Abstract

Syntaxin-1A and SNAP25 form the receptor component of the SNARE complex, which has been shown to be the minimal machinery for membrane fusion. In vivo studies have revealed that syntaxin-1A exists in cholesterol-dependent clusters that are distinct from lipid rafts. Additionally, SNARE-mediated membrane fusion has been shown to be stimulated by regulatory lipids, such as phosphatidylinositol 4,5-bisphosphate (PI-4,5-P2). An appreciation of the lipid-protein interactions which define syntaxin clustering dynamics is essential to understand the membrane role in organization of SNARE-mediated membrane fusion.

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