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{{Infobox_gene}}
{{PBB_Controls
'''Potassium channel subfamily K member 3''' is a [[protein]] that in humans is encoded by the ''KCNK3'' [[gene]].<ref name="pmid9312005">{{cite journal |vauthors=Duprat F, Lesage F, Fink M, Reyes R, Heurteaux C, Lazdunski M | title = TASK, a human background K+ channel to sense external pH variations near physiological pH | journal = EMBO J | volume = 16 | issue = 17 | pages = 5464–71 |date=Dec 1997 | pmid = 9312005 | pmc = 1170177 | doi = 10.1093/emboj/16.17.5464 }}</ref><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: KCNK3 potassium channel, subfamily K, member 3| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3777| 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 3
| HGNCid = 6278
| Symbol = KCNK3
| AltSymbols =; K2p3.1; OAT1; TASK; TASK-1; TBAK1
| OMIM = 603220
| ECnumber =
| Homologene = 1692
| MGIid = 1100509
| GeneAtlas_image1 = PBB_GE_KCNK3_205952_at_tn.png
| Function = {{GNF_GO|id=GO:0005244 |text = voltage-gated ion channel activity}} {{GNF_GO|id=GO:0005267 |text = potassium channel activity}} {{GNF_GO|id=GO:0030955 |text = potassium ion binding}}
| Component = {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}} {{GNF_GO|id=GO:0016020 |text = membrane}}
  | Process = {{GNF_GO|id=GO:0006811 |text = ion transport}} {{GNF_GO|id=GO:0006813 |text = potassium ion transport}} {{GNF_GO|id=GO:0007268 |text = synaptic transmission}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 3777
    | Hs_Ensembl = ENSG00000171303
    | Hs_RefseqProtein = NP_002237
    | Hs_RefseqmRNA = NM_002246
    | Hs_GenLoc_db =   
    | Hs_GenLoc_chr = 2
    | Hs_GenLoc_start = 26769123
    | Hs_GenLoc_end = 26806207
    | Hs_Uniprot = O14649
    | Mm_EntrezGene = 16527
    | Mm_Ensembl = ENSMUSG00000049265
    | Mm_RefseqmRNA = XM_990938
    | Mm_RefseqProtein = XP_996032
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 5
    | Mm_GenLoc_start = 30864668
    | Mm_GenLoc_end = 30901851
    | Mm_Uniprot = Q9QX34
  }}
}}
'''Potassium channel, subfamily K, member 3''', also known as '''KCNK3''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: KCNK3 potassium channel, subfamily K, member 3| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3777| 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 superfamily of potassium channel proteins containing two pore-forming P domains. The gene product is an outwardly rectifying channel that is sensitive to changes in extracellular pH and is inhibited by extracellular acidification. Also referred to as an acid-sensitive potassium channel, it is activated by the anesthetics halothane and isoflurane. Although three transcripts are detected in northern blots, there is currently no sequence available to confirm transcript variants for this gene.<ref name="entrez">{{cite web | title = Entrez Gene: KCNK3 potassium channel, subfamily K, member 3| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3777| accessdate = }}</ref>
| summary_text = This gene encodes K<sub>2P</sub>3.1, one of the members of the superfamily of potassium channel proteins containing two pore-forming P domains. K<sub>2P</sub>3.1 is an outwardly rectifying channel that is sensitive to changes in extracellular pH and is inhibited by extracellular acidification. Also referred to as an acid-sensitive potassium channel, it is activated by the anesthetics halothane and isoflurane. Although three transcripts are detected in northern blots, there is currently no sequence available to confirm transcript variants for this gene.<ref name="entrez"/>
}}
}}
== Interactive pathway map ==
{{NicotineDopaminergicActivity_WP1602|highlight=KCNK3}}
==Interactions==
KCNK3 has been shown to [[Protein-protein interaction|interact]] with [[YWHAB]]<ref name=pmid12437930>{{cite journal |doi=10.1016/S0092-8674(02)01040-1 |last=O'Kelly |first=Ita |authorlink= |author2=Butler Margaret H |author3=Zilberberg Noam |author4=Goldstein Steve A N  |date=Nov 2002 |title=Forward transport. 14-3-3 binding overcomes retention in endoplasmic reticulum by dibasic signals |journal=Cell |volume=111 |issue=4 |pages=577–88 |publisher= |location = United States| issn = 0092-8674| pmid = 12437930 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = }}</ref> and [[S100A10]].<ref name=pmid12198146>{{cite journal |doi=10.1093/emboj/cdf469 |last=Girard |first=Christophe |authorlink= |author2=Tinel Norbert |author3=Terrenoire Cécile |author4=Romey Georges |author5=Lazdunski Michel |author6=Borsotto Marc  |date=Sep 2002 |title=p11, an annexin II subunit, an auxiliary protein associated with the background K+ channel, TASK-1 |journal=EMBO J. |volume=21 |issue=17 |pages=4439–48 |publisher= |location = England| issn = 0261-4189| pmid = 12198146 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = |pmc=125412 }}</ref>


