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Two-pore domain K 2P  K +  channels responsible for the background K +  conductance and the resting membrane potential, are also finely regulated by a variety of chemical, physical and physiological stimuli. Hormones and transmitters acting through Gq protein-coupled receptors (GqPCRs) modulate the activity of various K 2P  channels but the signalling involved has remained elusive, in particular whether dynamic regulation by membrane PI(4,5)P 2 , common among other classes of K +  channels, affects K 2P  channels is controversial. Here we show that K 2P  K +  channel TASK-2 requires PI(4,5)P 2  for activity, a dependence that accounts for its run down in the absence of intracellular ATP and its full recovery by addition of exogenous PI(4,5)P 2 , its inhibition by low concentrations of polycation PI scavengers, and inhibition by PI(4,5)P 2  depletion from the membrane. Comprehensive mutagenesis suggests that PI(4,5)P 2  interaction with TASK-2 takes place at C-terminus where three basic aminoacids are identified as being part of a putative binding site.

Phosphatidylinositol (4,5)-bisphosphate dynamically regulates the K2P background K+ channel TASK-2