Regulation of SNAP-25 trafficking and function by palmitoylation.
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.
Greaves
Jennifer
J
Centre for Integrative Physiology, School of Biomedical Sciences, University of Edinburgh, Hugh Robson Building, George Square, Edinburgh EH8 9XD, UK. J.Greaves@ed.ac.uk
Prescott
Gerald R
GR
Gorleku
Oforiwa A
OA
Chamberlain
Luke H
LH
D000217:Acyltransferases / Q000378:metabolism; D000818:Animals; D005089:Exocytosis / Q000502:physiology*; D006801:Humans; D054878:Lipoylation; D021381:Protein Transport / Q000502:physiology; D050825:Synaptosomal-Associated Protein 25 / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*
D050825:Synaptosomal-Associated Protein 25; D000217:Acyltransferases