KCNK2: Difference between revisions
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Revision as of 18:49, 4 September 2012
| Potassium channel, subfamily K, member 2 | |||||||||||
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| Identifiers | |||||||||||
| Symbols | KCNK2 ; K2p2.1; MGC126742; MGC126744; TPKC1; TREK; TREK-1; TREK1; hTREK-1c; hTREK-1e | ||||||||||
| External IDs | Template:OMIM5 Template:MGI HomoloGene: 7794 | ||||||||||
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| RNA expression pattern | |||||||||||
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| Orthologs | |||||||||||
| Template:GNF Ortholog box | |||||||||||
| Species | Human | Mouse | |||||||||
| Entrez | n/a | n/a | |||||||||
| Ensembl | n/a | n/a | |||||||||
| UniProt | n/a | n/a | |||||||||
| RefSeq (mRNA) | n/a | n/a | |||||||||
| RefSeq (protein) | n/a | n/a | |||||||||
| Location (UCSC) | n/a | n/a | |||||||||
| PubMed search | n/a | n/a | |||||||||
Potassium channel, subfamily K, member 2, also known as KCNK2, is a human gene.[1]
This gene encodes one of the members of the two-pore-domain background potassium channel protein family. This type of potassium channel is formed by two homodimers that create a channel that leaks potassium out of the cell to control resting membrane potential. The channel can be opened, however, by certain anesthetics, membrane stretching, intracellular acidosis, and heat. Three transcript variants encoding different isoforms have been found for this gene.[1]
See also
References
Further reading
- Goldstein SA, Bockenhauer D, O'Kelly I, Zilberberg N (2001). "Potassium leak channels and the KCNK family of two-P-domain subunits". Nat. Rev. Neurosci. 2 (3): 175–84. PMID 11256078.
- Goldstein SA, Bayliss DA, Kim D; et al. (2006). "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.
- Honoré E (2007). "The neuronal background K2P channels: focus on TREK1". Nat. Rev. Neurosci. 8 (4): 251–61. doi:10.1038/nrn2117. PMID 17375039.
- Fink M, Duprat F, Lesage F; et al. (1997). "Cloning, functional expression and brain localization of a novel unconventional outward rectifier K+ channel". EMBO J. 15 (24): 6854–62. PMID 9003761.
- Lesage F, Lazdunski M (1998). "Mapping of human potassium channel genes TREK-1 (KCNK2) and TASK (KCNK3) to chromosomes 1q41 and 2p23". Genomics. 51 (3): 478–9. doi:10.1006/geno.1998.5397. PMID 9721223.
- Patel AJ, Honoré E, Lesage F; et al. (1999). "Inhalational anesthetics activate two-pore-domain background K+ channels". Nat. Neurosci. 2 (5): 422–6. doi:10.1038/8084. PMID 10321245.
- Meadows HJ, Benham CD, Cairns W; et al. (2000). "Cloning, localisation and functional expression of the human orthologue of the TREK-1 potassium channel". Pflugers Arch. 439 (6): 714–22. PMID 10784345.
- Maylie J, Adelman JP (2001). "Beam me up, Scottie! TREK channels swing both ways". Nat. Neurosci. 4 (5): 457–8. doi:10.1038/87402. PMID 11319549.
- Bockenhauer D, Zilberberg N, Goldstein SA (2001). "KCNK2: reversible conversion of a hippocampal potassium leak into a voltage-dependent channel". Nat. Neurosci. 4 (5): 486–91. doi:10.1038/87434. PMID 11319556.
- Enyeart JJ, Xu L, Danthi S, Enyeart JA (2003). "An ACTH- and ATP-regulated background K+ channel in adrenocortical cells is TREK-1". J. Biol. Chem. 277 (51): 49186–99. doi:10.1074/jbc.M207233200. PMID 12368289.
- Strausberg RL, Feingold EA, Grouse LH; et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932.
- Imabayashi H, Mori T, Gojo S; et al. (2003). "Redifferentiation of dedifferentiated chondrocytes and chondrogenesis of human bone marrow stromal cells via chondrosphere formation with expression profiling by large-scale cDNA analysis". Exp. Cell Res. 288 (1): 35–50. PMID 12878157.
- Miller P, Peers C, Kemp PJ (2004). "Polymodal regulation of hTREK1 by pH, arachidonic acid, and hypoxia: physiological impact in acidosis and alkalosis". Am. J. Physiol., Cell Physiol. 286 (2): C272–82. doi:10.1152/ajpcell.00334.2003. PMID 14522822.
- Fu GK, Wang JT, Yang J; et al. (2005). "Circular rapid amplification of cDNA ends for high-throughput extension cloning of partial genes". Genomics. 84 (1): 205–10. doi:10.1016/j.ygeno.2004.01.011. PMID 15203218.
- Kennard LE, Chumbley JR, Ranatunga KM; et al. (2005). "Inhibition of the human two-pore domain potassium channel, TREK-1, by fluoxetine and its metabolite norfluoxetine". Br. J. Pharmacol. 144 (6): 821–9. doi:10.1038/sj.bjp.0706068. PMID 15685212.
- Miller P, Kemp PJ, Peers C (2005). "Structural requirements for O2 sensing by the human tandem-P domain channel, hTREK1". Biochem. Biophys. Res. Commun. 331 (4): 1253–6. doi:10.1016/j.bbrc.2005.04.042. PMID 15883010.
- Murbartián J, Lei Q, Sando JJ, Bayliss DA (2005). "Sequential phosphorylation mediates receptor- and kinase-induced inhibition of TREK-1 background potassium channels". J. Biol. Chem. 280 (34): 30175–84. doi:10.1074/jbc.M503862200. PMID 16006563.
- Hughes S, Magnay J, Foreman M; et al. (2006). "Expression of the mechanosensitive 2PK+ channel TREK-1 in human osteoblasts". J. Cell. Physiol. 206 (3): 738–48. doi:10.1002/jcp.20536. PMID 16250016.
- Kimura K, Wakamatsu A, Suzuki Y; et al. (2006). "Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes". Genome Res. 16 (1): 55–65. doi:10.1101/gr.4039406. PMID 16344560.
External links
- KCNK2+protein,+human at the US National Library of Medicine Medical Subject Headings (MeSH)
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This article incorporates text from the United States National Library of Medicine, which is in the public domain.