KCNK9
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Potassium channel subfamily K member 9 is a protein that in humans is encoded by the KCNK9 gene.[1][2][3]
This gene encodes K2P9.1, one of the members of the superfamily of potassium channel proteins containing two pore-forming P domains. This open channel is highly expressed in the cerebellum. It is inhibited by extracellular acidification and arachidonic acid, and strongly inhibited by phorbol 12-myristate 13-acetate.[3][4] Phorbol 12-myristate 13-acetate is also known as 12-O-tetradecanoylphorbol-13-acetate (TPA). TASK channels are additionally inhibited by hormones and transmitters that signal through GqPCRs. The resulting cellular depolarization is thought to regulate processes such as motor control and aldosterone secretion. Despite early controversy about the exact mechanism underlying this inhibition, the current view is that diacyl-glycerol, produced by the breakdown of phosphatidylinositol-4,5-bis-phosphate by phospholipase Cβ causes channel closure.[5]
Expression
The KCNK9 gene is expressed as an ion channel more commonly known as TASK 3. This channel has a varied pattern of expression. TASK 3 is coexpressed with TASK 1 (KCNK3) in the cerebellar granule cells, locus coeruleus, motor neurons, pontine nuclei, some cells in the neocortex, habenula, olfactory bulb granule cells, and cells in the external plexiform layer of the olfactory bulb.[6] TASK-3 channels are also expressed in the hippocampus; both on pyramidal cells and interneurons.[7] It is thought that these channels may form heterodimers where their expressions co-localise.[8][9]
Function
Mice in which the TASK-3 gene has been deleted have reduced sensitivity to inhalation anaesthetics, exaggerated nocturnal activity and cognitive deficits as well as significantly increased appetite and weight gain.[10][11] A role for TASK-3 channels in neuronal network oscillations has also been described: TASK-3 knockout mice lack the atropine-sensitive halothane-induced theta oscillation (4–7 Hz) from the hippocampus and are unable to maintain theta oscillations during rapid eye movement (REM) sleep.[11]
Interactive pathway map
Click on genes, proteins and metabolites below to link to respective articles.[§ 1]
- ^ The interactive pathway map can be edited at WikiPathways: Page Module:Citation/CS1/styles.css has no content."NicotineDopaminergic_WP1602".
See also
References
Page Template:Reflist/styles.css has no content.
- ^ Page Module:Citation/CS1/styles.css has no content.Kim Y, Bang H, Kim D (May 2000). "TASK-3, a new member of the tandem pore K(+) channel family". Journal of Biological Chemistry. 275 (13): 9340–9347. doi:10.1074/jbc.275.13.9340. PMID 10734076.
- ^ Page Module:Citation/CS1/styles.css has no content.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): 527–540. doi:10.1124/pr.57.4.12. PMID 16382106. S2CID 7356601.
- ^ a b Page Module:Citation/CS1/styles.css has no content."Entrez Gene: KCNK9 potassium channel, subfamily K, member 9".
- ^ Page Module:Citation/CS1/styles.css has no content."UniProtKB - Q9NPC2 (KCNK9_HUMAN)". Uniprot. Retrieved 2019-05-29.
- ^ Page Module:Citation/CS1/styles.css has no content.Wilke BU, Lindner M, Greifenberg L, Albus A, Kronimus Y, Bunemann M, et al. (2014-11-25). "Diacylglycerol mediates regulation of TASK potassium channels by Gq-coupled receptors". Nature Communications. 5 (1): 5540. Bibcode:2014NatCo...5.5540W. doi:10.1038/ncomms6540. ISSN 2041-1723. PMID 25420509.
- ^ Page Module:Citation/CS1/styles.css has no content.Bayliss DA, Sirois JE, Talley EM (June 2003). "The TASK family: two-pore domain background K+ channels". Molecular Interventions. 3 (4): 205–219. doi:10.1124/mi.3.4.205. PMID 14993448.
