Available structures
PDBOrtholog search: PDBe RCSB
Aliases KCNK2, K2p2.1, TPKC1, TREK, TREK-1, TREK1, hTREK-1c, hTREK-1e, potassium two pore domain channel subfamily K member 2
External IDs MGI: 109366 HomoloGene: 7794 GeneCards: KCNK2
Targeted by Drug
arachidonic acid, halothane, riluzole[1]
RNA expression pattern
More reference expression data
Species Human Mouse









RefSeq (mRNA)



RefSeq (protein)



Location (UCSC) Chr 1: 215.01 – 215.24 Mb Chr 1: 189.21 – 189.4 Mb
PubMed search [2] [3]
View/Edit HumanView/Edit Mouse

Potassium channel subfamily K member 2 is a protein that in humans is encoded by the KCNK2 gene.[4][5][6]

This gene encodes K2P2.1, 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.[6]

Function in neurons

Another name for this channel is TREK-1. TREK-1 is part of the subfamily of mechano-gated potassium channels that are present in mammalian neurons. They can be gated in both chemical and physical ways and can be opened via both physical stimuli and chemical stimuli. TREK-1 channels are found in a variety of tissues, but are particularly abundant in the brain and heart and are seen in various types of neurons.[7] The C-terminal of TREK-1 channels plays a role in the mechanosensitivity of the channels.[8]

In the neurons of the central nervous system, TREK-1 channels are important in physiological, pathophysiological, and pharmacological processes, including having a role in electrogenesis, ischemia, and anesthesia. TREK-1 has an important role in neuroprotection against epilepsy and brain and spinal cord ischemia and is being evaluated as a potential target for new developments of therapeutic agents for neurology and anesthesiology.[9]

In the absence of a properly functioning cytoskeleton, TREK-1 channels can still open via mechanical gating.[8] The cell membrane functions independently of the cytoskeleton and the thickness and curvature of the membrane is able to modulate the activity of the TREK-1 channels.[10] The insertion of certain compounds into the membrane is thought to mediate the opening of TREK-1 by forming a curve in the membrane.[8]

See also


  1. "Drugs that physically interact with Potassium channel subfamily K member 2 view/edit references on wikidata".
  2. "Human PubMed Reference:".
  3. "Mouse PubMed Reference:".
  4. Lesage F, Lazdunski M (Oct 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.
  5. 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.
  6. 1 2 "Entrez Gene: KCNK2 potassium channel, subfamily K, member 2".
  7. Fink, M.; Duprat, F.; Lesage, F.; Reyes, R.; Romey, G.; Heurteaux, C.; Lazdunski, M. (1996). "Cloning, functional expression and brain localization of a novel unconventional outward rectifier K+ channel". The EMBO Journal. 15 (24): 6854–6862. PMC 452511Freely accessible. PMID 9003761.
  8. 1 2 3 Patel, A. J.; Honoré, E.; Maingret, F.; Lesage, F.; Fink, M.; Duprat, F.; Lazdunski, M. (1998). "A mammalian two pore domain mechano-gated S-like K+ channel". The EMBO Journal. 17 (15): 4283–4290. doi:10.1093/emboj/17.15.4283. PMC 1170762Freely accessible. PMID 9687497.
  9. Giorda, R.; Weisberg, E. P.; Ip, T. K.; Trucco, M. (1992). "Genomic structure and strain-specific expression of the natural killer cell receptor NKR-P1". Journal of immunology (Baltimore, Md. : 1950). 149 (6): 1957–1963. PMID 1517565.
  10. Patel, AJ; Lazdunski, M; Honoré, E (2001). "Lipid and mechano-gated 2P domain K(+) channels". Curr Opin Cell Biol. 13 (4): 422–428. doi:10.1016/s0955-0674(00)00231-3.

Further reading

External links

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