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PMID: 11157167 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Control of fusion pore dynamics during exocytosis by Munc18.

Science (New York, N.Y.) ·Vol. 291 ·No. 5505 ·2001-02-02 ·Pages 875-8

Fisher RJ, Pevsner J, Burgoyne RD

Abstract

Intracellular membrane fusion is mediated by the SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins. All vesicle transport steps also have an essential requirement for a member of the Sec1 protein family, including the neuronal Munc18-1 (also known as nSec1) in regulated exocytosis. Here, in adrenal chromaffin cells, we expressed a Munc18 mutant with reduced affinity for syntaxin, which specifically modified the kinetics of single-granule exocytotic release events, consistent with an acceleration of fusion pore expansion. Thus, Munc18 functions in a late stage in the fusion process, where its dissociation from syntaxin determines the kinetics of postfusion events.

MeSH Terms
Action Potentials Adrenal Medulla/cytology Animals Antigens, Surface/metabolism Catecholamines/metabolism Cattle Cells, Cultured Chromaffin Cells/physiology Exocytosis Membrane Fusion Munc18 Proteins Mutation Nerve Tissue Proteins/genetics,metabolism PC12 Cells Phosphorylation Rats Secretory Vesicles/physiology Syntaxin 1 Transfection Vesicular Transport Proteins
Chemicals
Antigens, Surface Catecholamines Munc18 Proteins Nerve Tissue Proteins Stxbp1 protein, rat Syntaxin 1 Vesicular Transport Proteins
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Fisher R J
Physiological Laboratory, University of Liverpool, Crown Street, Liverpool, L69 3BX, UK.
Pevsner J
Burgoyne R D
Article Info
Journal
Science (New York, N.Y.)
Abbr.
Science
ISSN
0036-8075
Published
2001-02-02
Pages
875-8
Language
English
Region
United States
NLM ID
0404511
Subset
IM
Grants
NINDS NIH HHS · R01 NS36670-01A1 · United States
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