VAMPsynaptobreviini

VAMPsynaptobreviini is not a recognized term in standard molecular biology nomenclature. It appears to be a concatenation of VAMP (vesicle-associated membrane protein) and synaptobrevin, phrases used to describe a family of SNARE proteins essential for vesicle fusion. In authoritative databases, the proteins are typically referred to as synaptobrevin or VAMP, with members including VAMP1, VAMP2 (synaptobrevin-2), VAMP3 (cellubrevin), VAMP4, VAMP5, VAMP7 (TI-VAMP) and VAMP8 (endobrevin).

These proteins share a conserved structure featuring a SNARE motif and a single C-terminal transmembrane domain that anchors them to vesicle or target membranes. They participate in the formation of the SNARE complex with cognate Q-SNAREs on the target membrane, such as syntaxin-1 and SNAP-25 (or SNAP-23 in some non-neuronal cells), driving calcium-triggered membrane fusion necessary for releasing neurotransmitters, hormones, or enzymes.

Localization and function vary among family members. In neurons, VAMP2 is predominantly located on synaptic vesicles and is critical for evoked neurotransmitter release. VAMP1 is expressed in various brain regions; VAMP3 associates with recycling endosomes and receptor trafficking; other VAMPs function in secretory and endolysosomal pathways.

Clinical and research notes indicate that disruption of VAMP/SNARE function impairs vesicle fusion and neurotransmission. Mouse models lacking synaptobrevin-2 exhibit perinatal lethality due to severe defects in vesicular release. Altered expression of VAMP family members has been explored in neurological and developmental contexts, though the exact term VAMPsynaptobreviini is not used in standard literature.

See also: VAMP family, Synaptobrevin, SNARE complex, Syntaxin, SNAP-25.