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Contents

   



(Top)
 


1 Function  





2 Interactions  





3 See also  





4 References  





5 Further reading  





6 External links  














KCNJ5






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From Wikipedia, the free encyclopedia
 


KCNJ5
Identifiers
AliasesKCNJ5, CIR, GIRK4, KATP1, KIR3.4, LQT13, potassium voltage-gated channel subfamily J member 5, potassium inwardly rectifying channel subfamily J member 5
External IDsOMIM: 600734; MGI: 104755; HomoloGene: 20248; GeneCards: KCNJ5; OMA:KCNJ5 - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_000890
NM_001354169

NM_010605

RefSeq (protein)

NP_000881
NP_001341098

NP_034735

Location (UCSC)Chr 11: 128.89 – 128.92 MbChr 9: 32.23 – 32.26 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

G protein-activated inward rectifier potassium channel 4 (GIRK-4) is a protein that in humans is encoded by the KCNJ5 gene and is a type of G protein-gated ion channel.[5][6]

Function

[edit]

Potassium channels are present in most mammalian cells, where they participate in a wide range of physiologic responses. The protein encoded by this gene is an integral membrane protein and inward-rectifier type potassium channel. The encoded protein, which has a greater tendency to allow potassium to flow into a cell rather than out of a cell, is controlled by G-proteins. It may associate with other G-protein-activated potassium channel subunits to form a heterotetrameric pore-forming complex.[6]

In humans KCNJ5 is mainly expressed in adrenal gland and pituitary, although it is also detected at low levels in pancreas, spleen, lung, heart and brain.[7] Consistent with this expression pattern, mutations in KCNJ5/Kir3.4 can cause familial hyperaldosteronism type III and a type of long QT syndrome.[8]

Interactions

[edit]

KCNJ5 has been shown to interact with KCNJ3.[9][10]

See also

[edit]

References

[edit]
  • ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  • ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  • ^ Kubo Y, Adelman JP, Clapham DE, Jan LY, Karschin A, Kurachi Y, Lazdunski M, Nichols CG, Seino S, Vandenberg CA (December 2005). "International Union of Pharmacology. LIV. Nomenclature and molecular relationships of inwardly rectifying potassium channels". Pharmacological Reviews. 57 (4): 509–26. doi:10.1124/pr.57.4.11. PMID 16382105. S2CID 11588492.
  • ^ a b "Entrez Gene: KCNJ5 potassium inwardly-rectifying channel, subfamily J, member 5".
  • ^ "Gtexportal". GETEX portal.
  • ^ Online Mendelian Inheritance in Man (OMIM): potassium channel, inwardly rectifying, subfamily j, member 5; KCNJ5 - 600734
  • ^ Huang CL, Jan YN, Jan LY (April 1997). "Binding of the G protein betagamma subunit to multiple regions of G protein-gated inward-rectifying K+ channels". FEBS Letters. 405 (3): 291–8. Bibcode:1997FEBSL.405..291H. doi:10.1016/S0014-5793(97)00197-X. PMID 9108307. S2CID 44072628.
  • ^ He C, Yan X, Zhang H, Mirshahi T, Jin T, Huang A, Logothetis DE (February 2002). "Identification of critical residues controlling G protein-gated inwardly rectifying K(+) channel activity through interactions with the beta gamma subunits of G proteins". The Journal of Biological Chemistry. 277 (8): 6088–96. doi:10.1074/jbc.M104851200. PMID 11741896.
  • Further reading

