KCNK9

Potassium channel subfamily K member 9 is a protein that in humans is encoded by the KCNK9 gene.[5][6][7]

KCNK9
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesKCNK9, K2p9.1, KT3.2, TASK-3, TASK3, potassium two pore domain channel subfamily K member 9
External IDsOMIM: 605874 MGI: 3521816 HomoloGene: 56758 GeneCards: KCNK9
Gene location (Human)
Chr.Chromosome 8 (human)[1]
Band8q24.3Start139,600,838 bp[1]
End139,704,109 bp[1]
RNA expression pattern
More reference expression data
Orthologs
SpeciesHumanMouse
Entrez

51305

223604

Ensembl

ENSG00000169427

ENSMUSG00000036760

UniProt

Q9NPC2

Q3LS21

RefSeq (mRNA)

NM_001282534

NM_001033876

RefSeq (protein)

NP_001269463

NP_001029048

Location (UCSC)Chr 8: 139.6 – 139.7 MbChr 15: 72.5 – 72.55 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

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.[7][8] 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. [9]

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.[10] TASK-3 channels are also expressed in the hippocampus; both on pyramidal cells and interneurons.[11] It is thought that these channels may form heterodimers where their expressions co-localise.[12][13]

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.[14][15] 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.[15]

Interactive pathway map

Click on genes, proteins and metabolites below to link to respective articles.[§ 1]

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|{{{bSize}}}px|alt=Nicotine Activity on Dopaminergic Neurons edit]]
Nicotine Activity on Dopaminergic Neurons edit
  1. The interactive pathway map can be edited at WikiPathways: "NicotineDopaminergic_WP1602".

See also

  • Tandem pore domain potassium channel

References

  1. GRCh38: Ensembl release 89: ENSG00000169427 - Ensembl, May 2017
  2. GRCm38: Ensembl release 89: ENSMUSG00000036760 - Ensembl, May 2017
  3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. Kim Y, Bang H, Kim D (May 2000). "TASK-3, a new member of the tandem pore K(+) channel family". J Biol Chem. 275 (13): 9340–7. doi:10.1074/jbc.275.13.9340. PMID 10734076.
  6. 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". Pharmacol Rev. 57 (4): 527–40. doi:10.1124/pr.57.4.12. PMID 16382106. S2CID 7356601.
  7. "Entrez Gene: KCNK9 potassium channel, subfamily K, member 9".
  8. "UniProtKB - Q9NPC2 (KCNK9_HUMAN)". Uniprot. Retrieved 2019-05-29.
  9. Wilke, Bettina U.; Lindner, Moritz; Greifenberg, Lea; Albus, Alexandra; Kronimus, Yannick; Bünemann, Moritz; Leitner, Michael G.; Oliver, Dominik (2014-11-25). "Diacylglycerol mediates regulation of TASK potassium channels by Gq-coupled receptors". Nature Communications. 5 (1): 5540. doi:10.1038/ncomms6540. ISSN 2041-1723. PMID 25420509.
  10. Bayliss DA, Sirois JE, Talley EM (June 2003). "The TASK family: two-pore domain background K+ channels". Molecular Interventions. 3 (4): 205–19. doi:10.1124/mi.3.4.205. PMID 14993448.
  11. 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): 7362–7. doi:10.1523/jneurosci.1257-06.2006. PMC 6674194. PMID 16837582.
  12. 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): 6693–702. doi:10.1523/jneurosci.1408-04.2004. PMC 6729708. PMID 15282272.
  13. 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.
  14. 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): 277–86. doi:10.1124/jpet.108.142083. PMID 18660435. S2CID 31086459.
  15. Pang DS, Robledo CJ, Carr DR, Gent TC, Vyssotski AL, Caley A, Zecharia AY, Wisden W, Brickley SG, Franks NP (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): 17546–51. doi:10.1073/pnas.0907228106. PMC 2751655. PMID 19805135.

Further reading

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