalung

Novick

et al. 2010

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

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“…A previous study indicated that COPII tethering and fusion was completely blocked in the presence of excess Sec23p in vitro (29). To evaluate the effects of the corresponding amino acid in AtSec23a on cargo ER export, we coexpressed the soluble cargo Aleurain-GFP with indicated mutants of AtSec23a and AtSec23b in Arabidopsis protoplasts.…”

Section: Atsar1a Interacts With the Unique Plant Copii-inner Coat Promentioning

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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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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“…19,[37][38][39] In the case of TRAPPI-mediated COPII tethering, it is believed that the initial tethering requires an interaction between TRAPPI and Sec23, 37 perhaps also an interaction between TRAPPI and Ypt1. 38 It is likely that TRAPPII in plant cells can also serve as RAB-A1c(Q72L).…”

confidence: 99%

Arabidopsis TRAPPII is functionally linked to Rab-A, but not Rab-D in polar protein trafficking intrans-Golgi network

Zheng

2011

Plant Signaling & Behavior

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TRAPPI tethers COPII vesicles by binding the coat subunit Sec23

Cited by 222 publications

References 28 publications

Structure of a C-terminal fragment of its Vps53 subunit suggests similarity of Golgi-associated retrograde protein (GARP) complex to a family of tethering complexes

Structure of a C-terminal fragment of its Vps53 subunit suggests similarity of Golgi-associated retrograde protein (GARP) complex to a family of tethering complexes

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

Arabidopsis TRAPPII is functionally linked to Rab-A, but not Rab-D in polar protein trafficking intrans-Golgi network

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