Ion channel regulation by protein palmitoylation

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


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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Animals
  • Humans
  • Ion Channel Gating / physiology*
  • Ion Channels / physiology*
  • Lipoylation / physiology*
  • Protein Modification, Translational / physiology*
  • Protein S / metabolism*
  • Signal Transduction / physiology*


  • Ion Channels
  • Protein S