Fusion complex formation protects synaptobrevin against proteolysis by tetanus toxin light chain

FEBS Letters

Pellegrini, Lorenzo L.¹  Betz, Heinrich¹  O'Connor, Vincent¹ 

[1] Abteilung Neurochemie, Max-Planck-Institut für Hirnforschung, Deutschordenstr. 46, D-60528 Frankfurt/Main, Germany

关键词: Neurotransmitter release;    Synaptic vesicle;    Synaptobrevin;    Tetanus toxin;    20 S fusion complex;    NSF;    N-ethylmaleimide-sensitive fusion protein;    SDS-PAGE;    sodium dodecylsulfate polyacrylamide gel-electrophoresis;    SNAP;    soluble NSF attachment protein;    SNAP-25;    synaptosomal associated protein of 25 kDa;    SNARE;    SNAP receptor;   

DOI  :  10.1016/0014-5793(94)01070-6

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 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 α-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.

【 授权许可】

Unknown