- ^ Page Module:Citation/CS1/styles.css has no content.Torborg CL, Berg AP, Jeffries BW, Bayliss DA, McBain CJ (Jul 12, 2006). "TASK-like conductances are present within hippocampal CA1 stratum oriens interneuron subpopulations". The Journal of Neuroscience. 26 (28): 7362–7367. doi:10.1523/jneurosci.1257-06.2006. PMC 6674194. PMID 16837582.
- ^ Page Module:Citation/CS1/styles.css has no content.Berg AP, Talley EM, Manger JP, Bayliss DA (Jul 28, 2004). "Motoneurons express heteromeric TWIK-related acid-sensitive K+ (TASK) channels containing TASK-1 (KCNK3) and TASK-3 (KCNK9) subunits". The Journal of Neuroscience. 24 (30): 6693–6702. doi:10.1523/jneurosci.1408-04.2004. PMC 6729708. PMID 15282272.
- ^ Page Module:Citation/CS1/styles.css has no content.Kang D, Han J, Talley EM, Bayliss DA, Kim D (Jan 1, 2004). "Functional expression of TASK-1/TASK-3 heteromers in cerebellar granule cells". The Journal of Physiology. 554 (Pt 1): 64–77. doi:10.1113/jphysiol.2003.054387. PMC 1664745. PMID 14678492.
- ^ Page Module:Citation/CS1/styles.css has no content.Linden AM, Aller MI, Leppä E, Rosenberg PH, Wisden W, Korpi ER (October 2008). "K+ channel TASK-1 knockout mice show enhanced sensitivities to ataxic and hypnotic effects of GABA(A) receptor ligands". The Journal of Pharmacology and Experimental Therapeutics. 327 (1): 277–286. doi:10.1124/jpet.108.142083. PMID 18660435. S2CID 31086459.
- ^ a b Page Module:Citation/CS1/styles.css has no content.Pang DS, Robledo CJ, Carr DR, Gent TC, Vyssotski AL, Caley A, et al. (Oct 13, 2009). "An unexpected role for TASK-3 potassium channels in network oscillations with implications for sleep mechanisms and anesthetic action" (PDF). Proceedings of the National Academy of Sciences of the United States of America. 106 (41): 17546–17551. Bibcode:2009PNAS..10617546P. doi:10.1073/pnas.0907228106. PMC 2751655. PMID 19805135.[permanent dead link]
Further reading
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- Page Module:Citation/CS1/styles.css has no content.Goldstein SA, Bockenhauer D, O'Kelly I, Zilberberg N (2001). "Potassium leak channels and the KCNK family of two-P-domain subunits". Nature Reviews. Neuroscience. 2 (3): 175–184. doi:10.1038/35058574. PMID 11256078. S2CID 9682396.
- Page Module:Citation/CS1/styles.css has no content.Rajan S, Wischmeyer E, Xin Liu G, Preisig-Müller R, Daut J, Karschin A, et al. (2000). "TASK-3, a novel tandem pore domain acid-sensitive K+ channel. An extracellular histiding as pH sensor". Journal of Biological Chemistry. 275 (22): 16650–16657. doi:10.1074/jbc.M000030200. hdl:11858/00-001M-0000-0012-F930-0. PMID 10747866.
- Page Module:Citation/CS1/styles.css has no content.Chapman CG, Meadows HJ, Godden RJ, Campbell DA, Duckworth M, Kelsell RE, et al. (2001). "Cloning, localisation and functional expression of a novel human, cerebellum specific, two pore domain potassium channel". Brain Research. Molecular Brain Research. 82 (1–2): 74–83. doi:10.1016/S0169-328X(00)00183-2. PMID 11042359.
- Page Module:Citation/CS1/styles.css has no content.Vega-Saenz de Miera E, Lau DH, Zhadina M, Pountney D, Coetzee WA, Rudy B (2001). "KT3.2 and KT3.3, two novel human two-pore K(+) channels closely related to TASK-1". Journal of Neurophysiology. 86 (1): 130–142. doi:10.1152/jn.2001.86.1.130. PMID 11431495. S2CID 14855672.
