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Potassium channel TASK-5 forms functional heterodimers with TASK-1 and TASK-3 to break its silence
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Potassium channel TASK-5 forms functional heterodimers with TASK-1 and TASK-3 to break its silence
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Journal Article
Potassium channel TASK-5 forms functional heterodimers with TASK-1 and TASK-3 to break its silence
2024
Overview
TASK-5 (
KCNK15
) belongs to the acid-sensitive subfamily of two-pore domain potassium (K
2P
) channels, which includes TASK-1 and TASK-3. TASK-5 stands out as K
2P
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
.
The TASK-5 potassium channel is thought to be non-functional. Here, the authors show that it forms complexes with TASK family members, resulting in heteromeric channels with unique pharmacology and potential as therapeutic targets.
Publisher
Nature Publishing Group UK,Nature Publishing Group,Nature Portfolio
