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

共 25 条

[21] VAMP-1 - A SYNAPTIC VESICLE-ASSOCIATED INTEGRAL MEMBRANE-PROTEIN [J].

TRIMBLE, WS ;

COWAN, DM ;

SCHELLER, RH .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1988, 85 (12) :4538-4542

[22] SNAP FAMILY OF NSF ATTACHMENT PROTEINS INCLUDES A BRAIN-SPECIFIC ISOFORM [J].

WHITEHEART, SW ;

GRIFF, IC ;

BRUNNER, M ;

CLARY, DO ;

MAYER, T ;

BUHROW, SA ;

ROTHMAN, JE .

NATURE, 1993, 362 (6418) :353-355

[23] IDENTIFICATION AND LOCALIZATION OF SYNAPTOPHYSIN, AN INTEGRAL MEMBRANE GLYCOPROTEIN OF MR 38,000 CHARACTERISTIC OF PRESYNAPTIC VESICLES [J].

WIEDENMANN, B ;

FRANKE, WW .

CELL, 1985, 41 (03) :1017-1028

[24]

YAMASAKI S, 1994, J BIOL CHEM, V269, P12764

[25]

YOSHIDA A, 1992, J BIOL CHEM, V267, P24925

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