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Institut de Pharmacologie Moléculaire, et Cellulaire, Centre National de la Recherche Scientifique-Unité Propre de Recherche 411, Sophia Antipolis, 06560 Valbonne, France
The two-pore-domain K+ channels, or K2P channels, constitute a novel class of K+ channel subunits. They have four transmembrane segments and are active as dimers. The tissue distribution of these channels is widespread, and they are found in both excitable and nonexcitable cells. K2P channels produce currents with unusual characteristics. They are quasi-instantaneous and noninactivating, and they are active at all membrane potentials and insensitive to the classic K+ channel blockers. These properties designate them as background K+ channels. They are expected to play a major role in setting the resting membrane potential in many cell types. Another salient feature of K2P channels is the diversity of their regulatory mechanisms. The weak inward rectifiers TWIK-1 and TWIK-2 are stimulated by activators of protein kinase C and decreased by internal acidification, the baseline TWIK-related acid-sensitive K+ (TASK)-1 and TASK-2 channels are sensitive to external pH changes in a narrow range near physiological pH, and the TWIK-related (TREK)-1 and TWIK-related arachidonic acid-stimulated K+ (TRAAK) channels are the first cloned polyunsaturated fatty acids-activated and mechanogated K+ channels. The recent demonstration that TASK-1 and TREK-1 channels are activated by inhalational general anesthetics, and that TRAAK is activated by the neuroprotective agent riluzole, indicates that this novel class of K+ channels is an interesting target for new therapeutic developments.
two-pore-domain channels; mechanosensitivity; anesthetics
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J. R. Trimarchi, L. Liu, P. J. S. Smith, and D. L. Keefe Apoptosis recruits two-pore domain potassium channels used for homeostatic volume regulation Am J Physiol Cell Physiol, March 1, 2002; 282(3): C588 - C594. [Abstract] [Full Text] [PDF]
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A. Barbuti, S. Ishii, T. Shimizu, R. B. Robinson, and S. J. Feinmark Block of the background K+ channel TASK-1 contributes to arrhythmogenic effects of platelet-activating factor Am J Physiol Heart Circ Physiol, June 1, 2002; 282(6): H2024 - H2030. [Abstract] [Full Text] [PDF]
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