KCNK18
| Potassium channel, two pore domain subfamily K, member 18 | |||||||||||||
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| Identifiers | |||||||||||||
| Symbols | KCNK18 ; K2p18.1; MGR13; TRESK; TRESK-2; TRESK2; TRIK | ||||||||||||
| External IDs | OMIM: 613655 MGI: 2685627 HomoloGene: 133808 IUPHAR: 527 GeneCards: KCNK18 Gene | ||||||||||||
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| Orthologs | |||||||||||||
| Species | Human | Mouse | |||||||||||
| Entrez | 338567 | 332396 | |||||||||||
| Ensembl | ENSG00000186795 | ENSMUSG00000040901 | |||||||||||
| UniProt | Q7Z418 | Q6VV64 | |||||||||||
| RefSeq (mRNA) | NM_181840 | NM_207261 | |||||||||||
| RefSeq (protein) | NP_862823 | NP_997144 | |||||||||||
| Location (UCSC) |
Chr 10: 117.2 – 117.21 Mb |
Chr 19: 59.22 – 59.24 Mb | |||||||||||
| PubMed search | |||||||||||||
Potassium channel subfamily K member 18 (KCNK18), also known as TWIK-related spinal cord potassium channel (TRESK) or K2P18.1 is a protein that in humans is encoded by the KCNK18 gene. K2P18.1 is a potassium channel containing two pore-forming P domains.[1]
A flaw in this gene could help trigger migraine headaches. If the gene does not work properly, environmental factors can more easily trigger pain centres in the brain and cause a severe headache.[2]
See also
References
- ↑ Goldstein SA, Bayliss DA, Kim D, Lesage F, Plant LD, Rajan S (December 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.
- ↑ Lafrenière RG, Cader MZ, Poulin J-F, Andres-Enguix I, Simoneau M, Gupta N, Boisvert K, Lafrenière F, McLaughlan S, Dubé M-P, Marcinkiewicz MM, Ramagopalan S, Ansorge O, Brais B, Sequeiros J, Pereira-Monteiro JM, Griffiths LR, Tucker SJ, Ebers G, Rouleau GA (September 2010). "A dominant-negative mutation in the TRESK potassium channel is linked to familial migraine with aura". Nature Medicine 16 (10): 1157–1160. doi:10.1038/nm.2216. PMID 20871611. Lay summary – BBC News (2010-09-27).
Further reading
- Andres-Enguix I, Shang L, Stansfeld PJ, Morahan JM, Sansom MSP, Lafrenière RG, Roy B, Griffiths LR, Rouleau GA, Ebers GC, Cader MZ and Tucker SJ (2012). "Functional analysis of missense variants in the TRESK (KCNK18) K+ channel.". Scientific Reports 2. article number 237. doi:10.1038/srep00237. PMC 3266952. PMID 22355750.
- Czirják G, Tóth ZE, Enyedi P (2004). "The two-pore domain K+ channel, TRESK, is activated by the cytoplasmic calcium signal through calcineurin". J. Biol. Chem. 279 (18): 18550–8. doi:10.1074/jbc.M312229200. PMID 14981085.
- Kang D, Mariash E, Kim D (2004). "Functional expression of TRESK-2, a new member of the tandem-pore K+ channel family". J. Biol. Chem. 279 (27): 28063–70. doi:10.1074/jbc.M402940200. PMID 15123670.
- Barrios-Rodiles M, Brown KR, Ozdamar B, et al. (2005). "High-throughput mapping of a dynamic signaling network in mammalian cells". Science 307 (5715): 1621–5. doi:10.1126/science.1105776. PMID 15761153.
- Czirják G, Vuity D, Enyedi P (2008). "Phosphorylation-dependent binding of 14-3-3 proteins controls TRESK regulation". J. Biol. Chem. 283 (23): 15672–80. doi:10.1074/jbc.M800712200. PMC 3259650. PMID 18397886.
- Pottosin II, Bonales-Alatorre E, Valencia-Cruz G, et al. (2008). "TRESK-like potassium channels in leukemic T cells". Pflugers Arch. 456 (6): 1037–48. doi:10.1007/s00424-008-0481-x. PMID 18506476.
- Sano Y, Inamura K, Miyake A, et al. (2003). "A novel two-pore domain K+ channel, TRESK, is localized in the spinal cord". J. Biol. Chem. 278 (30): 27406–12. doi:10.1074/jbc.M206810200. PMID 12754259.
External links
- KCNK18 protein, human at the US National Library of Medicine Medical Subject Headings (MeSH)
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