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{{Infobox_gene}}
{{PBB_Controls
'''Potassium channel subfamily K member 2''' is a [[protein]] that in humans is encoded by the ''KCNK2'' [[gene]].<ref name="pmid9721223">{{cite journal |vauthors=Lesage F, Lazdunski M | title = Mapping of human potassium channel genes TREK-1 (KCNK2) and TASK (KCNK3) to chromosomes 1q41 and 2p23 | journal = Genomics | volume = 51 | issue = 3 | pages = 478–9 |date=Oct 1998 | pmid = 9721223 | pmc =  | doi = 10.1006/geno.1998.5397 }}</ref><ref name="pmid16382106">{{cite journal |vauthors=Goldstein SA, Bayliss DA, Kim D, Lesage F, Plant LD, Rajan S | title = International Union of Pharmacology. LV. Nomenclature and molecular relationships of two-P potassium channels | journal = Pharmacol Rev | volume = 57 | issue = 4 | pages = 527–40 |date=Dec 2005 | pmid = 16382106 | pmc =  | doi = 10.1124/pr.57.4.12 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: KCNK2 potassium channel, subfamily K, member 2| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3776| accessdate = }}</ref>
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = 
| image_source = 
| PDB =
| Name = Potassium channel, subfamily K, member 2
| HGNCid = 6277
| Symbol = KCNK2
| AltSymbols =; K2p2.1; MGC126742; MGC126744; TPKC1; TREK; TREK-1; TREK1; hTREK-1c; hTREK-1e
| OMIM = 603219
| ECnumber = 
| Homologene = 7794
| MGIid = 109366
| GeneAtlas_image1 = PBB_GE_KCNK2_210261_at_tn.png
| Function = {{GNF_GO|id=GO:0005216 |text = ion channel activity}} {{GNF_GO|id=GO:0005267 |text = potassium channel activity}} {{GNF_GO|id=GO:0015271 |text = outward rectifier potassium channel activity}} {{GNF_GO|id=GO:0030955 |text = potassium ion binding}}
| Component = {{GNF_GO|id=GO:0008076 |text = voltage-gated potassium channel complex}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
  | Process = {{GNF_GO|id=GO:0006811 |text = ion transport}} {{GNF_GO|id=GO:0006813 |text = potassium ion transport}} {{GNF_GO|id=GO:0007186 |text = G-protein coupled receptor protein signaling pathway}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 3776
    | Hs_Ensembl = ENSG00000082482
    | Hs_RefseqProtein = NP_001017424
    | Hs_RefseqmRNA = NM_001017424
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 1
    | Hs_GenLoc_start = 213322731
    | Hs_GenLoc_end = 213477059
    | Hs_Uniprot = O95069
    | Mm_EntrezGene = 16526
    | Mm_Ensembl = ENSMUSG00000037624
    | Mm_RefseqmRNA = NM_010607
    | Mm_RefseqProtein = NP_034737
    | Mm_GenLoc_db =   
    | Mm_GenLoc_chr = 1
    | Mm_GenLoc_start = 190910578
    | Mm_GenLoc_end = 191043876
    | Mm_Uniprot = Q4VQI2
  }}
}}
'''Potassium channel, subfamily K, member 2''', also known as '''KCNK2''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: KCNK2 potassium channel, subfamily K, member 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3776| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
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{{PBB_Summary
{{PBB_Summary
| section_title =  
| section_title =  
| summary_text = 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.<ref name="entrez">{{cite web | title = Entrez Gene: KCNK2 potassium channel, subfamily K, member 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3776| accessdate = }}</ref>
| summary_text = This gene encodes K<sub>2P</sub>2.1, 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.<ref name="entrez"/>
}}
}}
==Function in neurons==
Another name for this channel is ''TREK-1''. TREK-1 is part of the subfamily of mechano-gated [[potassium channel]]s 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.<ref>{{Cite journal
| last1 = Fink | first1 = M.
| last2 = Duprat | first2 = F.
| last3 = Lesage | first3 = F.
| last4 = Reyes | first4 = R.
| last5 = Romey | first5 = G.
| last6 = Heurteaux | first6 = C.
| last7 = Lazdunski | first7 = M.
| title = Cloning, functional expression and brain localization of a novel unconventional outward rectifier K+ channel
| journal = The EMBO Journal
| volume = 15
| issue = 24
| pages = 6854–6862
| year = 1996
| pmid = 9003761
| pmc = 452511
}}</ref>  The  [[C-terminus|C-terminal]] of TREK-1 channels plays a role in the mechanosensitivity of the channels.<ref name="ReferenceA">{{Cite journal
| last1 = Patel | first1 = A. J.
| last2 = Honoré | first2 = E.
| last3 = Maingret | first3 = F.
| last4 = Lesage | first4 = F.
| last5 = Fink | first5 = M.
| last6 = Duprat | first6 = F.
| last7 = Lazdunski | first7 = M.
| doi = 10.1093/emboj/17.15.4283
| title = A mammalian two pore domain mechano-gated S-like K+ channel
| journal = The EMBO Journal
| volume = 17
| issue = 15
| pages = 4283–4290
| pmc = 1170762
| year = 1998
| pmid = 9687497
}}</ref>
In the neurons of the [[central nervous system]], TREK-1 channels are important in physiological, pathophysiological, and pharmacological processes, including having a role in  [[Bioelectrogenesis|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.<ref>{{Cite journal
| last1 = Giorda | first1 = R.
| last2 = Weisberg | first2 = E. P.
| last3 = Ip | first3 = T. K.
| last4 = Trucco | first4 = M.
| title = Genomic structure and strain-specific expression of the natural killer cell receptor NKR-P1
| journal = Journal of Immunology
| volume = 149
| issue = 6
| pages = 1957–1963
| year = 1992
| pmid = 1517565
}}</ref>
In the absence of a properly functioning [[cytoskeleton]], TREK-1 channels can still open via mechanical gating.<ref name="ReferenceA"/>  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.<ref>{{cite journal | last=Patel | first=AJ | last2=Lazdunski | first2=M | last3=Honoré | first3=E | year=2001 | title=Lipid and mechano-gated 2P domain K(+) channels | journal=Curr Opin Cell Biol | volume=13 | issue=4 | pages=422–428 | doi=10.1016/s0955-0674(00)00231-3 | pmid=11454447}}</ref> The insertion of certain compounds into the membrane is thought to mediate the opening of TREK-1 by forming a curve in the membrane.<ref name="ReferenceA"/>


