Two-pore-domain potassium channel

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The two-pore-domain or tandem pore domain potassium channels are a family of 15 members that form what is known as "leak channels" which possess Goldman-Hodgkin-Katz (open) rectification.[1] These channels are regulated by several mechanisms including signaling lipids, oxygen tension, pH, mechanical stretch, and G-proteins .[citation needed] Their name is derived from the fact that the α subunits consist of four transmembrane segments, each containing two pore loops. As such, they structurally correspond to two inward-rectifier α subunits and thus form dimers in the membrane.

Each single channel does not have two pores; the name of the channel comes from the fact that each subunit has two P (pore) domains in its primary sequence.[2] To quote Rang and Dale (2015), "The nomenclature is misleading, especially when they are incorrectly referred to as two-pore channels".[3]

Below is a list of the 15 known two-pore-domain human potassium channels:[1]

Gene Channel[4] Family Aliases
KCNK1 K2p1.1 TWIK[5][6] TWIK-1
KCNK2 K2p2.1 TREK[5][6] TREK-1
KCNK3 K2p3.1 TASK[5][6] TASK-1
KCNK4 K2p4.1 TREK[5][6] TRAAK[7]
KCNK5 K2p5.1 TASK[5][6] TASK-2[8]
KCNK6 K2p6.1 TWIK[5][6] TWIK-2
KCNK7 K2p7.1 TWIK[5][6]
KCNK9 K2p9.1 TASK[5][6] TASK-3
KCNK10 K2p10.1 TREK[5][6] TREK-2
KCNK12 K2p12.1 THIK THIK-2
KCNK13 K2p13.1 THIK THIK-1
KCNK15 K2p15.1 TASK[5][6] TASK-5
KCNK16 K2p16.1 TALK[5][6] TALK-1
KCNK17 K2p17.1 TALK[5][6] TALK-2, TASK-4
KCNK18 K2p18.1 TRIK, TRESK[5][6][9][10]

See also[edit]


  1. ^ a b Goldstein SA, Bayliss DA, Kim D, Lesage F, Plant LD, Rajan S (Dec 2005). "International Union of Pharmacology. LV. Nomenclature and molecular relationships of two-P potassium channels". Pharmacological Reviews. 57 (4): 527–40. doi:10.1124/pr.57.4.12. PMID 16382106.
  2. ^ "Two P domain potassium channels". Guide to Pharmacology. Retrieved 2019-05-28.
  3. ^ Rang, HP (2003). Pharmacology (8 ed.). Edinburgh: Churchill Livingstone. p. 59. ISBN 978-0-443-07145-4.
  4. ^ Gutman GA, Chandy KG, Adelman JP, Aiyar J, Bayliss DA, Clapham DE, et al. (Dec 2003). "International Union of Pharmacology. XLI. Compendium of voltage-gated ion channels: potassium channels". Pharmacological Reviews. 55 (4): 583–6. doi:10.1124/pr.55.4.9. PMID 14657415.
  5. ^ a b c d e f g h i j k l m Enyedi P, Czirják G (Apr 2010). "Molecular background of leak K+ currents: two-pore domain potassium channels". Physiological Reviews. 90 (2): 559–605. doi:10.1152/physrev.00029.2009. PMID 20393194.
  6. ^ a b c d e f g h i j k l m Lotshaw DP (2007). "Biophysical, pharmacological, and functional characteristics of cloned and native mammalian two-pore domain K+ channels". Cell Biochemistry and Biophysics. 47 (2): 209–56. doi:10.1007/s12013-007-0007-8. PMID 17652773.
  7. ^ Fink M, Lesage F, Duprat F, Heurteaux C, Reyes R, Fosset M, Lazdunski M (Jun 1998). "A neuronal two P domain K+ channel stimulated by arachidonic acid and polyunsaturated fatty acids". The EMBO Journal. 17 (12): 3297–308. doi:10.1093/emboj/17.12.3297. PMC 1170668. PMID 9628867.
  8. ^ Goldstein SA, Bockenhauer D, O'Kelly I, Zilberberg N (Mar 2001). "Potassium leak channels and the KCNK family of two-P-domain subunits". Nature Reviews. Neuroscience. 2 (3): 175–84. doi:10.1038/35058574. PMID 11256078.
  9. ^ Sano Y, Inamura K, Miyake A, Mochizuki S, Kitada C, Yokoi H, Nozawa K, Okada H, Matsushime H, Furuichi K (Jul 2003). "A novel two-pore domain K+ channel, TRESK, is localized in the spinal cord". The Journal of Biological Chemistry. 278 (30): 27406–12. doi:10.1074/jbc.M206810200. PMID 12754259.
  10. ^ Czirják G, Tóth ZE, Enyedi P (Apr 2004). "The two-pore domain K+ channel, TRESK, is activated by the cytoplasmic calcium signal through calcineurin". The Journal of Biological Chemistry. 279 (18): 18550–8. doi:10.1074/jbc.M312229200. PMID 14981085.

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