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Mol Biol Cell. 2017 Mar 15;28(6):707-711. doi: 10.1091/mbc.E16-07-0517.

A cascade of multiple proteins and lipids catalyzes membrane fusion.

Author information

1
Department of Biochemistry and Cell Biology, Geisel School of Medicine at Dartmouth, Hanover, NH 03755 Bill.Wickner@Dartmouth.edu) Jose.Rizo-Rey@UTSouthwestern.edu.
2
Departments of Biophysics, Biochemistry, and Biophysics, University of Texas Southwestern Medical Center, Dallas, TX 75390 Bill.Wickner@Dartmouth.edu) Jose.Rizo-Rey@UTSouthwestern.edu.

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.

PMID:
28292915
PMCID:
PMC5349777
DOI:
10.1091/mbc.E16-07-0517
[Indexed for MEDLINE]
Free PMC Article

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