Regulation of ion channels by protein tyrosine phosphorylation

Author:

Davis Michael J.1,Wu Xin1,Nurkiewicz Timothy R.1,Kawasaki Junya1,Gui Peichun1,Hill Michael A.2,Wilson Emily1

Affiliation:

1. Department of Medical Physiology, Cardiovascular Research Institute, Texas A&M University System Health Science Center, College Station, Texas 77845; and

2. Department of Human Biology, Royal Melbourne Institute of Technology University, Bundoora, Victoria 3083, Australia

Abstract

Ion channels are regulated by protein phosphorylation and dephosphorylation of serine, threonine, and tyrosine residues. Evidence for the latter process, tyrosine phosphorylation, has increased substantially since this topic was last reviewed. In this review, we present a comprehensive summary and synthesis of the literature regarding the mechanism and function of ion channel regulation by protein tyrosine kinases and phosphatases. Coverage includes the majority of voltage-gated, ligand-gated, and second messenger-gated channels as well as several types of channels that have not yet been cloned, including store-operated Ca2+ channels, nonselective cation channels, and epithelial Na+ and Cl channels. Additionally, we discuss the critical roles that channel-associated scaffolding proteins may play in localizing protein tyrosine kinases and phosphatases to the vicinity of ion channels.

Publisher

American Physiological Society

Subject

Physiology (medical),Cardiology and Cardiovascular Medicine,Physiology

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