Regulation of SNAP-25 trafficking and function by palmitoylation

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Greaves, Jennifer and Prescott, Gerald R and Gorleku, Oforiwa A and Chamberlain, Luke H (2010) Regulation of SNAP-25 trafficking and function by palmitoylation. Biochemical Society Transactions, 38 (1). pp. 163-166. (https://doi.org/10.1042/BST0380163)

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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.

ORCID iDs

Greaves, Jennifer ORCID logoORCID: https://orcid.org/0000-0001-8445-789X, Prescott, Gerald R, Gorleku, Oforiwa A and Chamberlain, Luke H ORCID logoORCID: https://orcid.org/0000-0002-8701-4995;
CORE (COnnecting REpositories)