==See also==
==See also==
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==References==
==References==
{{reflist|2}}
{{reflist}}


==Further reading==
==Further reading==
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{{PBB_Further_reading  
{{PBB_Further_reading  
| citations =  
| citations =  
*{{cite journal  | author=Goldstein SA, Bockenhauer D, O'Kelly I, Zilberberg N |title=Potassium leak channels and the KCNK family of two-P-domain subunits. |journal=Nat. Rev. Neurosci. |volume=2 |issue= 3 |pages= 175-84 |year= 2001 |pmid= 11256078 |doi=  }}
*{{cite journal  |vauthors=Goldstein SA, Bockenhauer D, O'Kelly I, Zilberberg N |title=Potassium leak channels and the KCNK family of two-P-domain subunits. |journal=Nat. Rev. Neurosci. |volume=2 |issue= 3 |pages= 175–84 |year= 2001 |pmid= 11256078 |doi=10.1038/35058574  }}
*{{cite journal  | author=Goldstein SA, Bayliss DA, Kim D, ''et al.'' |title=International Union of Pharmacology. LV. Nomenclature and molecular relationships of two-P potassium channels. |journal=Pharmacol. Rev. |volume=57 |issue= 4 |pages= 527-40 |year= 2006 |pmid= 16382106 |doi= 10.1124/pr.57.4.12 }}
*{{cite journal  | author=Honoré E |title=The neuronal background K2P channels: focus on TREK1. |journal=Nat. Rev. Neurosci. |volume=8 |issue= 4 |pages= 251–61 |year= 2007 |pmid= 17375039 |doi= 10.1038/nrn2117 }}
*{{cite journal  | author=Honoré E |title=The neuronal background K2P channels: focus on TREK1. |journal=Nat. Rev. Neurosci. |volume=8 |issue= 4 |pages= 251-61 |year= 2007 |pmid= 17375039 |doi= 10.1038/nrn2117 }}
*{{cite journal   |vauthors=Fink M, Duprat F, Lesage F, etal |title=Cloning, functional expression and brain localization of a novel unconventional outward rectifier K+ channel. |journal=EMBO J. |volume=15 |issue= 24 |pages= 6854–62 |year= 1997 |pmid= 9003761 |doi=  | pmc=452511  }}
*{{cite journal | author=Fink M, Duprat F, Lesage F, ''et al.'' |title=Cloning, functional expression and brain localization of a novel unconventional outward rectifier K+ channel. |journal=EMBO J. |volume=15 |issue= 24 |pages= 6854-62 |year= 1997 |pmid= 9003761 |doi= }}
*{{cite journal   |vauthors=Patel AJ, Honoré E, Lesage F, etal |title=Inhalational anesthetics activate two-pore-domain background K+ channels. |journal=Nat. Neurosci. |volume=2 |issue= 5 |pages= 422–6 |year= 1999 |pmid= 10321245 |doi= 10.1038/8084 }}
*{{cite journal | author=Lesage F, Lazdunski M |title=Mapping of human potassium channel genes TREK-1 (KCNK2) and TASK (KCNK3) to chromosomes 1q41 and 2p23. |journal=Genomics |volume=51 |issue= 3 |pages= 478-9 |year= 1998 |pmid= 9721223 |doi= 10.1006/geno.1998.5397 }}
*{{cite journal   |vauthors=Meadows HJ, Benham CD, Cairns W, etal |title=Cloning, localisation and functional expression of the human orthologue of the TREK-1 potassium channel. |journal=Pflügers Arch. |volume=439 |issue= 6 |pages= 714–22 |year= 2000 |pmid= 10784345 |doi=10.1007/s004240050997 }}
*{{cite journal | author=Patel AJ, Honoré E, Lesage F, ''et al.'' |title=Inhalational anesthetics activate two-pore-domain background K+ channels. |journal=Nat. Neurosci. |volume=2 |issue= 5 |pages= 422-6 |year= 1999 |pmid= 10321245 |doi= 10.1038/8084 }}
*{{cite journal  |vauthors=Maylie J, Adelman JP |title=Beam me up, Scottie! TREK channels swing both ways. |journal=Nat. Neurosci. |volume=4 |issue= 5 |pages= 457–8 |year= 2001 |pmid= 11319549 |doi= 10.1038/87402 }}
