Biology:KCNQ5
 Generic protein structure example |
Potassium voltage-gated channel subfamily KQT member 5 is a protein that in humans is encoded by the KCNQ5 gene.[1][2][3][4]
This gene is a member of the KCNQ potassium channel gene family that is differentially expressed in subregions of the brain and in skeletal muscle. The protein encoded by this gene yields currents that activate slowly with depolarization and can form heteromeric channels with the protein encoded by the KCNQ3 gene. Currents expressed from this protein have voltage dependences and inhibitor sensitivities in common with M-currents. They are also inhibited by M1 muscarinic receptor activation. Three alternatively spliced transcript variants encoding distinct isoforms have been found for this gene, but the full-length nature of only one has been determined.[4]
Interactions
KCNQ5 has been shown to interact with KvLQT3.[5]
See also
References
- ↑ "Molecular cloning and functional expression of KCNQ5, a potassium channel subunit that may contribute to neuronal M-current diversity". J Biol Chem 275 (29): 22395–400. Aug 2000. doi:10.1074/jbc.M002378200. PMID 10787416.
- ↑ "KCNQ5, a novel potassium channel broadly expressed in brain, mediates M-type currents". J Biol Chem 275 (31): 24089–95. Sep 2000. doi:10.1074/jbc.M003245200. PMID 10816588.
- ↑ "International Union of Pharmacology. LIII. Nomenclature and molecular relationships of voltage-gated potassium channels". Pharmacol Rev 57 (4): 473–508. Dec 2005. doi:10.1124/pr.57.4.10. PMID 16382104.
- ↑ 4.0 4.1 "Entrez Gene: KCNQ5 potassium voltage-gated channel, KQT-like subfamily, member 5". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=56479.
- ↑ Yus-Nájera, E; Muñoz A; Salvador N; Jensen B S; Rasmussen H B; Defelipe J; Villarroel A (2003). "Localization of KCNQ5 in the normal and epileptic human temporal neocortex and hippocampal formation". Neuroscience 120 (2): 353–64. doi:10.1016/S0306-4522(03)00321-X. ISSN 0306-4522. PMID 12890507.
Further reading
- "Characterization of KCNQ5/Q3 potassium channels expressed in mammalian cells.". Br. J. Pharmacol. 132 (2): 381–4. 2001. doi:10.1038/sj.bjp.0703861. PMID 11159685.
- "The identification and characterization of a noncontinuous calmodulin-binding site in noninactivating voltage-dependent KCNQ potassium channels.". J. Biol. Chem. 277 (32): 28545–53. 2002. doi:10.1074/jbc.M204130200. PMID 12032157.
- "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. 2003. doi:10.1073/pnas.242603899. PMID 12477932. Bibcode: 2002PNAS...9916899M.
- "Disrupted-in-Schizophrenia-1 (DISC-1): mutant truncation prevents binding to NudE-like (NUDEL) and inhibits neurite outgrowth.". Proc. Natl. Acad. Sci. U.S.A. 100 (1): 289–94. 2003. doi:10.1073/pnas.0136913100. PMID 12506198. Bibcode: 2003PNAS..100..289O.
- "Localization of KCNQ5 in the normal and epileptic human temporal neocortex and hippocampal formation.". Neuroscience 120 (2): 353–64. 2003. doi:10.1016/S0306-4522(03)00321-X. PMID 12890507.
- "The DNA sequence and analysis of human chromosome 6.". Nature 425 (6960): 805–11. 2003. doi:10.1038/nature02055. PMID 14574404. Bibcode: 2003Natur.425..805M.
- "Dual phosphorylations underlie modulation of unitary KCNQ K(+) channels by Src tyrosine kinase.". J. Biol. Chem. 279 (44): 45399–407. 2004. doi:10.1074/jbc.M408410200. PMID 15304482.
- "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121–7. 2004. doi:10.1101/gr.2596504. PMID 15489334.
- "Inactivation as a new regulatory mechanism for neuronal Kv7 channels.". Biophys. J. 92 (8): 2747–56. 2007. doi:10.1529/biophysj.106.101287. PMID 17237198. Bibcode: 2007BpJ....92.2747J.
This article incorporates text from the United States National Library of Medicine, which is in the public domain.
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