A direct role for the Sec1/Munc18-family protein Vps33 as a template for SNARE assembly-Reference-Cited by-同舟云学术

A direct role for the Sec1/Munc18-family protein Vps33 as a template for SNARE assembly

Published:2015-09-04 Issue:6252 Volume:349 Page:1111-1114
ISSN:0036-8075
Container-title:Science
language:en
Short-container-title:Science

Author:

Baker Richard W.¹,Jeffrey Philip D.¹,Zick Michael²,Phillips Ben P.¹,Wickner William T.²,Hughson Frederick M.¹

Affiliation:

1. Department of Molecular Biology, Princeton University, Princeton, NJ 08544, USA.

2. Department of Biochemistry, Geisel School of Medicine at Dartmouth, Hanover, NH 03755, USA.

Abstract

Unravelling the SM-SNARE conundrum So-called SNARE proteins mediate and lend specificity to the fusion between different intracellular membranes. The SM proteins are universally required for intracellular vesicle fusion, yet their mechanism of action has long been enigmatic. Baker et al. have solved a piece of the puzzle by “capturing” SNAREs in the process of assembling into fusogenic complexes on the surface of an SM protein. The findings suggest exactly how and why SM proteins help vesicular fusion during intracellular membrane trafficking. Science , this issue p. 1111

Funder

NSF

NIH

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

Reference44 articles.

1. Membrane Fusion: Grappling with SNARE and SM Proteins

2. Conserved structural features of the synaptic fusion complex: SNARE proteins reclassified as Q- and R-SNAREs

3. The Membrane Fusion Enigma: SNAREs, Sec1/Munc18 Proteins, and Their Accomplices—Guilty as Charged?

4. Sec1/Munc18 protein Vps33 binds to SNARE domains and the quaternary SNARE complex

5. HOPS drives vacuole fusion by binding the vacuolar SNARE complex and the Vam7 PX domain via two distinct sites

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