*{{cite journal | author=Meadows HJ, Benham CD, Cairns W, ''et al.'' |title=Cloning, localisation and functional expression of the human orthologue of the TREK-1 potassium channel. |journal=Pflugers Arch. |volume=439 |issue= 6 |pages= 714-22 |year= 2000 |pmid= 10784345 |doi=  }}
*{{cite journal  |vauthors=Bockenhauer D, Zilberberg N, Goldstein SA |title=KCNK2: reversible conversion of a hippocampal potassium leak into a voltage-dependent channel. |journal=Nat. Neurosci. |volume=4 |issue= 5 |pages= 486–91 |year= 2001 |pmid= 11319556 |doi= 10.1038/87434 }}
*{{cite journal  | author=Maylie J, Adelman JP |title=Beam me up, Scottie! TREK channels swing both ways. |journal=Nat. Neurosci. |volume=4 |issue= 5 |pages= 457-8 |year= 2001 |pmid= 11319549 |doi= 10.1038/87402 }}
*{{cite journal  |vauthors=Enyeart JJ, Xu L, Danthi S, Enyeart JA |title=An ACTH- and ATP-regulated background K+ channel in adrenocortical cells is TREK-1. |journal=J. Biol. Chem. |volume=277 |issue= 51 |pages= 49186–99 |year= 2003 |pmid= 12368289 |doi= 10.1074/jbc.M207233200 }}
*{{cite journal  | author=Bockenhauer D, Zilberberg N, Goldstein SA |title=KCNK2: reversible conversion of a hippocampal potassium leak into a voltage-dependent channel. |journal=Nat. Neurosci. |volume=4 |issue= 5 |pages= 486-91 |year= 2001 |pmid= 11319556 |doi= 10.1038/87434 }}
*{{cite journal   |vauthors=Strausberg RL, Feingold EA, Grouse LH, etal |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 | pmc=139241 }}
*{{cite journal  | author=Enyeart JJ, Xu L, Danthi S, Enyeart JA |title=An ACTH- and ATP-regulated background K+ channel in adrenocortical cells is TREK-1. |journal=J. Biol. Chem. |volume=277 |issue= 51 |pages= 49186-99 |year= 2003 |pmid= 12368289 |doi= 10.1074/jbc.M207233200 }}
*{{cite journal   |vauthors=Imabayashi H, Mori T, Gojo S, etal |title=Redifferentiation of dedifferentiated chondrocytes and chondrogenesis of human bone marrow stromal cells via chondrosphere formation with expression profiling by large-scale cDNA analysis. |journal=Exp. Cell Res. |volume=288 |issue= 1 |pages= 35–50 |year= 2003 |pmid= 12878157 |doi=10.1016/S0014-4827(03)00130-7 }}
*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal  |vauthors=Miller P, Peers C, Kemp PJ |title=Polymodal regulation of hTREK1 by pH, arachidonic acid, and hypoxia: physiological impact in acidosis and alkalosis. |journal=Am. J. Physiol., Cell Physiol. |volume=286 |issue= 2 |pages= C272–82 |year= 2004 |pmid= 14522822 |doi= 10.1152/ajpcell.00334.2003 }}
*{{cite journal | author=Imabayashi H, Mori T, Gojo S, ''et al.'' |title=Redifferentiation of dedifferentiated chondrocytes and chondrogenesis of human bone marrow stromal cells via chondrosphere formation with expression profiling by large-scale cDNA analysis. |journal=Exp. Cell Res. |volume=288 |issue= 1 |pages= 35-50 |year= 2003 |pmid= 12878157 |doi=  }}
*{{cite journal   |vauthors=Fu GK, Wang JT, Yang J, etal |title=Circular rapid amplification of cDNA ends for high-throughput extension cloning of partial genes. |journal=Genomics |volume=84 |issue= 1 |pages= 205–10 |year= 2005 |pmid= 15203218 |doi= 10.1016/j.ygeno.2004.01.011 }}
*{{cite journal  | author=Miller P, Peers C, Kemp PJ |title=Polymodal regulation of hTREK1 by pH, arachidonic acid, and hypoxia: physiological impact in acidosis and alkalosis. |journal=Am. J. Physiol., Cell Physiol. |volume=286 |issue= 2 |pages= C272-82 |year= 2004 |pmid= 14522822 |doi= 10.1152/ajpcell.00334.2003 }}
