At the junction of SNARE and SM protein function

被引：147

作者：

Carr, Chavela M. ^{[1
]}

Rizo, Josep ^{[2
,3
]}

机构：

[1] Texas A&M Univ, Dept Biochem & Biophys, College Stn, TX 77843 USA

[2] Univ Texas SW Med Ctr Dallas, Dept Biochem, Dallas, TX 75390 USA

[3] Univ Texas SW Med Ctr Dallas, Dept Pharmacol, Dallas, TX 75390 USA

来源：

CURRENT OPINION IN CELL BIOLOGY | 2010年 / 22卷 / 04期

基金：

美国国家卫生研究院;

关键词：

SYNAPTIC VESICLE FUSION; N-TERMINAL DOMAIN; MEDIATED MEMBRANE-FUSION; 3-DIMENSIONAL STRUCTURE; CLOSED CONFORMATION; NEUROTRANSMITTER RELEASE; TETHERING COMPLEXES; MUNC18-1; BINDING; MUN DOMAIN; SYNTAXIN;

D O I：

10.1016/j.ceb.2010.04.006

中图分类号：

Q2 [细胞生物学];

学科分类号：

071009 ; 090102 ;

摘要：

Sec1/Munc18 (SM) proteins bind to and function with soluble N-ethylmaleimide-sensitive factor attachment protein receptors (SNAREs) at each vesicle fusion site in the cell. The purpose for these interactions is becoming clearer, as what had been interpreted as functional divergence between SM proteins acting at different vesicle trafficking steps, or in specialized cells, is giving way to more recent evidence for common functions among all SM proteins. What is emerging is a picture of SM proteins acting not merely as SNARE regulators, but also as central components of the membrane fusion apparatus. The available data suggest sequential models that describe how the soluble SM protein might first regulate SNARE complex assembly and then cooperate with SNAREs to stimulate membrane fusion.

引用

页码：488 / 495

页数：8

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