Journal
BIOCHEMICAL SOCIETY TRANSACTIONS
Volume 38, Issue -, Pages 163-166Publisher
PORTLAND PRESS LTD
DOI: 10.1042/BST0380163
Keywords
acylation; aspartate-histidine-histidine-cysteine (DHHC) palmitoyltransferase; exocytosis; palmitoylation; 25 kDa synaptosome-associated protein (SNAP-25); soluble N-ethylmaleimide-sensitive fusion protein-attachment protein receptor (SNARE)
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Funding
- Medical Research Council [G0601597] Funding Source: researchfish
- Medical Research Council [G0601597] Funding Source: Medline
- MRC [G0601597] Funding Source: UKRI
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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.
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