Journal
AMERICAN JOURNAL OF PHYSIOLOGY-HEART AND CIRCULATORY PHYSIOLOGY
Volume 281, Issue 5, Pages H1835-H1862Publisher
AMER PHYSIOLOGICAL SOC
DOI: 10.1152/ajpheart.2001.281.5.H1835
Keywords
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
Funding
- NHLBI NIH HHS [HL-60180, HL-46502] Funding Source: Medline
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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.
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