Three SNARE complexes cooperate to mediate membrane fusion

被引：150

作者：

Hua, YY ^{[1
]}

Scheller, RH ^{[1
]}

机构：

[1] Stanford Univ, Sch Med, Howard Hughes Med Inst, Dept Cellular & Mol Physiol, Stanford, CA 94305 USA

来源：

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 2001年 / 98卷 / 14期

关键词：

D O I：

10.1073/pnas.131214798

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

Soluble M-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) proteins of the syntaxin, SNAP-25, and VAMP families mediate intracellular membrane fusion through the formation of helical bundles that span opposing membranes. Soluble SNARE domains that lack their integral membrane anchors inhibit membrane fusion by forming nonfunctional complexes with endogenous SNARE proteins. In this study we investigate the dependence of membrane fusion on the concentration of a soluble SNARE coil domain derived from VAMP2, The increase in the inhibition of fusion observed with increasing concentration of inhibitor is best fit to a function that suggests three SNARE complexes cooperate to mediate fusion of a single vesicle. These three complexes likely contribute part of a protein and lipidic fusion pore.

引用

页码：8065 / 8070

页数：6

共 28 条

[1] A SNARE complex mediating fusion of late endosomes defines conserved properties of SNARE structure and function [J].