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 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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Animals
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Antigens, Surface / metabolism
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Brain / metabolism
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Carrier Proteins / genetics
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Carrier Proteins / metabolism
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Cell Membrane / metabolism
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Membrane Proteins / genetics
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Membrane Proteins / metabolism*
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N-Ethylmaleimide-Sensitive Proteins
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Nerve Tissue Proteins / metabolism*
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Protein Precursors / metabolism
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R-SNARE Proteins
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Rats
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Recombinant Proteins / metabolism
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Soluble N-Ethylmaleimide-Sensitive Factor Attachment Proteins
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Synaptosomal-Associated Protein 25
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Syntaxin 1
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Tetanus Toxin / chemistry
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Tetanus Toxin / pharmacology*
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Vesicular Transport Proteins*
Substances
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Antigens, Surface
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Carrier Proteins
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Membrane Proteins
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Nerve Tissue Proteins
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Protein Precursors
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R-SNARE Proteins
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Recombinant Proteins
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Snap25 protein, rat
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Soluble N-Ethylmaleimide-Sensitive Factor Attachment Proteins
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Synaptosomal-Associated Protein 25
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Syntaxin 1
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Tetanus Toxin
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Vesicular Transport Proteins
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N-Ethylmaleimide-Sensitive Proteins
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Nsf protein, rat