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J Biol Chem. 2011 Mar 18;286(11):8709-16. doi: 10.1074/jbc.R110.210005. Epub 2011 Jan 7.

Ion channel regulation by protein palmitoylation.

Author information

1
Centre for Integrative Physiology, College of Medicine and Veterinary Medicine, University of Edinburgh, Edinburgh EH8 9XD, Scotland, United Kingdom. mike.shipston@ed.ac.uk

Abstract

Protein S-palmitoylation, the reversible thioester linkage of a 16-carbon palmitate lipid to an intracellular cysteine residue, is rapidly emerging as a fundamental, dynamic, and widespread post-translational mechanism to control the properties and function of ligand- and voltage-gated ion channels. Palmitoylation controls multiple stages in the ion channel life cycle, from maturation to trafficking and regulation. An emerging concept is that palmitoylation is an important determinant of channel regulation by other signaling pathways. The elucidation of enzymes controlling palmitoylation and developments in proteomics tools now promise to revolutionize our understanding of this fundamental post-translational mechanism in regulating ion channel physiology.

PMID:
21216969
PMCID:
PMC3058972
DOI:
10.1074/jbc.R110.210005
[Indexed for MEDLINE]
Free PMC Article

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