The riddle of the Sec1/Munc-18 proteins - new twists added to their interactions with SNAREs

被引：72

作者：

Gallwitz, D

Jahn, R

机构：

[1] Max Planck Inst Biophys Chem, Dept Mol Genet, D-37070 Gottingen, Germany

[2] Max Planck Inst Biophys Chem, Dept Neurobiol, D-37070 Gottingen, Germany

来源：

TRENDS IN BIOCHEMICAL SCIENCES | 2003年 / 28卷 / 03期

关键词：

D O I：

10.1016/S0968-0004(03)00028-8

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：

Sec1/Munc-18 (SM) proteins are essential for intracellular membrane fusion reactions. Most of them bind to membrane-associated soluble N-ethylmaleimide-sensitive fusion (NSF)-attachment protein receptors (SNAREs) of the syntaxin subfamily but it is unclear whether regulating syntaxins is their primary role. Recent studies now have shown that the mechanism of syntaxin binding is not conserved, even though the structures of both protein families are. Amazing as this might be for those considering the evolution of conserved folds, it leaves the question of how SM proteins operate in membrane fusion unanswered.

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页码：113 / 116

页数：4

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