Synaptic Vesicle Antibody Sampler Kit #8630

Fusion of a vesicle to its target membrane is a universal process in eukaryotic cells for proper cellular organization and function. Several protein-protein interactions are essential to membrane fusion during endocytosis. Membrane fusion requires interaction among SNARE1 proteins associated with both donor and acceptor membranes (1,2). SNAP25 forms a core complex with the SNARE proteins syntaxin and synaptobrevin to mediate synaptic vesicle fusion with the plasma membrane during Ca²⁺-dependent exocytosis (3). Syntaxin 6 is a ubiquitously expressed S25C family member of the SNARE proteins (4,5). Munc18-1 acts as a molecular chaperone for syntaxin-1, allowing for formation of the SNARE complex at the plasma membrane (6). Following membrane fusion, the α-SNAP cytoplasmic adapter protein binds to the SNARE complex. N-ethylmaleimide-sensitive factor (NSF), a hexameric ATPase, then associates with the α-SNAP/SNARE complex to mediate SNARE disassembly during membrane fusion (7,8). The ATPase activity of NSF induces a conformational change in the α-SNAP/SNARE complex that leads to its dissociation from the membrane, membrane fusion, and eventual recycling of the SNARE complex for subsequent membrane fusion (7,8).