Synaptic vesicle fusion protein

Synaptic vesicle fusion proteins are a group of proteins—most notably the SNARE complex (comprising synaptobrevin/VAMP on the vesicle membrane and syntaxin-1 plus SNAP-25 on the presynaptic plasma membrane)—that catalyze the fusion of neurotransmitter-containing synaptic vesicles with the presynaptic membrane in response to neuronal activation[3][4][5][1]. This fusion is dependent on calcium influx, which is sensed primarily by synaptotagmin, and is tightly regulated by several proteins, including Munc18 and complexin[8][4]. The core role of these proteins is to bring the vesicle membrane and plasma membrane into close proximity and supply the energy required for merger, thus enabling neurotransmitter release and communication between neurons[3][4][5][7]. Pathologically, these proteins are targets for clostridial neurotoxins (botulinum, tetanus), which disrupt neurotransmission by proteolytic cleavage of SNAREs[3][5]. SNARE complex function is essential for central nervous system integrity, and alterations have been implicated in neurodegenerative and certain neurodevelopmental disorders[5][9].

Other names

SNARE proteinsvesicular SNARE (v-SNARE)target-membrane SNARE (t-SNARE)soluble N-ethylmaleimide-sensitive factor attachment protein receptorsyntaxinSNAP-25synaptobrevinVAMPsynaptic fusion machinery

Inhibition of vesicle fusion via cleavage of SNARE proteins (botulinum and tetanus neurotoxins)