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ER cargo properties specify a requirement for COPII coat rigidity mediated by Sec13p.

ABSTRACT: Eukaryotic secretory proteins exit the endoplasmic reticulum (ER) via transport vesicles generated by the essential coat protein complex II (COPII) proteins. The outer coat complex, Sec13-Sec31, forms a scaffold that is thought to enforce curvature. By exploiting yeast bypass-of-sec-thirteen (bst) mutants, where Sec13p is dispensable, we probed the relationship between a compromised COPII coat and the cellular context in which it could still function. Genetic and biochemical analyses suggested that Sec13p was required to generate vesicles from membranes that contained asymmetrically distributed cargoes that were likely to confer opposing curvature. Thus, Sec13p may rigidify the COPII cage and increase its membrane-bending capacity; this function could be bypassed when a bst mutation renders the membrane more deformable.

SUBMITTER: Copic A

PROVIDER: S-EPMC3306526 | biostudies-literature | 2012 Mar

REPOSITORIES: biostudies-literature

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ER cargo properties specify a requirement for COPII coat rigidity mediated by Sec13p.

Copic Alenka A Latham Catherine F CF Horlbeck Max A MA D'Arcangelo Jennifer G JG Miller Elizabeth A EA

Science (New York, N.Y.) 20120202 6074

Eukaryotic secretory proteins exit the endoplasmic reticulum (ER) via transport vesicles generated by the essential coat protein complex II (COPII) proteins. The outer coat complex, Sec13-Sec31, forms a scaffold that is thought to enforce curvature. By exploiting yeast bypass-of-sec-thirteen (bst) mutants, where Sec13p is dispensable, we probed the relationship between a compromised COPII coat and the cellular context in which it could still function. Genetic and biochemical analyses suggested t ...[more]

PMID: 22300850

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