The SNARE (soluble N-ethylmaleimide-sensitive fusion protein-attachment protein receptor) protein SNAP-25 (25 kDa synaptosome-associated protein) is essential for regulated exocytosis in neuronal and neuroendocrine cells. Whereas the majority of SNARE proteins contain transmembrane domains, SNAP-25 is instead anchored to membranes by the palmitoylation of a central cysteine-rich region. In this review, we discuss the mechanisms of SNAP-25 palmitoylation and how this modification regulates the intracellular trafficking and exocytotic function of this essential protein.
Regulation of SNAP-25 trafficking and function by palmitoylation
Jennifer Greaves, Gerald R. Prescott, Oforiwa A. Gorleku, Luke H. Chamberlain; Regulation of SNAP-25 trafficking and function by palmitoylation. Biochem Soc Trans 1 February 2010; 38 (1): 163–166. doi: https://doi.org/10.1042/BST0380163
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