*{{cite journal   |vauthors=Kennard LE, Chumbley JR, Ranatunga KM, etal |title=Inhibition of the human two-pore domain potassium channel, TREK-1, by fluoxetine and its metabolite norfluoxetine. |journal=Br. J. Pharmacol. |volume=144 |issue= 6 |pages= 821–9 |year= 2005 |pmid= 15685212 |doi= 10.1038/sj.bjp.0706068 | pmc=1576064 }}
*{{cite journal | author=Fu GK, Wang JT, Yang J, ''et al.'' |title=Circular rapid amplification of cDNA ends for high-throughput extension cloning of partial genes. |journal=Genomics |volume=84 |issue= 1 |pages= 205-10 |year= 2005 |pmid= 15203218 |doi= 10.1016/j.ygeno.2004.01.011 }}
*{{cite journal  |vauthors=Miller P, Kemp PJ, Peers C |title=Structural requirements for O2 sensing by the human tandem-P domain channel, hTREK1. |journal=Biochem. Biophys. Res. Commun. |volume=331 |issue= 4 |pages= 1253–6 |year= 2005 |pmid= 15883010 |doi= 10.1016/j.bbrc.2005.04.042 }}
*{{cite journal | author=Kennard LE, Chumbley JR, Ranatunga KM, ''et al.'' |title=Inhibition of the human two-pore domain potassium channel, TREK-1, by fluoxetine and its metabolite norfluoxetine. |journal=Br. J. Pharmacol. |volume=144 |issue= 6 |pages= 821-9 |year= 2005 |pmid= 15685212 |doi= 10.1038/sj.bjp.0706068 }}
*{{cite journal  |vauthors=Murbartián J, Lei Q, Sando JJ, Bayliss DA |title=Sequential phosphorylation mediates receptor- and kinase-induced inhibition of TREK-1 background potassium channels. |journal=J. Biol. Chem. |volume=280 |issue= 34 |pages= 30175–84 |year= 2005 |pmid= 16006563 |doi= 10.1074/jbc.M503862200 }}
*{{cite journal  | author=Miller P, Kemp PJ, Peers C |title=Structural requirements for O2 sensing by the human tandem-P domain channel, hTREK1. |journal=Biochem. Biophys. Res. Commun. |volume=331 |issue= 4 |pages= 1253-6 |year= 2005 |pmid= 15883010 |doi= 10.1016/j.bbrc.2005.04.042 }}
*{{cite journal   |vauthors=Hughes S, Magnay J, Foreman M, etal |title=Expression of the mechanosensitive 2PK+ channel TREK-1 in human osteoblasts. |journal=J. Cell. Physiol. |volume=206 |issue= 3 |pages= 738–48 |year= 2006 |pmid= 16250016 |doi= 10.1002/jcp.20536 }}
*{{cite journal  | author=Murbartián J, Lei Q, Sando JJ, Bayliss DA |title=Sequential phosphorylation mediates receptor- and kinase-induced inhibition of TREK-1 background potassium channels. |journal=J. Biol. Chem. |volume=280 |issue= 34 |pages= 30175-84 |year= 2005 |pmid= 16006563 |doi= 10.1074/jbc.M503862200 }}
*{{cite journal   |vauthors=Kimura K, Wakamatsu A, Suzuki Y, etal |title=Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes. |journal=Genome Res. |volume=16 |issue= 1 |pages= 55–65 |year= 2006 |pmid= 16344560 |doi= 10.1101/gr.4039406 | pmc=1356129 }}
*{{cite journal | author=Hughes S, Magnay J, Foreman M, ''et al.'' |title=Expression of the mechanosensitive 2PK+ channel TREK-1 in human osteoblasts. |journal=J. Cell. Physiol. |volume=206 |issue= 3 |pages= 738-48 |year= 2006 |pmid= 16250016 |doi= 10.1002/jcp.20536 }}
*{{cite journal | author=Kimura K, Wakamatsu A, Suzuki Y, ''et al.'' |title=Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes. |journal=Genome Res. |volume=16 |issue= 1 |pages= 55-65 |year= 2006 |pmid= 16344560 |doi= 10.1101/gr.4039406 }}
}}
}}
{{refend}}
{{refend}}
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* {{MeshName|KCNK2+protein,+human}}
* {{MeshName|KCNK2+protein,+human}}


