Synaptobrevin

  • OMIM: 185 881
  • UniProt: P63027

Synaptobrevine (isotypes 1-2 ) are small major membrane proteins of secretory vesicles with a molecular mass of 18 kDa. They belong to the family of vesicle- associated membrane protein ( VAMP ).

Synaptobrevin is one of the SNARE proteins involved in the formation of SNARE complexes. Of the four alpha helices of the SNARE core complex is set one of synaptobrevin, syntaxin and one of two from SNAP -25 ( in neurons ).

SNARE proteins are the core components of the molecular apparatus that drives the membrane fusion in exocytosis. Their function is also supported by various regulatory proteins, which are collectively referred to as SNARE -masters.

Since all proteins from the VAMP / synaptobrevin family share common structural properties, these are classified as R- SNAREs. An alternative classification (V- and t- SNAREs ) considered the origin of the synaptobrevin -bearing organelle in place of their structural properties.

Synaptobrevin plays an important role in the release of the neurotransmitter acetylcholine, and the associated excitation transfer in a motor end plate of nerve cells. Even the presence of a single molecule of botulinum toxin ( the strongest known poison) can split the synaptobrevin by its catalytic effect, as long as destroyed until the affected nerve cell. The tailed muscle fiber can thus irreversibly no longer be controlled and be reactivated only by formation of new nerve cells.

Synaptobrevin is also destroyed by tetanus toxin. This is produced by minor injuries from occurring tetanus bacteria taken up by peripheral nerves and retrogradely transported to the spinal cord.

For his research on synaptobrevin Cesare Montecucco the Paul Ehrlich and Ludwig Darmstaedter Prize for 2011 was awarded.

Protein isoform Human Genome Organisation SNARE (Protein) Neuromuscular junction The EMBO Journal Proceedings of the National Academy of Sciences of the United States of America Cell (journal)
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