Two-pore-domain potassium channel

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

The two-pore-domain potassium channel is 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 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.

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

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

See also

• Ion channel


• Potassium channel

References

1. 
   ^ ^ab 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..mw-parser-output cite.citation{font-style:inherit}.mw-parser-output q{quotes:"""""""'""'"}.mw-parser-output code.cs1-code{color:inherit;background:inherit;border:inherit;padding:inherit}.mw-parser-output .cs1-lock-free a{background:url("//upload.wikimedia.org/wikipedia/commons/thumb/6/65/Lock-green.svg/9px-Lock-green.svg.png")no-repeat;background-position:right .1em center}.mw-parser-output .cs1-lock-limited a,.mw-parser-output .cs1-lock-registration a{background:url("//upload.wikimedia.org/wikipedia/commons/thumb/d/d6/Lock-gray-alt-2.svg/9px-Lock-gray-alt-2.svg.png")no-repeat;background-position:right .1em center}.mw-parser-output .cs1-lock-subscription a{background:url("//upload.wikimedia.org/wikipedia/commons/thumb/a/aa/Lock-red-alt-2.svg/9px-Lock-red-alt-2.svg.png")no-repeat;background-position:right .1em center}.mw-parser-output .cs1-subscription,.mw-parser-output .cs1-registration{color:#555}.mw-parser-output .cs1-subscription span,.mw-parser-output .cs1-registration span{border-bottom:1px dotted;cursor:help}.mw-parser-output .cs1-hidden-error{display:none;font-size:100%}.mw-parser-output .cs1-visible-error{font-size:100%}.mw-parser-output .cs1-subscription,.mw-parser-output .cs1-registration,.mw-parser-output .cs1-format{font-size:95%}.mw-parser-output .cs1-kern-left,.mw-parser-output .cs1-kern-wl-left{padding-left:0.2em}.mw-parser-output .cs1-kern-right,.mw-parser-output .cs1-kern-wl-right{padding-right:0.2em}
   


2. 
   ^ 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.
   


3. 
   ^ ^{abcdefghijklm} 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.
   


4. 
   ^ ^{abcdefghijklm} 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.
   


5. 
   ^ 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.
   


6. 
   ^ 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.
   


7. 
   ^ 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.
   


8. 
   ^ 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.
   

External links

• 
  Tandem+Pore+Domain+Potassium+Channel at the US National Library of Medicine Medical Subject Headings (MeSH)


• 
  "Two-P Potassium Channels". IUPHAR Database of Receptors and Ion Channels. International Union of Basic and Clinical Pharmacology.
  

v t e Membrane transport protein: ion channels (TC 1A)
Ca2+: Calcium channel Ligand-gated Inositol trisphosphate receptor 1 2 3 Ryanodine receptor 1 2 3 Voltage-gated L-type/Cavα 1.1 1.2 1.3 1.4 N-type/Cavα2.2 P-type/Cavα 2.1 Q-type/Cavα2.1 R-type/Cavα2.3 T-type/Cavα 3.1 3.2 3.3 α2δ-subunits 1 2 β-subunits β1 β2 β3 β4 γ-subunits γ1 γ2 γ3 γ4 Cation channels of sperm 1 2 3 4 Two-pore channel 1 2
Na+: Sodium channel Constitutively active Epithelial sodium channel α β γ δ Proton-gated Amiloride-sensitive cation channel 1 2 3 4 Voltage-gated Navα 1.1 1.2 1.3 1.4 1.5 1.6 1.7 1.8 1.9 7A Navβ 1 2 3 4
K+: Potassium channel Calcium-activated BK channel α1 β1 β2 β3 β4 SK channel SK1 SK2 SK3 IK channel IK1 KCa 1.1 2.1 2.2 2.3 3.1 4.1 4.2 5.1 Inward-rectifier KATP Kir 1.1 2.1 2.2 2.3 2.4 2.6 GIRK/Kir 3.1 3.2 3.3 3.4 Kir 4.1 4.2 5.1 6.1 6.2 7.1 Tandem pore domain K2P 1 2 3 4 5 6 7 9 10 12 13 15 16 17 18 Voltage-gated Kvα1-6 1.1 1.2 1.3 1.4 1.5 1.6 1.7 1.8 2.1 2.2 3.1 3.2 3.3 3.4 4.1 4.2 4.3 5.1 6.1 6.2 6.3 6.4 Kvα7-12 7.1 7.2 7.3 7.4 7.5 8.1 8.2 9.1 9.2 9.3 10.1 10.2 11.1/hERG 11.2 11.3 12.1 12.2 12.3 Kvβ 1 2 3 KCNIP 1 2 3 4 minK/ISK minK/ISK-like MiRP 1 2 3 Shaker gene
Miscellaneous Cl−: Chloride channel Calcium-activated chloride channels Anoctamin ANO1 Bestrophin 1 2 Chloride Channel Accessory 1 2 3 4 CFTR CLCN 1 2 3 4 5 6 7 KA KB CLIC 1 2 3 4 5 6 L1 CLNS 1A 1B H+: Proton channel HVCN1 M+: CNG cation channel α 1 2 3 4 β 1 2 3 HCN FC 1 2 3 4 M+: TRP cation channel TRPA (1) TRPC 1 2 3 4 4AP 5 6 7 TRPM 1 2 3 4 5 6 7 8 TRPML 1 2 3 TRPN TRPP 1 2 TRPV 1 2 3 4 5 6 H2O (+ solutes): Porin Aquaporin 0 1 2 3 4 5 6 7 8 9 Voltage-dependent anion channel 1 2 3 General bacterial porin family Cytoplasm: Gap junction Connexin A GJA1 GJA3 GJA4 GJA5 GJA8 GJA9 GJA10 B GJB1 GJB2 GJB3 GJB4 GJB5 GJB6 GJB7 C GJC1 GJC2 GJC3 D GJD2 GJD3 GJD4 Innexin
By gating mechanism Ion channel class Ligand-gated Light-gated Voltage-gated Stretch-activated
see also disorders

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