Regulation of potassium channels by protein kinases

Curr Opin Neurobiol. 1996 Jun;6(3):318-23. doi: 10.1016/s0959-4388(96)80114-0.


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.

Publication types

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

MeSH terms

  • Animals
  • Cell Membrane / metabolism
  • Enzyme Activation
  • Humans
  • Kinetics
  • Phosphorylation
  • Potassium Channels / metabolism
  • Potassium Channels / physiology*
  • Protein Kinases / physiology*
  • Serine / metabolism
  • Threonine / metabolism
  • Tyrosine / metabolism


  • Potassium Channels
  • Threonine
  • Tyrosine
  • Serine
  • Protein Kinases