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Article

Yeast synaptobrevin homologs are modified posttranslationally by the addition of palmitate.

Proceedings of the National Academy of Sciences of the United States of America - 20 Jun 1995

Couve A, Protopopov V, Gerst J E

Abstract excerpt

Yeast possess two homologs of the synaptobrevin family of vesicle-associated membrane proteins that function in membrane recognition and vesicle fusion. Yeast proteins Snc1 and Snc2 localize to secretory vesicles and are required for constitutive exocytosis. They also form a physical complex with a plasma membrane protein, Sec9, which is necessary for vesicle docking and fusion to occur in vivo. Formation of this...

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Identifiers

PMID: 7597066
DOI: 10.1073/pnas.92.13.5987
PMCID: PMC41627

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Yeast synaptobrevin homologs are modified posttranslationally by the addition of palmitate.PMID 7597066Read ↗

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Geranylgeranylated SNAREs are dominant inhibitors of membrane fusion.Semantic proximity Read ↗

Palmitoylation determines the function of Vac8 at the yeast vacuole.Semantic proximity Read ↗

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Palmitoylation and plasma membrane localization of Ras2p by a nonclassical trafficking pathway in Saccharomyces cerevisiae.Semantic proximity Read ↗

New links between <i>S</i>‐acylation and cancerSemantic proximity Read ↗

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A facile assay for zDHHC palmitoyl transferase activation elucidates effects of mutation and modification.Semantic proximity Read ↗

The synaptobrevin homologue Snc2p recruits the exocyst to secretory vesicles by binding to Sec6pSemantic proximity Read ↗

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