    [edit]
    • Zhuo ML, Huang Y, Liu DP, Liang CC (April 2005). "KATP channel: relation with cell metabolism and role in the cardiovascular system". The International Journal of Biochemistry & Cell Biology. 37 (4): 751–64. doi:10.1016/j.biocel.2004.10.008. PMID 15694835.
  • Tucker SJ, James MR, Adelman JP (July 1995). "Assignment of KATP-1, the cardiac ATP-sensitive potassium channel gene (KCNJ5), to human chromosome 11q24". Genomics. 28 (1): 127–8. doi:10.1006/geno.1995.1121. PMID 7590741.
  • Ashford ML, Bond CT, Blair TA, Adelman JP (1996). "Cloning and functional expression of a rat heart KATP channel". Nature. 378 (6559): 792. doi:10.1038/378792a0. PMID 8524415.
  • Spauschus A, Lentes KU, Wischmeyer E, Dissmann E, Karschin C, Karschin A (February 1996). "A G-protein-activated inwardly rectifying K+ channel (GIRK4) from human hippocampus associates with other GIRK channels". The Journal of Neuroscience. 16 (3): 930–8. doi:10.1523/JNEUROSCI.16-03-00930.1996. PMC 6578796. PMID 8558261.
  • Iizuka M, Kubo Y, Tsunenari I, Pan CX, Akiba I, Kono T (1996). "Functional characterization and localization of a cardiac-type inwardly rectifying K+ channel". Receptors & Channels. 3 (4): 299–315. PMID 8834003.
  • Chan KW, Langan MN, Sui JL, Kozak JA, Pabon A, Ladias JA, Logothetis DE (March 1996). "A recombinant inwardly rectifying potassium channel coupled to GTP-binding proteins". The Journal of General Physiology. 107 (3): 381–97. doi:10.1085/jgp.107.3.381. PMC 2216996. PMID 8868049.
  • Huang CL, Jan YN, Jan LY (April 1997). "Binding of the G protein betagamma subunit to multiple regions of G protein-gated inward-rectifying K+ channels". FEBS Letters. 405 (3): 291–8. Bibcode:1997FEBSL.405..291H. doi:10.1016/S0014-5793(97)00197-X. PMID 9108307. S2CID 44072628.
  • Kanzaki M, Lindorfer MA, Garrison JC, Kojima I (June 1997). "Activation of the calcium-permeable cation channel CD20 by alpha subunits of the Gi protein". The Journal of Biological Chemistry. 272 (23): 14733–9. doi:10.1074/jbc.272.23.14733. PMID 9169438.
  • Wischmeyer E, Döring F, Wischmeyer E, Spauschus A, Thomzig A, Veh R, Karschin A (1997). "Subunit interactions in the assembly of neuronal Kir3.0 inwardly rectifying K+ channels". Molecular and Cellular Neurosciences. 9 (3): 194–206. doi:10.1006/mcne.1997.0614. PMID 9245502. S2CID 8455396.
  • Krapivinsky G, Kennedy ME, Nemec J, Medina I, Krapivinsky L, Clapham DE (July 1998). "Gbeta binding to GIRK4 subunit is critical for G protein-gated K+ channel activation". The Journal of Biological Chemistry. 273 (27): 16946–52. doi:10.1074/jbc.273.27.16946. PMID 9642257.
  • Corey S, Clapham DE (October 1998). "Identification of native atrial G-protein-regulated inwardly rectifying K+ (GIRK4) channel homomultimers". The Journal of Biological Chemistry. 273 (42): 27499–504. doi:10.1074/jbc.273.42.27499. PMID 9765280.
  • Kennedy ME, Nemec J, Corey S, Wickman K, Clapham DE (January 1999). "GIRK4 confers appropriate processing and cell surface localization to G-protein-gated potassium channels". The Journal of Biological Chemistry. 274 (4): 2571–82. doi:10.1074/jbc.274.4.2571. PMID 9891030.
  • Schoots O, Wilson JM, Ethier N, Bigras E, Hebert TE, Van Tol HH (December 1999). "Co-expression of human Kir3 subunits can yield channels with different functional properties". Cellular Signalling. 11 (12): 871–83. doi:10.1016/S0898-6568(99)00059-5. PMID 10659995.
  • He C, Yan X, Zhang H, Mirshahi T, Jin T, Huang A, Logothetis DE (February 2002). "Identification of critical residues controlling G protein-gated inwardly rectifying K(+) channel activity through interactions with the beta gamma subunits of G proteins". The Journal of Biological Chemistry. 277 (8): 6088–96. doi:10.1074/jbc.M104851200. PMID 11741896.
  • Ma D, Zerangue N, Raab-Graham K, Fried SR, Jan YN, Jan LY (February 2002). "Diverse trafficking patterns due to multiple traffic motifs in G protein-activated inwardly rectifying potassium channels from brain and heart". Neuron. 33 (5): 715–29. doi:10.1016/S0896-6273(02)00614-1. PMID 11879649. S2CID 10459917.
  • Lavine N, Ethier N, Oak JN, Pei L, Liu F, Trieu P, Rebois RV, Bouvier M, Hebert TE, Van Tol HH (November 2002). "G protein-coupled receptors form stable complexes with inwardly rectifying potassium channels and adenylyl cyclase". The Journal of Biological Chemistry. 277 (48): 46010–9. doi:10.1074/jbc.M205035200. PMID 12297500.
  • Shankar H, Murugappan S, Kim S, Jin J, Ding Z, Wickman K, Kunapuli SP (September 2004). "Role of G protein-gated inwardly rectifying potassium channels in P2Y12 receptor-mediated platelet functional responses". Blood. 104 (5): 1335–43. doi:10.1182/blood-2004-01-0069. PMID 15142872.
  • [edit]

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


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