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Potassium channel TASK-5 forms functional heterodimers with TASK-1 and TASK-3 to break its silence

Author

Listed:
  • Susanne Rinné

    (Philipps University Marburg)

  • Florian Schick

    (Philipps University Marburg)

  • Kirsty Vowinkel

    (Philipps University Marburg)

  • Sven Schütte

    (Philipps University Marburg)

  • Cornelius Krasel

    (Philipps-University Marburg)

  • Silke Kauferstein

    (Goethe‐University
    Partner Site Rhein‐Main)

  • Martin K.-H. Schäfer

    (Philipps University Marburg)

  • Aytug K. Kiper

    (Philipps University Marburg)

  • Thomas Müller

    (Pharmaceuticals)

  • Niels Decher

    (Philipps University Marburg)

Abstract

TASK-5 (KCNK15) belongs to the acid-sensitive subfamily of two-pore domain potassium (K2P) channels, which includes TASK-1 and TASK-3. TASK-5 stands out as K2P channel for which there is no functional data available, since it was reported in 2001 as non-functional and thus “silent”. Here we show that TASK-5 channels are indeed non-functional as homodimers, but are involved in the formation of functional channel complexes with TASK-1 and TASK-3. TASK-5 negatively modulates the surface expression of TASK channels, while the heteromeric TASK-5-containing channel complexes located at the plasma membrane are characterized by changes in single-channel conductance, Gq-coupled receptor-mediated channel inhibition, and sensitivity to TASK modulators. The unique pharmacology of TASK-1/TASK-5 heterodimers, affected by a common polymorphism in KCNK15, needs to be carefully considered in the future development of drugs targeting TASK channels. Our observations provide an access to study TASK-5 at the functional level, particularly in malignant cancers associated with KCNK15.

Suggested Citation

  • Susanne Rinné & Florian Schick & Kirsty Vowinkel & Sven Schütte & Cornelius Krasel & Silke Kauferstein & Martin K.-H. Schäfer & Aytug K. Kiper & Thomas Müller & Niels Decher, 2024. "Potassium channel TASK-5 forms functional heterodimers with TASK-1 and TASK-3 to break its silence," Nature Communications, Nature, vol. 15(1), pages 1-12, December.
    • Handle: RePEc:nat:natcom:v:15:y:2024:i:1:d:10.1038_s41467-024-51288-8
    DOI: 10.1038/s41467-024-51288-8
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    References listed on IDEAS

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    1. Bettina U. Wilke & Moritz Lindner & Lea Greifenberg & Alexandra Albus & Yannick Kronimus & Moritz Bünemann & Michael G. Leitner & Dominik Oliver, 2014. "Diacylglycerol mediates regulation of TASK potassium channels by Gq-coupled receptors," Nature Communications, Nature, vol. 5(1), pages 1-11, December.
    2. Han Sun & Liqun Luo & Bachchu Lal & Xinrong Ma & Lieping Chen & Christine L. Hann & Amy M. Fulton & Daniel J. Leahy & John Laterra & Min Li, 2016. "A monoclonal antibody against KCNK9 K+ channel extracellular domain inhibits tumour growth and metastasis," Nature Communications, Nature, vol. 7(1), pages 1-12, April.
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