Control of eukaryotic membrane fusion by N-terminal domains of SNARE proteins

被引:40
作者
Dietrich, LEP [1 ]
Boeddinghaus, C [1 ]
LaGrassa, TJ [1 ]
Ungermann, C [1 ]
机构
[1] Univ Heidelberg, Zentrum Biochem, D-69120 Heidelberg, Germany
来源
BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR CELL RESEARCH | 2003年 / 1641卷 / 2-3期
基金
美国国家科学基金会;
关键词
SNARE; N-terminal domain; syntaxin; longin; SM protein; Vam7;
D O I
10.1016/S0167-4889(03)00094-6
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
SNARE proteins function at the center of membrane fusion reactions by forming complexes with each other via their coiled-coil domains. Several SNAREs have N-terminal domains (NTDs) that precede the coiled-coil domain and have critical functions in regulating the fusion cascade. This review will highlight recent findings on NTDs of syntaxins, the longin domain of VAMP proteins and SNAP-23/25 homologues in yeast. Biochemical and genetic experiments as well as the resolution of several NMR and crystal structures of SNARE NTDs shed light on their diverse function. (C) 2003 Elsevier B.V. All rights reserved.
引用
收藏
页码:111 / 119
页数:9
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