A cascade of multiple proteins and lipids catalyzes membrane fusion-Reference-Cited by-同舟云学术

A cascade of multiple proteins and lipids catalyzes membrane fusion

Published:2017-03-15 Issue:6 Volume:28 Page:707-711
ISSN:1059-1524
Container-title:Molecular Biology of the Cell
language:en
Short-container-title:MBoC

Author:

Wickner William¹,Rizo Josep²

Affiliation:

1. Department of Biochemistry and Cell Biology, Geisel School of Medicine at Dartmouth, Hanover, NH 03755

2. Departments of Biophysics, Biochemistry, and Biophysics, University of Texas Southwestern Medical Center, Dallas, TX 75390

Abstract

Recent studies suggest revisions to the SNARE paradigm of membrane fusion. Membrane tethers and/or SNAREs recruit proteins of the Sec 1/Munc18 family to catalyze SNARE assembly into trans-complexes. SNARE-domain zippering draws the bilayers into immediate apposition and provides a platform to position fusion triggers such as Sec 17/α-SNAP and/or synaptotagmin, which insert their apolar “wedge” domains into the bilayers, initiating the lipid rearrangements of fusion.

Publisher

American Society for Cell Biology (ASCB)

Subject

Cell Biology,Molecular Biology

Reference69 articles.

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

4. A minimal domain responsible for Munc13 activity

5. Dynamic binding mode of a Synaptotagmin-1–SNARE complex in solution

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