Kinase Signaling Initiates Coat Complex II (COPII) Recruitment and Export from the Mammalian Endoplasmic Reticulum

Aridor, Meir; Balch, William E.

doi:10.1074/jbc.c000449200

Cited by 109 publications

(132 citation statements)

References 29 publications

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“…As a control, under identical conditions we also tested the effect of Sar1-GTP(H79G) on the processing of the reporter cargo type 1 transmembrane protein vesicular stomatitis virus glycoprotein (VSV-G) from the endoglycosidase H (endo H)-sensitive pre-Golgi form to the endo H-resistant, Golgi-processed glycoisoform as described previously (28,30). Consistent with previous findings (26,30,(32)(33)(34), transport of VSV-G was potently inhibited by the Sar1-GTP(H79G) mutant (Fig. 1D).…”

Section: Cftr Maturation Issupporting

confidence: 63%

Non-conventional Trafficking of the Cystic Fibrosis Transmembrane Conductance Regulator through the Early Secretory Pathway

Yoo¹,

Moyer²,

Bannykh³

et al. 2002

Journal of Biological Chemistry

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174

156

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The mechanism(s) of cystic fibrosis transmembrane conductance regulator (CFTR) trafficking from the endoplasmic reticulum (ER) through the Golgi apparatus, the step impaired in individuals afflicted with the prevalent CFTR-⌬F508 mutation leading to cystic fibrosis, is largely unknown. Recent morphological observations suggested that CFTR is largely absent from the Golgi in situ (Bannykh, S. I., Bannykh, G. I., Fish, K. N., Moyer, B. D., Riordan, J. R., and Balch, W. E. (2000) Traffic 1, 852-870), raising the possibility of a novel trafficking pathway through the early secretory pathway. We now report that export of CFTR from the ER is regulated by the conventional coat protein complex II (COPII) in all cell types tested. Remarkably, in a cell type-specific manner, processing of CFTR from the core-glycosylated (band B) ER form to the complex-glycosylated (band C) isoform followed a non-conventional pathway that was insensitive to dominant negative Arf1, Rab1a/Rab2 GTPases, or the SNAp REceptor (SNARE) component syntaxin 5, all of which block the conventional trafficking pathway from the ER to the Golgi. Moreover, CFTR transport through the non-conventional pathway was potently blocked by overexpression of the late endosomal target-SNARE syntaxin 13, suggesting that recycling through a late Golgi/endosomal system was a prerequisite for CFTR maturation. We conclude that CFTR transport in the early secretory pathway can involve a novel pathway between the ER and late Golgi/endosomal compartments that may influence developmental expression of CFTR on the cell surface in polarized epithelial cells.

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Section: Cftr Maturation Issupporting

confidence: 63%

Non-conventional Trafficking of the Cystic Fibrosis Transmembrane Conductance Regulator through the Early Secretory Pathway

Yoo¹,

Moyer²,

Bannykh³

et al. 2002

Journal of Biological Chemistry

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174

156

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“…S1 A and B). To confirm that the punctate structures labeled by AtSar1a-GFP and AtSar1c-GFP are bona fide COPII assembly sites, we treated the transgenic plants with H89, the protein kinase inhibitor used to inhibit Sar1 and COPII assembly onto the ER membrane (22). The punctae labeled by AtSar1a-GFP and AtSar1c-GFP gradually decreased upon treatments with increasing concentrations of H89 (SI Appendix, Fig.…”

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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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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“…Sar1 under these conditions is localized to these elongated sites, which contain recruited punctated Sec13 (data not shown). Notably, Sec13 recruitment was blocked by the addition of the protein kinase inhibitor H89, which inhibits Sar1 recruitment, COPII assembly, and ER export (Muniz et al, 1996(Muniz et al, , 1997Aridor and Balch, 2000;Leemhuis et al, 2002) (Fig. 2 and data not shown).…”

Section: Resultsmentioning

confidence: 99%

Endoplasmic Reticulum Export Site Formation and Function in Dendrites

Aridor

Guzik²,

Bielli³

et al. 2004

J. Neurosci.

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The elongated and polarized characteristics of neurons render targeting of receptors to the plasma membrane of distal axonal projections and dendritic branches a major sorting task. Although the majority of biosynthetic cargo synthesis, transport, and sorting are believed to occur in the soma, local membrane protein translation and sorting has been reported recently to take place in dendrites and axons. We investigated where endoplasmic reticulum (ER) export occurs in dendrites using an in vitro permeabilized neuron system that enables us to specifically control the assembly of ER export sites. We show that ER export sites are assembled regularly throughout the entire dendritic tree by the regulated sequential recruitment of Sar1 and COPII (coat protein complex II). Moreover, activation of metabotropic glutamate receptors leads to the recruitment of the NMDA receptor subunit NR1 to remodeled ER export sites. We propose that regulation of receptor assembly and export from the ER in dendrites plays an important role in modulating receptor surface expression and neuronal function.

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Kinase Signaling Initiates Coat Complex II (COPII) Recruitment and Export from the Mammalian Endoplasmic Reticulum

Cited by 109 publications

References 29 publications

Non-conventional Trafficking of the Cystic Fibrosis Transmembrane Conductance Regulator through the Early Secretory Pathway

Non-conventional Trafficking of the Cystic Fibrosis Transmembrane Conductance Regulator through the Early Secretory Pathway

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

Endoplasmic Reticulum Export Site Formation and Function in Dendrites

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