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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
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.
receptor tyrosine kinase; nonreceptor tyrosine kinase; protein
tyrosine phosphatase; integrins; cytoskeleton; K+ channel; Ca2+ channel; Cl channel; ligand-gated
channel; Na+ channel; receptor-activated channel; calcium
release-activated current; focal adhesion; growth factors; scaffolding
proteins; Src; Fyn; Lck; Hck; A kinase-associated protein; PDZ; SH2; SH3; CFTR; MAGUK
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