- Page Module:Citation/CS1/styles.css has no content.Talley EM, Bayliss DA (2002). "Modulation of TASK-1 (Kcnk3) and TASK-3 (Kcnk9) potassium channels: volatile anesthetics and neurotransmitters share a molecular site of action". Journal of Biological Chemistry. 277 (20): 17733–17742. doi:10.1074/jbc.M200502200. PMID 11886861.
- Page Module:Citation/CS1/styles.css has no content.Rajan S, Preisig-Müller R, Wischmeyer E, Nehring R, Hanley PJ, Renigunta V, et al. (2003). "Interaction with 14-3-3 proteins promotes functional expression of the potassium channels TASK-1 and TASK-3". The Journal of Physiology. 545 (Pt 1): 13–26. doi:10.1113/jphysiol.2002.027052. PMC 2290646. PMID 12433946.
- Page Module:Citation/CS1/styles.css has no content.Mu D, Chen L, Zhang X, See LH, Koch CM, Yen C, et al. (2003). "Genomic amplification and oncogenic properties of the KCNK9 potassium channel gene". Cancer Cell. 3 (3): 297–302. doi:10.1016/S1535-6108(03)00054-0. PMID 12676587.
- Page Module:Citation/CS1/styles.css has no content.Pei L, Wiser O, Slavin A, Mu D, Powers S, Jan LY, et al. (2003). "Oncogenic potential of TASK3 (Kcnk9) depends on K+ channel function". Proceedings of the National Academy of Sciences of the United States of America. 100 (13): 7803–7807. Bibcode:2003PNAS..100.7803P. doi:10.1073/pnas.1232448100. PMC 164668. PMID 12782791.
- Page Module:Citation/CS1/styles.css has no content.Rusznák Z, Pocsai K, Kovács I, Pór A, Pál B, Bíró T, et al. (2004). "Differential distribution of TASK-1, TASK-2 and TASK-3 immunoreactivities in the rat and human cerebellum". Cellular and Molecular Life Sciences. 61 (12): 1532–1542. doi:10.1007/s00018-004-4082-3. PMC 11138546. PMID 15197476. S2CID 11439105.
- Page Module:Citation/CS1/styles.css has no content.Clarke CE, Veale EL, Green PJ, Meadows HJ, Mathie A (2005). "Selective block of the human 2-P domain potassium channel, TASK-3, and the native leak potassium current, IKSO, by zinc". The Journal of Physiology. 560 (Pt 1): 51–62. doi:10.1113/jphysiol.2004.070292. PMC 1665210. PMID 15284350.
- Page Module:Citation/CS1/styles.css has no content.Kim CJ, Cho YG, Jeong SW, Kim YS, Kim SY, Nam SW, et al. (2005). "Altered expression of KCNK9 in colorectal cancers". APMIS: Acta Pathologica, Microbiologica, et Immunologica Scandinavica. 112 (9): 588–594. doi:10.1111/j.1600-0463.2004.apm1120905.x. PMID 15601307. S2CID 41751315.
- Page Module:Citation/CS1/styles.css has no content.Pocsai K, Kosztka L, Bakondi G, Gönczi M, Fodor J, Dienes B, et al. (2006). "Melanoma cells exhibit strong intracellular TASK-3-specific immunopositivity in both tissue sections and cell culture". Cellular and Molecular Life Sciences. 63 (19–20): 2364–2376. doi:10.1007/s00018-006-6166-8. PMC 11136003. PMID 17013562. S2CID 30705845.
- Page Module:Citation/CS1/styles.css has no content.Zuzarte M, Rinné S, Schlichthörl G, Schubert A, Daut J, Preisig-Müller R (2007). "A di-acidic sequence motif enhances the surface expression of the potassium channel TASK-3". Traffic. 8 (8). Copenhagen, Denmark: 1093–1100. doi:10.1111/j.1600-0854.2007.00593.x. PMID 17547699. S2CID 9662403.
External links
- KCNK9+protein,+human at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
- Template:PDBe-KB2
This article incorporates text from the United States National Library of Medicine, which is in the public domain.
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