P23763, P63027, Q15836

Syntaxins were originally thought to be docking proteins, but have more recently been categorized as anchoring proteins that anchor themselves to the cytoplasmic surfaces of cellular membranes. Syntaxins have been shown to bind to various proteins involved in exocytosis, including VAMPs (vesicle-associated membrane proteins), NSF (N-ethylmaleimide-sensitive factor), SNAP 25 (synaptosomal-associated protein of 25 kDa), SNAPs (soluble NSF attachment proteins) and synaptotagmin. VAMPs, also designated synaptobrevins, including VAMP-1 and VAMP-2, and synaptotagmin, a protein that may function as an inhibitor of exocytosis, are vesicular proteins. SNAPs, including a- and g-SNAP, are cytoplasmic proteins that bind to a membrane receptor complex composed of VAMP, SNAP 25 and Syntaxin. SNAPs mediate the membrane binding of NSF, which is essential for membrane fusion reactions. An additional protein designated synaptophysin may regulate exo-cytosis by competing with SNAP 25 and syntaxins for VAMP binding.