Soluble NSF attachment protein

Soluble NSF attachment proteins (SNAP, or Sec17p in yeast) are proteins involved in membrane fusion, where they recycle key tethering components after each fusion event. After membrane fusion, the tethering SNARE proteins remain tightly bound to each other. SNAPs bind to the SNARE complex and recruit the soluble ATPase NSF. NSF provides the energy to untangle the SNARE complex, allowing it to be recycled for future fusion events.[1] Mammals have three SNAP genes: α-SNAP, β-SNAP, and γ-SNAP. α- and γ-SNAP are expressed throughout the body, while β-SNAP is specific to the brain.[2]

SNAP proteins were identified by James Rothman's laboratory group in 1990.[2][3]

References
  1. Bonifacino JS, Glick BS (January 2004). "The mechanisms of vesicle budding and fusion". Cell. 116 (2): 153–166. doi:10.1016/S0092-8674(03)01079-1.
  2. Stenbeck, G. (May 1998). "Soluble NSF-attachment proteins". Int J Biochem Cell Biol. 30 (5): 573–7. doi:10.1016/S1357-2725(97)00064-2. PMID 9693958.
  3. Clary DO, Griff IC, Rothman JE (May 1990). "SNAPs, a family of NSF attachment proteins involved in intracellular membrane fusion in animals and yeast". Cell. 61: 709–721.


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