A constitutively open potassium channel formed by KCNQ1 and KCNE3

Björn C. Schroeder, Siegfried Waldegger, Susanne Fehr, Markus Bleich, Richard Warth, Rainer Greger and Thomas J. Jentsch ()
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Björn C. Schroeder: Zentrum für Molekulare Neurobiologie Hamburg (ZMNH), Hamburg University
Siegfried Waldegger: Zentrum für Molekulare Neurobiologie Hamburg (ZMNH), Hamburg University
Susanne Fehr: Zentrum für Molekulare Neurobiologie Hamburg (ZMNH), Hamburg University
Markus Bleich: Physiologisches Institut der Albert-Ludwigs-Universität Freiburg
Richard Warth: Physiologisches Institut der Albert-Ludwigs-Universität Freiburg
Rainer Greger: Physiologisches Institut der Albert-Ludwigs-Universität Freiburg
Thomas J. Jentsch: Zentrum für Molekulare Neurobiologie Hamburg (ZMNH), Hamburg University

Nature, 2000, vol. 403, issue 6766, 196-199

Abstract: Abstract Mutations in all four known KCNQ potassium channel α-subunit genes lead to human diseases1,2,3,4,5,6. KCNQ1 (KvLQT1)1 interacts with the β-subunit KCNE1 (IsK, minK)7 to form the slow, depolarization-activated potassium current IKs8,9 that is affected in some forms of cardiac arrhythmia. Here we show that the novel β-subunit KCNE3 markedly changes KCNQ1 properties to yield currents that are nearly instantaneous and depend linearly on voltage. It also suppresses the currents of KCNQ4 and HERG potassium channels. In the intestine, KCNQ1 and KCNE3 messenger RNAs colocalized in crypt cells. This localization and the pharmacology, voltage-dependence and stimulation by cyclic AMP of KCNQ1/KCNE3 currents indicate that these proteins may assemble to form the potassium channel that is important for cyclic AMP-stimulated intestinal chloride secretion and that is involved in secretory diarrhoea and cystic fibrosis.

Date: 2000
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DOI: 10.1038/35003200

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