SNARE-ing the structures of Sec1/Munc18 proteins

被引：28

作者：

Archbold, Julia K. ^{[1
]}

Whitten, Andrew E. ^{[1
]}

Hu, Shu-Hong ^{[1
]}

Collins, Brett M. ^{[2
]}

Martin, Jennifer L. ^{[1
]}

机构：

[1] Univ Queensland, Inst Mol Biosci, Div Chem & Struct Biol, St Lucia, Qld 4072, Australia

[2] Univ Queensland, Inst Mol Biosci, Mol Cell Biol Div, St Lucia, Qld 4072, Australia

来源：

CURRENT OPINION IN STRUCTURAL BIOLOGY | 2014年 / 29卷

基金：

澳大利亚国家健康与医学研究理事会;

关键词：

MUNC18-1; DOMAIN; 3A; SYNTAXIN N-PEPTIDE; PLASMA-MEMBRANE; BINDING MODE; COMPLEX; TRAFFICKING; FUSION; SEC1; CONFORMATION; RECRUITMENT;

D O I：

10.1016/j.sbi.2014.09.003

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Membrane fusion is essential for cellular transport in eukaryotes. Abnormalities contribute to a wide range of diseases including diabetes and neurological disorders. A key regulator of SNARE-mediated membrane fusion is the Sec1/Munc18 (SM) protein family. Universal structural features of SM proteins have been identified that affect the way these interact with their partner Syntaxin SNARE proteins. Whilst the molecular basis for SM-regulated SNARE complex formation has been extensively studied, it remains poorly understood. Recent crystal structures of SM proteins alone or in complex have provided new insight. Here we examine the available structural information on SM proteins for clues to how these enigmatic proteins might regulate SNARE complex assembly and membrane fusion.

引用

页码：44 / 51

页数：8

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