This review highlights the role of protein phosphorylation in regulating the function and kinetics of potassium channels, providing mechanistic insights into neuronal excitability.
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May inform models of cardiac excitability; leaves open whether kinase targeting alters arrhythmia risk.
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.
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Jonas et al. (1996) studied this question.
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