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

Ion channel regulation by protein palmitoylation

Michael J Shipston  1
Affiliations
Review

Ion channel regulation by protein palmitoylation

Michael J Shipston. J Biol Chem. .

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.

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Figures

FIGURE 1.
FIGURE 1.
Reversible protein palmitoylation and regulation of the ion channel life cycle. a, schematic illustrating reversible protein palmitoylation. Palmitoylation is controlled by a family of acyl palmitoyltransferases (zDHHCs), and depalmitoylation is controlled by a limited number of thioesterases. b, palmitoylation controls multiple steps in the life cycle of an ion channel that include assembly (step 1), maturation (step 2), control of Golgi exit/sorting (step 3) and trafficking (step 4), insertion in the plasma membrane (step 5), clustering and localization in membrane microdomains (step 6), determination of activity regulation by other signaling pathways (step 7), internalization (step 8), recycling (step 9), and degradation (step 10).
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