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

Susanne Rinné, Florian Schick, Kirsty Vowinkel, Sven Schütte, Cornelius Krasel, Silke Kauferstein, Martin K.-H. Schäfer, Aytug K. Kiper, Thomas Müller and Niels Decher ()
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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
Martin K.-H. Schäfer: Philipps University Marburg
Aytug K. Kiper: Philipps University Marburg
Thomas Müller: Pharmaceuticals
Niels Decher: Philipps University Marburg

Nature Communications, 2024, vol. 15, issue 1, 1-12

Abstract: 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.

Date: 2024
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DOI: 10.1038/s41467-024-51288-8

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