==See also==
==See also==
Line 58: Line 18:


==References==
==References==
{{reflist|2}}
{{reflist}}


==Further reading==
==Further reading==
Line 64: Line 24:
{{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   |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=Duprat F, Lesage F, Fink M, ''et al.'' |title=TASK, a human background K+ channel to sense external pH variations near physiological pH. |journal=EMBO J. |volume=16 |issue= 17 |pages= 5464-71 |year= 1997 |pmid= 9312005 |doi= 10.1093/emboj/16.17.5464 }}
*{{cite journal  |vauthors=Manjunath NA, Bray-Ward P, Goldstein SA, Gallagher PG |title=Assignment of the 2P domain, acid-sensitive potassium channel OAT1 gene KCNK3 to human chromosome bands 2p24.1→p23.3 and murine 5B by in situ hybridization. |journal=Cytogenet. Cell Genet. |volume=86 |issue= 3-4 |pages= 242–3 |year= 2000 |pmid= 10575216 |doi=10.1159/000015349 }}
*{{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=Lopes CM, Gallagher PG, Buck ME, etal |title=Proton block and voltage gating are potassium-dependent in the cardiac leak channel Kcnk3. |journal=J. Biol. Chem. |volume=275 |issue= 22 |pages= 16969–78 |year= 2000 |pmid= 10748056 |doi= 10.1074/jbc.M001948200 }}
*{{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=Ashmole I, Goodwin PA, Stanfield PR |title=TASK-5, a novel member of the tandem pore K+ channel family. |journal=Pflugers Arch. |volume=442 |issue= 6 |pages= 828–33 |year= 2002 |pmid= 11680614 |doi=10.1007/s004240100620 }}
*{{cite journal  | author=Manjunath NA, Bray-Ward P, Goldstein SA, Gallagher PG |title=Assignment of the 2P domain, acid-sensitive potassium channel OAT1 gene KCNK3 to human chromosome bands 2p24.1-->p23.3 and murine 5B by in situ hybridization. |journal=Cytogenet. Cell Genet. |volume=86 |issue= 3-4 |pages= 242-3 |year= 2000 |pmid= 10575216 |doi=  }}
*{{cite journal  |vauthors=Talley EM, Bayliss DA |title=Modulation of TASK-1 (Kcnk3) and TASK-3 (Kcnk9) potassium channels: volatile anesthetics and neurotransmitters share a molecular site of action. |journal=J. Biol. Chem. |volume=277 |issue= 20 |pages= 17733–42 |year= 2002 |pmid= 11886861 |doi= 10.1074/jbc.M200502200 }}
*{{cite journal | author=Lopes CM, Gallagher PG, Buck ME, ''et al.'' |title=Proton block and voltage gating are potassium-dependent in the cardiac leak channel Kcnk3. |journal=J. Biol. Chem. |volume=275 |issue= 22 |pages= 16969-78 |year= 2000 |pmid= 10748056 |doi= 10.1074/jbc.M001948200 }}
*{{cite journal   |vauthors=Buist SC, Cherrington NJ, Choudhuri S, etal |title=Gender-specific and developmental influences on the expression of rat organic anion transporters. |journal=J. Pharmacol. Exp. Ther. |volume=301 |issue= 1 |pages= 145–51 |year= 2002 |pmid= 11907168 |doi=10.1124/jpet.301.1.145 }}
