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Science 295 (5554): 496-499

Copyright © 2002 by the American Association for the Advancement of Science

Requirement of a Macromolecular Signaling Complex for beta  Adrenergic Receptor Modulation of the KCNQ1-KCNE1 Potassium Channel

Steven O. Marx,* Junko Kurokawa,* Steven Reiken, Howard Motoike, Jeanine D'Armiento, Andrew R. Marks, Robert S. Kassdagger

Sympathetic nervous system (SNS) regulation of cardiac action potential duration (APD) is mediated by beta  adrenergic receptor (beta AR) activation, which increases the slow outward potassium ion current (IKS). Mutations in two human IKS channel subunits, hKCNQ1 and hKCNE1, prolong APD and cause inherited cardiac arrhythmias known as LQTS (long QT syndrome). We show that beta AR modulation of IKS requires targeting of adenosine 3',5'-monophosphate (cAMP)-dependent protein kinase (PKA) and protein phosphatase 1 (PP1) to hKCNQ1 through the targeting protein yotiao. Yotiao binds to hKCNQ1 by a leucine zipper motif, which is disrupted by an LQTS mutation (hKCNQ1-G589D). Identification of the hKCNQ1 macromolecular complex provides a mechanism for SNS modulation of cardiac APD through IKS.

Department of Pharmacology, Center for Molecular Cardiology, Department of Medicine, College of Physicians and Surgeons of Columbia University, New York, NY 10032, USA.
*   These authors contributed equally to this report.

dagger    To whom correspondence should be addressed. E-mail: rsk20{at}columbia.edu

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Cardiovasc Res 70, 466-474
   Abstract »    Full Text »    PDF »
A New Role for Calmodulin in Ion Channel Biology.
D. M. Roden (2006)
Circ. Res. 98, 979-981
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Compartmentation of Cyclic Nucleotide Signaling in the Heart: The Role of A-Kinase Anchoring Proteins.
K. L. Dodge-Kafka, L. Langeberg, and J. D. Scott (2006)
Circ. Res. 98, 993-1001
   Abstract »    Full Text »    PDF »
KCNQ1 Assembly and Function Is Blocked by Long-QT Syndrome Mutations That Disrupt Interaction With Calmodulin.
S. Ghosh, D. A. Nunziato, and G. S. Pitt (2006)
Circ. Res. 98, 1048-1054
   Abstract »    Full Text »    PDF »
Calmodulin Is Essential for Cardiac IKS Channel Gating and Assembly: Impaired Function in Long-QT Mutations.
L. Shamgar, L. Ma, N. Schmitt, Y. Haitin, A. Peretz, R. Wiener, J. Hirsch, O. Pongs, and B. Attali (2006)
Circ. Res. 98, 1055-1063
   Abstract »    Full Text »    PDF »
Identification by mass spectrometry and functional characterization of two phosphorylation sites of KCNQ2/KCNQ3 channels.
T. S. Surti, L. Huang, Y. N. Jan, L. Y. Jan, and E. C. Cooper (2005)
PNAS 102, 17828-17833
   Abstract »    Full Text »    PDF »
The KCNQ1 Potassium Channel: From Gene to Physiological Function.
T. Jespersen, M. Grunnet, and S.-P. Olesen (2005)
Physiology 20, 408-416
   Abstract »    Full Text »    PDF »
Molecular Physiology of Cardiac Repolarization.
J. M. Nerbonne and R. S. Kass (2005)
Physiol Rev 85, 1205-1253
   Abstract »    Full Text »    PDF »
Phosphorylation of the A-kinase-anchoring Protein Yotiao Contributes to Protein Kinase A Regulation of a Heart Potassium Channel.
L. Chen, J. Kurokawa, and R. S. Kass (2005)
J. Biol. Chem. 280, 31347-31352
   Abstract »    Full Text »    PDF »

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