Biology:KCNJ5
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Short description: Protein-coding gene in the species Homo sapiens
 Generic protein structure example |
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.[1][2]
Function
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.[2]
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.[3] Consistent with this expression pattern, mutations in KCNJ5/Kir3.4 can cause familial hyperaldosteronism type III and a type of long QT syndrome.[4]
Interactions
KCNJ5 has been shown to interact with KCNJ3.[5][6]
See also
- G protein-coupled inwardly-rectifying potassium channel
- Inward-rectifier potassium ion channel
References
- ↑ "International Union of Pharmacology. LIV. Nomenclature and molecular relationships of inwardly rectifying potassium channels". Pharmacological Reviews 57 (4): 509–26. December 2005. doi:10.1124/pr.57.4.11. PMID 16382105.
- ↑ 2.0 2.1 "Entrez Gene: KCNJ5 potassium inwardly-rectifying channel, subfamily J, member 5". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3762.
- ↑ "Gtexportal". https://gtexportal.org/home/gene/KCNJ5.
- ↑ Online Mendelian Inheritance in Man (OMIM) potassium channel, inwardly rectifying, subfamily j, member 5; KCNJ5 -600734
- ↑ "Binding of the G protein betagamma subunit to multiple regions of G protein-gated inward-rectifying K+ channels". FEBS Letters 405 (3): 291–8. April 1997. doi:10.1016/S0014-5793(97)00197-X. PMID 9108307.
- ↑ "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. February 2002. doi:10.1074/jbc.M104851200. PMID 11741896.
Further reading
- "KATP channel: relation with cell metabolism and role in the cardiovascular system". The International Journal of Biochemistry & Cell Biology 37 (4): 751–64. April 2005. doi:10.1016/j.biocel.2004.10.008. PMID 15694835.
- "Assignment of KATP-1, the cardiac ATP-sensitive potassium channel gene (KCNJ5), to human chromosome 11q24". Genomics 28 (1): 127–8. July 1995. doi:10.1006/geno.1995.1121. PMID 7590741.
- "Cloning and functional expression of a rat heart KATP channel". Nature 378 (6559): 792. 1996. doi:10.1038/378792a0. PMID 8524415.
- "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. February 1996. doi:10.1523/JNEUROSCI.16-03-00930.1996. PMID 8558261.
- "Functional characterization and localization of a cardiac-type inwardly rectifying K+ channel". Receptors & Channels 3 (4): 299–315. 1996. PMID 8834003.
- "A recombinant inwardly rectifying potassium channel coupled to GTP-binding proteins". The Journal of General Physiology 107 (3): 381–97. March 1996. doi:10.1085/jgp.107.3.381. PMID 8868049.
- "Binding of the G protein betagamma subunit to multiple regions of G protein-gated inward-rectifying K+ channels". FEBS Letters 405 (3): 291–8. April 1997. doi:10.1016/S0014-5793(97)00197-X. PMID 9108307.
- "Activation of the calcium-permeable cation channel CD20 by alpha subunits of the Gi protein". The Journal of Biological Chemistry 272 (23): 14733–9. June 1997. doi:10.1074/jbc.272.23.14733. PMID 9169438.
- "Subunit interactions in the assembly of neuronal Kir3.0 inwardly rectifying K+ channels". Molecular and Cellular Neurosciences 9 (3): 194–206. 1997. doi:10.1006/mcne.1997.0614. PMID 9245502.
- "Gbeta binding to GIRK4 subunit is critical for G protein-gated K+ channel activation". The Journal of Biological Chemistry 273 (27): 16946–52. July 1998. doi:10.1074/jbc.273.27.16946. PMID 9642257.
- "Identification of native atrial G-protein-regulated inwardly rectifying K+ (GIRK4) channel homomultimers". The Journal of Biological Chemistry 273 (42): 27499–504. October 1998. doi:10.1074/jbc.273.42.27499. PMID 9765280.
- "GIRK4 confers appropriate processing and cell surface localization to G-protein-gated potassium channels". The Journal of Biological Chemistry 274 (4): 2571–82. January 1999. doi:10.1074/jbc.274.4.2571. PMID 9891030.
- "Co-expression of human Kir3 subunits can yield channels with different functional properties". Cellular Signalling 11 (12): 871–83. December 1999. doi:10.1016/S0898-6568(99)00059-5. PMID 10659995.
- "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. February 2002. doi:10.1074/jbc.M104851200. PMID 11741896.
- "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. February 2002. doi:10.1016/S0896-6273(02)00614-1. PMID 11879649.
- "G protein-coupled receptors form stable complexes with inwardly rectifying potassium channels and adenylyl cyclase". The Journal of Biological Chemistry 277 (48): 46010–9. November 2002. doi:10.1074/jbc.M205035200. PMID 12297500.
- "Role of G protein-gated inwardly rectifying potassium channels in P2Y12 receptor-mediated platelet functional responses". Blood 104 (5): 1335–43. September 2004. doi:10.1182/blood-2004-01-0069. PMID 15142872.
External links
- KCNJ5+protein,+human at the US National Library of Medicine Medical Subject Headings (MeSH)
- GTEX portal: KCNJ5 expression in human tissue
This article incorporates text from the United States National Library of Medicine, which is in the public domain.
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