Two-pore-domain potassium channel

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 . Their name is derived from the fact that the α subunits consist of four transmembrane segments, and each pair of transmembrane segments contains a pore loop between the two transmembrane segments. Thus, each subunit has two pore loops. As such, they structurally correspond to two inward-rectifier α subunits and thus form dimers in the membrane (whereas inward-rectifier α subunits form tetramers).

Not to be confused with the small family of two-pore channels.

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]

GeneChannel[4]FamilyAliases
KCNK1K2p1.1TWIK[5][6]TWIK-1
KCNK2K2p2.1TREK[5][6]TREK-1
KCNK3K2p3.1TASK[5][6]TASK-1
KCNK4K2p4.1TREK[5][6]TRAAK[7]
KCNK5K2p5.1TASK[5][6]TASK-2[8]
KCNK6K2p6.1TWIK[5][6]TWIK-2
KCNK7K2p7.1TWIK[5][6]
KCNK9K2p9.1TASK[5][6]TASK-3
KCNK10K2p10.1TREK[5][6]TREK-2
KCNK12K2p12.1THIKTHIK-2
KCNK13K2p13.1THIKTHIK-1
KCNK15K2p15.1TASK[5][6]TASK-5
KCNK16K2p16.1TALK[5][6]TALK-1
KCNK17K2p17.1TALK[5][6]TALK-2, TASK-4
KCNK18K2p18.1TRIK, TRESK[5][6][9][10]

See also

References
  1. 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. S2CID 7356601.
  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. S2CID 34963430.
  5. 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. 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. S2CID 12759521.
  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. S2CID 9682396.
  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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