Thetwo-pore-domain ortandem pore domain potassium channels are a family of 15 members that form what is known asleak channels which possessGoldman-Hodgkin-Katz (open)rectification.[1] These channels are regulated by several mechanisms includingsignaling lipids,oxygen tension,pH,mechanical stretch, andG-proteins.[2] Two-pore-domain potassium channels correspond structurally to ainward-rectifier potassium channel α-subunits. Each inward-rectifier potassium channel α-subunit is composed of twotransmembrane α-helices, a pore helix and a potassium ion selectivity filter sequence and assembles into atetramer forming the complete channel.[3] The two-pore domain potassium channels instead aredimers where each subunit is essentially two α-subunits joined together.[4]
Each single channel doesnot have two pores; the name of the channel comes from the fact thateach subunit has two P (pore) domains in its primary sequence.[5] To quote Rang and Dale (2015), "The nomenclature is misleading, especially when they are incorrectly referred to as two-pore channels".[6]
A decrease in these leak channels activity is known as 'channel arrest', which reduces oxygen consumption[7] and allows animals to survive anoxia.[8]
^Doyle DA, Morais Cabral J, Pfuetzner RA, Kuo A, Gulbis JM, Cohen SL, et al. (April 1998). "The structure of the potassium channel: molecular basis of K+ conduction and selectivity".Science.280 (5360):69–77.Bibcode:1998Sci...280...69D.doi:10.1126/science.280.5360.69.PMID9525859.
^Gutman GA, Chandy KG, Adelman JP, Aiyar J, Bayliss DA, Clapham DE, et al. (December 2003). "International Union of Pharmacology. XLI. Compendium of voltage-gated ion channels: potassium channels".Pharmacological Reviews.55 (4):583–586.doi:10.1124/pr.55.4.9.PMID14657415.S2CID34963430.
