Regulation of SNAP-25 trafficking and function by palmitoylation

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

Research output: Contribution to journalArticlepeer-review

16 Citations (Scopus)


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.
Original languageEnglish
Pages (from-to)163-166
Number of pages4
JournalBiochemical Society Transactions
Issue number1
Publication statusPublished - 2010


  • acyltransferases
  • animals
  • exocytosis
  • humans
  • lipoylation
  • protein transport
  • synaptosomal-associated protein 25


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