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A minK–HERG complex regulates the cardiac potassium current IKr

Author

Listed:
  • Thomas V. McDonald

    (Section of Molecular Cardiology, Albert Einstein College of Medicine)

  • Zhihui Yu

    (Section of Molecular Cardiology, Albert Einstein College of Medicine)

  • Zhen Ming

    (Section of Molecular Cardiology, Albert Einstein College of Medicine)

  • Eugen Palma

    (Section of Molecular Cardiology, Albert Einstein College of Medicine)

  • Marian B. Meyers

    (Section of Molecular Cardiology, Albert Einstein College of Medicine)

  • Ke-Wei Wang

    (The Boyer Center for Molecular Medicine, Yale University School of Medicine)

  • Steve A. N. Goldstein

    (The Boyer Center for Molecular Medicine, Yale University School of Medicine)

  • Glenn I. Fishman

    (Section of Molecular Cardiology, Albert Einstein College of Medicine)

Abstract

MinK is a widely expressed protein of relative molecular mass ∼15K that forms potassium channels by aggregation with other membrane proteins1,2,3. MinK governs ion channel activation4, regulation by second messengers5,6, and the function and structure of the ion conduction pathway7,8. Association of minK with a channel protein known as KvLQT1 produces a voltage-gated outward K+ current (IsK) resembling the slow cardiac repolarization current (IKs)9,10. HERG, a human homologue of the ether-a-go-go gene of the fruitfly Drosophila melanogaster, encodes a protein that produces the rapidly activating cardiac delayed rectifier (IKr)11,12. These two potassium currents, IKs and IKr, provide the principal repolarizing currents in cardiac myocytes for the termination of action potentials13,14. Although heterologously expressed HERG channels are largely indistinguishable from native cardiac IKr, a role for minK in this current is suggested by the diminished IKr in an atrial tumour line subjected to minK antisense suppression15. Here we show that HERG and minK form a stable complex, and that this heteromultimerization regulates IKr activity. MinK, through the formation of heteromeric channel complexes, is thus central to the control of the heart rate and rhythm.

Suggested Citation

  • Thomas V. McDonald & Zhihui Yu & Zhen Ming & Eugen Palma & Marian B. Meyers & Ke-Wei Wang & Steve A. N. Goldstein & Glenn I. Fishman, 1997. "A minK–HERG complex regulates the cardiac potassium current IKr," Nature, Nature, vol. 388(6639), pages 289-292, July.
  • Handle: RePEc:nat:nature:v:388:y:1997:i:6639:d:10.1038_40882
    DOI: 10.1038/40882
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    Cited by:

    1. Megan C. Lancaster & Hung-Hsin Chen & M. Benjamin Shoemaker & Matthew R. Fleming & Teresa L. Strickland & James T. Baker & Grahame F. Evans & Hannah G. Polikowsky & David C. Samuels & Chad D. Huff & D, 2024. "Detection of distant relatedness in biobanks to identify undiagnosed cases of Mendelian disease as applied to Long QT syndrome," Nature Communications, Nature, vol. 15(1), pages 1-10, December.

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