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Regulation of SNAP-25 trafficking and function by palmitoylation

Research output: Contribution to journalArticlepeer-review

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Author(s)

Jennifer Greaves, Gerald R. Prescott, Oforiwa A. Gorleku, Luke H. Chamberlain

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Abstract

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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Original languageEnglish
Pages (from-to)163-166
Number of pages4
JournalBiochemical Society Transactions
Volume38
DOIs
Publication statusPublished - Feb 2010

    Research areas

  • 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), CYSTEINE-STRING PROTEIN, HUNTINGTIN-INTERACTING PROTEIN-14, PC12 CELLS, SNARE PROTEINS, LIPID RAFTS, RICH DOMAIN, MEMBRANE LOCALIZATION, SYNAPTIC VESICLES, PLASMA-MEMBRANE, EXOCYTOSIS

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