{{membrane-protein-stub}}
{{NLM content}}
{{NLM content}}
{{Ion channels}}
{{Ion channels|g3}}
 
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[[Category:Ion channels]]
[[Category:Ion channels]]
{{WikiDoc Sources}}

Latest revision as of 16:03, 29 June 2018

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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n/a

Ensembl

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UniProt

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n/a

RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

Potassium channel subfamily K member 2 is a protein that in humans is encoded by the KCNK2 gene.[1][2][3]

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.[3]

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.[4] The C-terminal of TREK-1 channels plays a role in the mechanosensitivity of the channels.[5]

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.[6]

In the absence of a properly functioning cytoskeleton, TREK-1 channels can still open via mechanical gating.[5] 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.[7] The insertion of certain compounds into the membrane is thought to mediate the opening of TREK-1 by forming a curve in the membrane.[5]

See also

References

  1. ↑ 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.
  2. ↑ 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.
  3. ↑ 3.0 3.1 "Entrez Gene: KCNK2 potassium channel, subfamily K, member 2".
  4. ↑ 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 452511. PMID 9003761.
  5. ↑ 5.0 5.1 5.2 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 1170762. PMID 9687497.
  6. ↑ 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. 149 (6): 1957–1963. PMID 1517565.
  7. ↑ 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. PMID 11454447.

Further reading

External links

This article incorporates text from the United States National Library of Medicine, which is in the public domain.

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