Regulation of excitatory and inhibitory neurotransmitter-gated ion channels by protein phosphorylation.
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.
Smart
T G
TG
Department of Pharmacology, School of Pharmacy, 29-39 Brunswick Square, London, WC1N 1AX, UK. tsmart@ulsop.ac.uk
D000818:Animals; D007473:Ion Channels / Q000378:metabolism / Q000502:physiology*; D018377:Neurotransmitter Agents / Q000378:metabolism* / Q000502:physiology*; D010766:Phosphorylation; D011494:Protein Kinases / Q000502:physiology*; D011505:Protein-Tyrosine Kinases / Q000378:metabolism; D011963:Receptors, GABA-A / Q000502:physiology; D018009:Receptors, Glycine / Q000502:physiology; D016194:Receptors, N-Methyl-D-Aspartate / Q000502:physiology
D007473:Ion Channels; D018377:Neurotransmitter Agents; D011963:Receptors, GABA-A; D018009:Receptors, Glycine; D016194:Receptors, N-Methyl-D-Aspartate; D011494:Protein Kinases; D011505:Protein-Tyrosine Kinases