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PMID: 7990964 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Ypt1p implicated in v-SNARE activation.

Nature ·Vol. 372 ·No. 6507 ·1994-12-15 ·Pages 698-701

Lian JP, Stone S, Jiang Y, Lyons P, Ferro-Novick S

Abstract

Synaptobrevin-like membrane proteins that reside on transport vesicles, called the vesicle SNARE (v-SNARE), play a key role in ensuring that a vesicle targets and fuses with its correct acceptor compartment. Here we show that Bos1p, the v-SNARE of yeast endoplasmic reticulum-to-Golgi transport vesicles, pairs with another integral membrane protein of similar topology (Sec22p) on vesicles. This pairing, which appears to require functional Ypt1p (Rab in mammalian cells), may aid the activity of Bos1p on this compartment. These findings suggest that Rabs regulate the specificity of membrane fusion by selectively activating the v-SNARE on carrier vesicles. Because the v-SNARE resides on more than one membrane, such a regulated activation step may be necessary to prevent the premature fusion of donor and acceptor compartments.

Related Genes
MeSH Terms
Biological Transport Endoplasmic Reticulum/metabolism Fungal Proteins/metabolism GTP-Binding Proteins/metabolism Genes, Fungal Golgi Apparatus/metabolism Intracellular Membranes/metabolism Membrane Fusion Membrane Proteins/genetics,metabolism Organelles/metabolism Qb-SNARE Proteins Saccharomyces cerevisiae/metabolism Saccharomyces cerevisiae Proteins Vesicular Transport Proteins rab GTP-Binding Proteins
Chemicals
BOS1 protein, S cerevisiae Fungal Proteins Membrane Proteins Qb-SNARE Proteins Saccharomyces cerevisiae Proteins Vesicular Transport Proteins GTP-Binding Proteins YPT1 protein, S cerevisiae rab GTP-Binding Proteins
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Lian J P
Department of Cell Biology, Yale University Medical School, New Haven, Connecticut 06510.
Stone S
Jiang Y
Lyons P
Ferro-Novick S
Article Info
Journal
Nature
Abbr.
Nature
ISSN
0028-0836
Published
1994-12-15
Pages
698-701
Language
English
Region
England
NLM ID
0410462
Subset
IM
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