About VAMP / Synaptobrevin:
Synaptobrevins (synaptobrevin isotypes 1-2) belong to the vesicle-associated membrane protein (VAMP) family. They are small integral membrane proteins of secretory vesicles. Synaptobrevin is one of the SNAP REceptor (SNARE) proteins used in exocytosis.
Mutations in the VAMP proteins are associated with neurodevelopmental disorders. These include autism, epilepsy, movement disorders, and synaptopathy.
As one of the SNARE proteins, the main function of Synaptobrevin is to mediate the fusion of vesicles with the target membrane. This is mainly through exocytosis. The SNARE proteins can, however, also mediate the fusion of vesicles with membrane-bound compartments, for example, lysosomes.
For clinical (and cosmetic) reasons, most attention has been paid to the SNARES that mediate the neurotransmitter release of synaptic vesicles in neurons. This includes Synaptobrevin. This protein is known to be degraded by tetanospasmin. Tetanospasmin is derived from Clostridium tetani. This is the bacteria that causes tetanus.
In the cosmetic field (and, to some extent, the medical one) Synaptobrevin is also noted as being a target for the botulinum toxin. This is produced by the Clostridium botulinum, itself a relative of the Clostridium tetani bacterium.
Synaptobrevin is structured as an α-helix (Alpha helix). This type of structure is also known as a 3.613-helix. Synaptobrevin forms one of the four α-helices in the SNARE complex. The other three are syntaxin (one) and SNAP-25 (two, in neurons).
Synaptobrevin is best known for its interaction with Synaptophysin. This interaction promotes the formation of functional SNARE complexes. It, therefore, plays a key role in modulating synaptic efficiency.
Synaptobrevin is present in several human proteins. These are: