Diacylglycerol mediates regulation of TASK potassium channels by Gq-coupled receptors

Bettina U. Wilke, Moritz Lindner, Lea Greifenberg, Alexandra Albus, Yannick Kronimus, Moritz Bünemann, Michael G. Leitner and Dominik Oliver ()
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Bettina U. Wilke: Institute of Physiology and Pathophysiology, Philipps University
Moritz Lindner: Institute of Physiology and Pathophysiology, Philipps University
Lea Greifenberg: Institute of Physiology and Pathophysiology, Philipps University
Alexandra Albus: Institute of Physiology and Pathophysiology, Philipps University
Yannick Kronimus: Institute of Physiology and Pathophysiology, Philipps University
Moritz Bünemann: Philipps University
Michael G. Leitner: Institute of Physiology and Pathophysiology, Philipps University
Dominik Oliver: Institute of Physiology and Pathophysiology, Philipps University

Nature Communications, 2014, vol. 5, issue 1, 1-11

Abstract: Abstract The two-pore domain potassium (K2P) channels TASK-1 (KCNK3) and TASK-3 (KCNK9) are important determinants of background K+ conductance and membrane potential. TASK-1/3 activity is regulated by hormones and transmitters that act through G protein-coupled receptors (GPCR) signalling via G proteins of the Gαq/11 subclass. How the receptors inhibit channel activity has remained unclear. Here, we show that TASK-1 and -3 channels are gated by diacylglycerol (DAG). Receptor-initiated inhibition of TASK required the activity of phospholipase C, but neither depletion of the PLC substrate PI(4,5)P2 nor release of the downstream messengers IP3 and Ca2+. Attenuation of cellular DAG transients by DAG kinase or lipase suppressed receptor-dependent inhibition, showing that the increase in cellular DAG—but not in downstream lipid metabolites—mediates channel inhibition. The findings identify DAG as the signal regulating TASK channels downstream of GPCRs and define a novel role for DAG that directly links cellular DAG dynamics to excitability.

Date: 2014
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DOI: 10.1038/ncomms6540

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