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A constitutively open potassium channel formed by KCNQ1 and KCNE3

Author

Listed:
  • 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)

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.

Suggested Citation

  • Björn C. Schroeder & Siegfried Waldegger & Susanne Fehr & Markus Bleich & Richard Warth & Rainer Greger & Thomas J. Jentsch, 2000. "A constitutively open potassium channel formed by KCNQ1 and KCNE3," Nature, Nature, vol. 403(6766), pages 196-199, January.
    • Handle: RePEc:nat:nature:v:403:y:2000:i:6766:d:10.1038_35003200
    DOI: 10.1038/35003200
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    Cited by:

    1. Karen Mruk & William R Kobertz, 2009. "Discovery of a Novel Activator of KCNQ1-KCNE1 K+ Channel Complexes," PLOS ONE, Public Library of Science, vol. 4(1), pages 1-9, January.
    2. Kamilla Kelemen & Ian D. Greener & Xiaoping Wan & Shankar Parajuli & J. Kevin Donahue, 2022. "Heterogeneous repolarization creates ventricular tachycardia circuits in healed myocardial infarction scar," Nature Communications, Nature, vol. 13(1), pages 1-14, December.
    3. Katrien Willegems & Jodene Eldstrom & Efthimios Kyriakis & Fariba Ataei & Harutyun Sahakyan & Ying Dou & Sophia Russo & Filip Petegem & David Fedida, 2022. "Structural and electrophysiological basis for the modulation of KCNQ1 channel currents by ML277," Nature Communications, Nature, vol. 13(1), pages 1-17, December.

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