Premium
Fusion complex formation protects synaptobrevin against proteolysis by tetanus toxin light chain
Author(s) -
Pellegrini Lorenzo L.,
O'Connor Vincent,
Betz Heinrich
Publication year - 1994
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(94)01070-6
Subject(s) - synaptobrevin , proteolysis , exocytosis , snap25 , biochemistry , chemistry , synaptic vesicle , vesicle fusion , toxin , snare complex , protease , neurotoxin , lipid bilayer fusion , biology , microbiology and biotechnology , biophysics , vesicle , enzyme , membrane
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 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.