*{{cite journal  | author=Ashmole I, Goodwin PA, Stanfield PR |title=TASK-5, a novel member of the tandem pore K+ channel family. |journal=Pflugers Arch. |volume=442 |issue= 6 |pages= 828-33 |year= 2002 |pmid= 11680614 |doi=  }}
*{{cite journal   |vauthors=Barbuti A, Ishii S, Shimizu T, etal |title=Block of the background K(+) channel TASK-1 contributes to arrhythmogenic effects of platelet-activating factor. |journal=Am. J. Physiol. Heart Circ. Physiol. |volume=282 |issue= 6 |pages= H2024–30 |year= 2002 |pmid= 12003807 |doi= 10.1152/ajpheart.00956.2001 }}
*{{cite journal  | author=Talley EM, Bayliss DA |title=Modulation of TASK-1 (Kcnk3) and TASK-3 (Kcnk9) potassium channels: volatile anesthetics and neurotransmitters share a molecular site of action. |journal=J. Biol. Chem. |volume=277 |issue= 20 |pages= 17733-42 |year= 2002 |pmid= 11886861 |doi= 10.1074/jbc.M200502200 }}
*{{cite journal   |vauthors=Girard C, Tinel N, Terrenoire C, etal |title=p11, an annexin II subunit, an auxiliary protein associated with the background K+ channel, TASK-1. |journal=EMBO J. |volume=21 |issue= 17 |pages= 4439–48 |year= 2002 |pmid= 12198146 |doi=10.1093/emboj/cdf469  | pmc=125412 }}
*{{cite journal | author=Buist SC, Cherrington NJ, Choudhuri S, ''et al.'' |title=Gender-specific and developmental influences on the expression of rat organic anion transporters. |journal=J. Pharmacol. Exp. Ther. |volume=301 |issue= 1 |pages= 145-51 |year= 2002 |pmid= 11907168 |doi=  }}
*{{cite journal  |vauthors=O'Kelly I, Butler MH, Zilberberg N, Goldstein SA |title=Forward transport. 14-3-3 binding overcomes retention in endoplasmic reticulum by dibasic signals. |journal=Cell |volume=111 |issue= 4 |pages= 577–88 |year= 2002 |pmid= 12437930 |doi=10.1016/S0092-8674(02)01040-1 }}
*{{cite journal | author=Barbuti A, Ishii S, Shimizu T, ''et al.'' |title=Block of the background K(+) channel TASK-1 contributes to arrhythmogenic effects of platelet-activating factor. |journal=Am. J. Physiol. Heart Circ. Physiol. |volume=282 |issue= 6 |pages= H2024-30 |year= 2002 |pmid= 12003807 |doi= 10.1152/ajpheart.00956.2001 }}
*{{cite journal   |vauthors=Aslamkhan A, Han YH, Walden R, etal |title=Stoichiometry of organic anion/dicarboxylate exchange in membrane vesicles from rat renal cortex and hOAT1-expressing cells. |journal=Am. J. Physiol. Renal Physiol. |volume=285 |issue= 4 |pages= F775–83 |year= 2003 |pmid= 12837685 |doi= 10.1152/ajprenal.00140.2003 }}
*{{cite journal | author=Girard C, Tinel N, Terrenoire C, ''et al.'' |title=p11, an annexin II subunit, an auxiliary protein associated with the background K+ channel, TASK-1. |journal=EMBO J. |volume=21 |issue= 17 |pages= 4439-48 |year= 2002 |pmid= 12198146 |doi=  }}
