NSF

Trimeric ATPase required for membrane fusion during vesicular transport

General Information

N-ethylamide sensitive fusion protein NSF functions together with SNAPs (soluble NSF attachment proteins) and SNAREs (SNAP receptors) in vesicular transport.
NSF is a homotrimer whose polypeptide subunits are made up of three distinct domains: an amino - terminal domain (N) and two homologous ATP-binding domains (D1 and D2). NSF is an ATPase that dissociates SNARE complexes, such as the core complex composed of synaptobrevin/VAMP, syntaxin 1 and SNAP 25 under ATP hydrolysis. The ability of the D1 domain to hydrolyze ATP is required for NSF activity. The D2 domain is required for trimerization, but its ability to hydrolyze ATP is not absolutely required for NSF function.