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

17 Citations (Scopus)

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.

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

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)
  • 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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