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PMID: 8794088 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S. Review

Regulation of potassium channels by protein kinases.

Current opinion in neurobiology ·Vol. 6 ·No. 3 ·1996-06-00 ·Pages 318-23

Jonas EA, Kaczmarek LK

Abstract

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.

MeSH Terms
Animals Cell Membrane/metabolism Enzyme Activation Humans Kinetics Phosphorylation Potassium Channels/metabolism,physiology Protein Kinases/physiology Serine/metabolism Threonine/metabolism Tyrosine/metabolism
Chemicals
Potassium Channels Threonine Tyrosine Serine Protein Kinases
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Jonas E A
Department of Pharmacology, Yale University School of Medicine, 333 Cedar Street, New Haven, Connecticut 06520, USA.
Kaczmarek L K
Article Info
Journal
Current opinion in neurobiology
Abbr.
Curr Opin Neurobiol
ISSN
0959-4388
Published
1996-06-00
Pages
318-23
Language
English
Region
England
NLM ID
9111376
Subset
IM
Grants
NIDCD NIH HHS · DC-01919 · United States
NIGMS NIH HHS · GM-48851 · United States
NINDS NIH HHS · NS018492 · United States
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