Fusion complex formation protects synaptobrevin against proteolysis by tetanus toxin light chain
作者： Lorenzo L. Pellegrini , Vincent O'Connor , Heinrich Betz
DOI: 10.1016/0014-5793(94)01070-6
关键词: Cell biology 、 Syntaxin 、 Synaptic vesicle 、 Vesicle 、 Exocytosis 、 Fusion protein 、 Membrane protein 、 Biochemistry 、 Synaptobrevin 、 Chemistry 、 SNAP25
摘要: Abstract The clostridial neurotoxin, tetanus toxin, is a Zn 2+ -dependent protease which inhibits neurotransmitter exocytosis by selective cleavage of the synaptic vesicle protein, synaptobrevin. Synaptobrevin thought to serve as receptor for two neuronal plasma membrane proteins, syntaxin and SNAP-25, in presence non-hydrolyzable ATP analogs form 20 S fusion complex with soluble proteins NSF α-SNAP. Here we show that synaptobrevin, when this complex, or its 7 precursor, protected against proteolysis enzymatically active toxin light chain. Our data define distinct pools provide markers different steps vesicle/plasma interaction.
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