*{{cite journal  | author=Strebel K |title=HIV-1 Vpu: putting a channel to the TASK. |journal=Mol. Cell |volume=14 |issue= 2 |pages= 150–2 |year= 2004 |pmid= 15099514 |doi=10.1016/S1097-2765(04)00205-9 }}
*{{cite journal  | author=O'Kelly I, Butler MH, Zilberberg N, Goldstein SA |title=Forward transport. 14-3-3 binding overcomes retention in endoplasmic reticulum by dibasic signals. |journal=Cell |volume=111 |issue= 4 |pages= 577-88 |year= 2002 |pmid= 12437930 |doi=  }}
*{{cite journal   |vauthors=Hsu K, Seharaseyon J, Dong P, etal |title=Mutual functional destruction of HIV-1 Vpu and host TASK-1 channel. |journal=Mol. Cell |volume=14 |issue= 2 |pages= 259–67 |year= 2004 |pmid= 15099524 |doi=10.1016/S1097-2765(04)00183-2 }}
*{{cite journal | author=Aslamkhan A, Han YH, Walden R, ''et al.'' |title=Stoichiometry of organic anion/dicarboxylate exchange in membrane vesicles from rat renal cortex and hOAT1-expressing cells. |journal=Am. J. Physiol. Renal Physiol. |volume=285 |issue= 4 |pages= F775-83 |year= 2003 |pmid= 12837685 |doi= 10.1152/ajprenal.00140.2003 }}
*{{cite journal   |vauthors=Rusznák Z, Pocsai K, Kovács I, etal |title=Differential distribution of TASK-1, TASK-2 and TASK-3 immunoreactivities in the rat and human cerebellum. |journal=Cell. Mol. Life Sci. |volume=61 |issue= 12 |pages= 1532–42 |year= 2004 |pmid= 15197476 |doi= 10.1007/s00018-004-4082-3 }}
*{{cite journal  | author=Strebel K |title=HIV-1 Vpu: putting a channel to the TASK. |journal=Mol. Cell |volume=14 |issue= 2 |pages= 150-2 |year= 2004 |pmid= 15099514 |doi=  }}
*{{cite journal   |vauthors=Bai X, Greenwood SL, Glazier JD, etal |title=Localization of TASK and TREK, two-pore domain K+ channels, in human cytotrophoblast cells. |journal=J. Soc. Gynecol. Investig. |volume=12 |issue= 2 |pages= 77–83 |year= 2005 |pmid= 15695101 |doi= 10.1016/j.jsgi.2004.08.004 }}
*{{cite journal | author=Hsu K, Seharaseyon J, Dong P, ''et al.'' |title=Mutual functional destruction of HIV-1 Vpu and host TASK-1 channel. |journal=Mol. Cell |volume=14 |issue= 2 |pages= 259-67 |year= 2004 |pmid= 15099524 |doi=  }}
*{{cite journal | author=Rusznák Z, Pocsai K, Kovács I, ''et al.'' |title=Differential distribution of TASK-1, TASK-2 and TASK-3 immunoreactivities in the rat and human cerebellum. |journal=Cell. Mol. Life Sci. |volume=61 |issue= 12 |pages= 1532-42 |year= 2004 |pmid= 15197476 |doi= 10.1007/s00018-004-4082-3 }}
*{{cite journal | author=Bai X, Greenwood SL, Glazier JD, ''et al.'' |title=Localization of TASK and TREK, two-pore domain K+ channels, in human cytotrophoblast cells. |journal=J. Soc. Gynecol. Investig. |volume=12 |issue= 2 |pages= 77-83 |year= 2005 |pmid= 15695101 |doi= 10.1016/j.jsgi.2004.08.004 }}
}}
}}
{{refend}}
{{refend}}
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* {{MeshName|KCNK3+protein,+human}}
* {{MeshName|KCNK3+protein,+human}}


