title: Regulation of potassium channels by protein kinases.
abstract: Studies of the role of protein phosphorylation in the modulation of neuronal excitability are beginning to identify specific sites on ion channels that are substrates for serine/threonine kinases and that contribute to short-term and long-term regulation of current amplitude and kinetics. In addition, it is becoming apparent that phosphorylation of tyrosine residues may produce acute changes in the characteristics of ion channels. These recent findings are best illustrated by examining the Shaker superfamily of potassium channels.
authors.affiliation: Department of Pharmacology, Yale University School of Medicine, 333 Cedar Street, New Haven, Connecticut 06520, USA.
authors.forename: E A
authors.initials: EA
authors.lastname: Jonas
authors.forename: L K
authors.initials: LK
authors.lastname: Kaczmarek
mesh_terms: D000818:Animals; D002462:Cell Membrane / Q000378:metabolism; D004789:Enzyme Activation; D006801:Humans; D007700:Kinetics; D010766:Phosphorylation; D015221:Potassium Channels / Q000378:metabolism / Q000502:physiology*; D011494:Protein Kinases / Q000502:physiology*; D012694:Serine / Q000378:metabolism; D013912:Threonine / Q000378:metabolism; D014443:Tyrosine / Q000378:metabolism
chemical_list: D015221:Potassium Channels; D013912:Threonine; D014443:Tyrosine; D012694:Serine; D011494:Protein Kinases