Molecular Dissection of Erv26p Identifies Separable Cargo Binding and Coat Protein Sorting Activities

Bue, Catherine A.; Barlowe, Charles

doi:10.1074/jbc.m109.022590

Cited by 26 publications

(18 citation statements)

References 49 publications

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“…The cargo includes vacuolar alkaline phosphatase and several Golgi-localized glycosyltransferases (Bue & Barlowe 2009, Herzig et al 2012. Typically, these cargo proteins have larger luminal domains and short cytosolic tail sequences.…”

Section: Erv26mentioning

confidence: 99%

Cargo Capture and Bulk Flow in the Early Secretory Pathway

Barlowe

Helenius

2016

Annu. Rev. Cell Dev. Biol.

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175

191

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Transport of newly synthesized proteins from the endoplasmic reticulum (ER) to the Golgi complex is highly selective. As a general rule, such transport is limited to soluble and membrane-associated secretory proteins that have reached properly folded and assembled conformations. To secure the efficiency, fidelity, and control of this crucial transport step, cells use a combination of mechanisms. The mechanisms are based on selective retention of proteins in the ER to prevent uptake into transport vesicles, on selective capture of proteins in COPII carrier vesicles, on inclusion of proteins in these vesicles by default as part of fluid and membrane bulk flow, and on selective retrieval of proteins from post-ER compartments by retrograde vesicle transport.

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Section: Erv26mentioning

confidence: 99%

Cargo Capture and Bulk Flow in the Early Secretory Pathway

Barlowe

Helenius

2016

Annu. Rev. Cell Dev. Biol.

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175

191

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“…Yeast Erv26p is one such adaptor that mediates ER export of type-II integral membrane proteins. These single pass proteins often have short N-terminal tails with binding signals for trafficking in the late secretory pathway, thus perhaps necessitating the aid of a cargo adaptor for ER exit [88] (Figure 2C). Erv14 is another conserved non-canonical receptor that appears to be required for ER exit of many integral membrane proteins that ultimately reside in the plasma membrane [89, Herzig, 2012 #93].…”

Section: Lumenal Regulation Of Copii Function: Cargo As Active Parmentioning

confidence: 99%

Vesicle-mediated export from the ER: COPII coat function and regulation

D’Arcangelo

Stahmer

Miller

2013

Biochimica et Biophysica Acta (BBA) - Molecular Cell Research

134

119

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Vesicle trafficking from the endoplasmic reticulum (ER) is a vital cellular process in all eukaryotes responsible for moving secretory cargoes from the ER to the Golgi apparatus. To accomplish this feat, the cell employs a set of conserved cytoplasmic coat proteins – the coat protein II (COPII) complex – that recruits cargo into nascent buds and deforms the ER membrane to drive vesicle formation. While our understanding of COPII coat mechanics has developed substantially since its discovery, we have only recently begun to appreciate the factors that regulate this complex and, in turn, ER-to-Golgi trafficking. Here, we describe these factors and their influences on COPII vesicle formation. Properties intrinsic to the GTP cycle of the coat, as well as coat structure, have critical implications for COPII vesicle trafficking. Extrinsic factors in the cytosol can modulate COPII activity through direct interaction with the coat or with scaffolding components, or by changing composition of the ER membrane. Further, lumenal and membrane-bound cargoes and cargo receptors can influence COPII-mediated trafficking in equally profound ways. Together, these factors work in concert to ensure proper cargo movement in this first step of the secretory pathway.

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“…In yeast, Erv29p is essential for export of the soluble pheromone, pro-a-factor (27). Erv26p has been recently reported to be required for sorting of soluble yeast alkaline phosphatase in vesicles exiting the ER (28). These and other studies strongly suggest that export of soluble cargo is a receptor-mediated event.…”

Section: Exit Of Soluble Cargo From the Ermentioning

confidence: 65%

Proteostasis Strategies for Restoring 1-Antitrypsin Deficiency

Bouchecareilh

Conkright²,

Balch³

2010

Proceedings of the American Thoracic Society

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The function of the human proteome is defined by the proteostasis network (PN) (Science 2008;319:916; Science 2010;329:766), a biological system that generates, protects, and, where necessary, degrades a protein to optimize the cell, tissue, and organismal response to diet, stress, and aging. Numerous human diseases result from the failure of proteins to fold properly in response to mutation, disrupting the proteome. In the case of the exocytic pathway, this includes proteostasis components that direct folding, and export of proteins from the endoplasmic reticulum (ER). Included here are serpin deficiencies, a class of related diseases that result in a significant reduction of secretion of serine proteinase inhibitors from the liver into serum. In response to misfolding, variants of the serine protease a 1 -antitrypsin (a1AT) fail to exit the ER and are targeted for either ER-associated degradation or autophagic pathways. The challenge for developing a1AT deficiency therapeutics is to understand the PN pathways involved in folding and export. Herein, we review the role of the PN in managing the protein fold and function during synthesis in the ER and trafficking to the cell surface or extracellular space. We highlight the role of the proteostasis boundary to define the operation of the proteome (Annu Rev Biochem 2009;78:959). We discuss how manipulation of folding energetics or the PN by pharmacological intervention could provide multiple routes for restoration of variant a1AT function to the benefit of human health.

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Molecular Dissection of Erv26p Identifies Separable Cargo Binding and Coat Protein Sorting Activities

Cited by 26 publications

References 49 publications

Cargo Capture and Bulk Flow in the Early Secretory Pathway

Cargo Capture and Bulk Flow in the Early Secretory Pathway

Vesicle-mediated export from the ER: COPII coat function and regulation

Proteostasis Strategies for Restoring 1-Antitrypsin Deficiency

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