{{membrane-protein-stub}}
{{NLM content}}
{{NLM content}}
{{Ion channels}}
{{Ion channels|g3}}
 
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[[Category:Ion channels]]
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Revision as of 06:16, 2 September 2017

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

n/a

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RefSeq (protein)

n/a

n/a

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

Potassium channel subfamily K member 3 is a protein that in humans is encoded by the KCNK3 gene.[1][2][3][4]

This gene encodes K2P3.1, one of the members of the superfamily of potassium channel proteins containing two pore-forming P domains. K2P3.1 is an outwardly rectifying channel that is sensitive to changes in extracellular pH and is inhibited by extracellular acidification. Also referred to as an acid-sensitive potassium channel, it is activated by the anesthetics halothane and isoflurane. Although three transcripts are detected in northern blots, there is currently no sequence available to confirm transcript variants for this gene.[4]

Interactive pathway map

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

[[File:
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<imagemap> Image:NicotineDopaminergic_WP1602.png
|{{{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".

Interactions

KCNK3 has been shown to interact with YWHAB[5] and S100A10.[6]

See also

References

  1. Duprat F, Lesage F, Fink M, Reyes R, Heurteaux C, Lazdunski M (Dec 1997). "TASK, a human background K+ channel to sense external pH variations near physiological pH". EMBO J. 16 (17): 5464–71. doi:10.1093/emboj/16.17.5464. PMC 1170177. PMID 9312005.
  2. 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.
  3. 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.
  4. 4.0 4.1 "Entrez Gene: KCNK3 potassium channel, subfamily K, member 3".
  5. O'Kelly, Ita; Butler Margaret H; Zilberberg Noam; Goldstein Steve A N (Nov 2002). "Forward transport. 14-3-3 binding overcomes retention in endoplasmic reticulum by dibasic signals". Cell. United States. 111 (4): 577–88. doi:10.1016/S0092-8674(02)01040-1. ISSN 0092-8674. PMID 12437930.
  6. Girard, Christophe; Tinel Norbert; Terrenoire Cécile; Romey Georges; Lazdunski Michel; Borsotto Marc (Sep 2002). "p11, an annexin II subunit, an auxiliary protein associated with the background K+ channel, TASK-1". EMBO J. England. 21 (17): 4439–48. doi:10.1093/emboj/cdf469. ISSN 0261-4189. PMC 125412. PMID 12198146.

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. doi:10.1038/35058574. PMID 11256078.
  • 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.
  • Manjunath NA, Bray-Ward P, Goldstein SA, Gallagher PG (2000). "Assignment of the 2P domain, acid-sensitive potassium channel OAT1 gene KCNK3 to human chromosome bands 2p24.1→p23.3 and murine 5B by in situ hybridization". Cytogenet. Cell Genet. 86 (3–4): 242–3. doi:10.1159/000015349. PMID 10575216.
  • Lopes CM, Gallagher PG, Buck ME, et al. (2000). "Proton block and voltage gating are potassium-dependent in the cardiac leak channel Kcnk3". J. Biol. Chem. 275 (22): 16969–78. doi:10.1074/jbc.M001948200. PMID 10748056.
  • Ashmole I, Goodwin PA, Stanfield PR (2002). "TASK-5, a novel member of the tandem pore K+ channel family". Pflugers Arch. 442 (6): 828–33. doi:10.1007/s004240100620. PMID 11680614.
  • Talley EM, Bayliss DA (2002). "Modulation of TASK-1 (Kcnk3) and TASK-3 (Kcnk9) potassium channels: volatile anesthetics and neurotransmitters share a molecular site of action". J. Biol. Chem. 277 (20): 17733–42. doi:10.1074/jbc.M200502200. PMID 11886861.
  • Buist SC, Cherrington NJ, Choudhuri S, et al. (2002). "Gender-specific and developmental influences on the expression of rat organic anion transporters". J. Pharmacol. Exp. Ther. 301 (1): 145–51. doi:10.1124/jpet.301.1.145. PMID 11907168.
  • Barbuti A, Ishii S, Shimizu T, et al. (2002). "Block of the background K(+) channel TASK-1 contributes to arrhythmogenic effects of platelet-activating factor". Am. J. Physiol. Heart Circ. Physiol. 282 (6): H2024–30. doi:10.1152/ajpheart.00956.2001. PMID 12003807.
  • Girard C, Tinel N, Terrenoire C, et al. (2002). "p11, an annexin II subunit, an auxiliary protein associated with the background K+ channel, TASK-1". EMBO J. 21 (17): 4439–48. doi:10.1093/emboj/cdf469. PMC 125412. PMID 12198146.
  • O'Kelly I, Butler MH, Zilberberg N, Goldstein SA (2002). "Forward transport. 14-3-3 binding overcomes retention in endoplasmic reticulum by dibasic signals". Cell. 111 (4): 577–88. doi:10.1016/S0092-8674(02)01040-1. PMID 12437930.
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This article incorporates text from the United States National Library of Medicine, which is in the public domain.