Inward-rectifier potassium channels (Kir, IRK) are a specific lipid-gated subset of potassium channels. To date, seven subfamilies have been identified in various mammalian cell types,[1] plants,[2] and bacteria.[3] They are activated by phosphatidylinositol 4,5-bisphosphate (PIP2). The malfunction of the channels has been implicated in several diseases.[4][5] IRK channels possess a pore domain, homologous to that of voltage-gated ion channels, and flanking transmembrane segments (TMSs). They may exist in the membrane as homo- or heterooligomers and each monomer possesses between 2 and 4 TMSs. In terms of function, these proteins transport potassium (K+), with a greater tendency for K+ uptake than K+ export.[3] The process of inward-rectification was discovered by Denis Noble in cardiac muscle cells in 1960s[6] and by Richard Adrian and Alan Hodgkin in 1970 in skeletal muscle cells.[7]
^Kubo Y, Adelman JP, Clapham DE, Jan LY, Karschin A, Kurachi Y, et al. (December 2005). "International Union of Pharmacology. LIV. Nomenclature and Molecular Relationships of Inwardly Rectifying Potassium Channels". Pharmacological Reviews. 57 (4): 509–26. doi:10.1124/pr.57.4.11. PMID16382105. S2CID11588492.
^Hedrich R, Moran O, Conti F, Busch H, Becker D, Gambale F, et al. (1995). "Inward rectifier potassium channels in plants differ from their animal counterparts in response to voltage and channel modulators". European Biophysics Journal. 24 (2): 107–15. doi:10.1007/BF00211406. PMID8582318. S2CID12718513.