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

by: Trevor G Smart

Current Opinion in Neurobiology, Vol. 7, No. 3. (June 1997), pp. 358-367.

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Abstract

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.

@article{citeulike:2823196, abstract = {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.}, author = {Smart, Trevor G. }, citeulike-article-id = {2823196}, doi = {10.1016/S0959-4388(97)80063-3}, journal = {Current Opinion in Neurobiology}, keywords = {anatomical, cascade, neuron, neurotrasmitters}, month = {June}, number = {3}, pages = {358--367}, posted-at = {2008-05-22 16:00:37}, priority = {2}, title = {Regulation of excitatory and inhibitory neurotransmitter-gated ion channels by protein phosphorylation}, url = {http://dx.doi.org/10.1016/S0959-4388(97)80063-3}, volume = {7}, year = {1997} }

RIS record

TY - JOUR ID - citeulike:2823196 L3 - citeulike-article-id:2823196 TI - Regulation of excitatory and inhibitory neurotransmitter-gated ion channels by protein phosphorylation JF - Current Opinion in Neurobiology VL - 7 IS - 3 SP - 358 EP - 367 N2 - 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. KW - anatomical KW - cascade KW - neuron KW - neurotrasmitters AU - Smart, Trevor PY - 1997/06// UR - http://dx.doi.org/10.1016/S0959-4388(97)80063-3 ER -

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