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.
- protein transport
- synaptosomal-associated protein 25
Greaves, J., Prescott, G. R., Gorleku, O. A., & Chamberlain, L. H. (2010). Regulation of SNAP-25 trafficking and function by palmitoylation. Biochemical Society Transactions, 38(1), 163-166. https://doi.org/10.1042/BST0380163