Regulation of excitatory and inhibitory neurotransmitter-gated ion channels by protein phosphorylation

Curr Opin Neurobiol. 1997 Jun;7(3):358-67. doi: 10.1016/s0959-4388(97)80063-3.


Phosphorylation of ligand-gated ion channels is recognised as a potentially important mechanism for short- and long-term modulation of ion-channel function. Following the discovery of numerous sites of phosphorylation on ligand-gated ion channel proteins, recent studies have demonstrated that neurotransmitter-induced activation of serine/threonine, tyrosine and other kinases can result in the modulation of glutamate, type A gamma-aminobutyric acid (GABAA) and glycine receptors. These findings may have important consequences for our understanding of synaptic transmission and neuronal excitability.

Publication types

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

MeSH terms

  • Animals
  • Ion Channels / metabolism
  • Ion Channels / physiology*
  • Neurotransmitter Agents / metabolism*
  • Neurotransmitter Agents / physiology*
  • Phosphorylation
  • Protein Kinases / physiology*
  • Protein-Tyrosine Kinases / metabolism
  • Receptors, GABA-A / physiology
  • Receptors, Glycine / physiology
  • Receptors, N-Methyl-D-Aspartate / physiology


  • Ion Channels
  • Neurotransmitter Agents
  • Receptors, GABA-A
  • Receptors, Glycine
  • Receptors, N-Methyl-D-Aspartate
  • Protein Kinases
  • Protein-Tyrosine Kinases