FUSION COMPLEX-FORMATION PROTECTS SYNAPTOBREVIN AGAINST PROTEOLYSIS BY TETANUS TOXIN LIGHT-CHAIN

被引：44

作者：

PELLEGRINI, LL ^{[1
]}

OCONNOR, V ^{[1
]}

BETZ, H ^{[1
]}

机构：

[1] MAX PLANCK INST HIRNFORSCH,NEUROCHEM ABT,D-60528 FRANKFURT,GERMANY

来源：

FEBS LETTERS | 1994年 / 353卷 / 03期

关键词：

NEUROTRANSMITTER RELEASE; SYNAPTIC VESICLE; SYNAPTOBREVIN; TETANUS TOXIN; 20 S FUSION COMPLEX;

D O I：

10.1016/0014-5793(94)01070-6

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：

The clostridial neurotoxin, tetanus toxin, is a Zn2+-dependent protease which inhibits neurotransmitter exocytosis by selective cleavage of the synaptic vesicle protein, synaptobrevin. Synaptobrevin is thought to serve as a receptor for two neuronal plasma membrane proteins, syntaxin and SNAP-25, which in the presence of non-hydrolyzable ATP analogs form a 20 S fusion complex with the soluble fusion proteins NSF and alpha-SNAP. Here we show that synaptobrevin, when in this 20 S complex, or its 7 S precursor, is protected against proteolysis by the enzymatically active tetanus toxin light chain. Our data define distinct pools of synaptobrevin, which provide markers of different steps of vesicle/plasma membrane interaction.

引用

页码：319 / 323

页数：5

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