KCNA5
Potassium voltage-gated channel, shaker-related subfamily, member 5, also known as KCNA5 or Kv1.5, is a protein that in humans is encoded by the KCNA5 gene.[1]
Function
Potassium channels represent the most complex class of voltage-gated ion channels from both functional and structural standpoints. KCNA5 encodes a member of the potassium channel, voltage-gated, shaker-related subfamily. This member contains six membrane-spanning domains with a shaker-type repeat in the fourth segment. It belongs to the delayed rectifier class, the function of which could restore the resting membrane potential of beta cells after depolarization, thereby contributing to the regulation of insulin secretion. This gene is intronless, and the gene is clustered with genes KCNA1 and KCNA6 on chromosome 12.[1] Mutations in this gene have been related to both atrial fibrillation [2] and sudden cardiac death.[3] KCNA5 are also key players in pulmonary vascular function, where they play a role in setting the resting membrane potential and its involvement during hypoxic pulmonary vasoconstriction.
Interactions
KCNA5 has been shown to interact with DLG4[4][5] and Actinin, alpha 2.[4][6]
See also
References
- ↑ 1.0 1.1 "Entrez Gene: KCNA5 potassium voltage-gated channel, shaker-related subfamily, member 5".
- ↑ Olson, TM; Alekseev AE; Liu XK; Park S; Zingman LV; Bienengraeber M; Sattiraju S; Ballew JD; Jahangir A; Terzic A (July 2006). "Kv1.5 channelopathy due to KCNA5 loss-of-function mutation causes human atrial fibrillation". Hum Mol Genet 15 (14): 2185–91. doi:10.1093/hmg/ddl143. PMID 16772329.
- ↑ Nielsen, NH; Winkel BG, Kanters JK, Schmitt N, Hofman-Bang J, Jensen HS, Bentzen BH, Sigurd B, Larsen LA, Andersen PS, Haunsø S, Kjeldsen K, Grunnet M, Christiansen M, Olesen SP (March 2007). "Mutations in the Kv1.5 channel gene KCNA5 in cardiac arrest patients". Biochem Biophys Res Commun 354 (3): 776–82. doi:10.1016/j.bbrc.2007.01.048. PMID 17266934.
- ↑ 4.0 4.1 Eldstrom, Jodene; Choi Woo Sung; Steele David F; Fedida David (July 2003). "SAP97 increases Kv1.5 currents through an indirect N-terminal mechanism". FEBS Lett. (Netherlands) 547 (1–3): 205–11. doi:10.1016/S0014-5793(03)00668-9. ISSN 0014-5793. PMID 12860415.
- ↑ Eldstrom, Jodene; Doerksen Kyle W; Steele David F; Fedida David (November 2002). "N-terminal PDZ-binding domain in Kv1 potassium channels". FEBS Lett. (Netherlands) 531 (3): 529–37. doi:10.1016/S0014-5793(02)03572-X. ISSN 0014-5793. PMID 12435606.
- ↑ Maruoka, N D; Steele D F; Au B P; Dan P; Zhang X; Moore E D; Fedida D (May 2000). "alpha-actinin-2 couples to cardiac Kv1.5 channels, regulating current density and channel localization in HEK cells". FEBS Lett. (NETHERLANDS) 473 (2): 188–94. doi:10.1016/S0014-5793(00)01521-0. ISSN 0014-5793. PMID 10812072.
Further reading
- Gutman GA, Chandy KG, Grissmer S et al. (2006). "International Union of Pharmacology. LIII. Nomenclature and molecular relationships of voltage-gated potassium channels". Pharmacol. Rev. 57 (4): 473–508. doi:10.1124/pr.57.4.10. PMID 16382104.
- Curran ME, Landes GM, Keating MT (1992). "Molecular cloning, characterization, and genomic localization of a human potassium channel gene". Genomics 12 (4): 729–37. doi:10.1016/0888-7543(92)90302-9. PMID 1349297.
- Philipson LH, Hice RE, Schaefer K et al. (1991). "Sequence and functional expression in Xenopus oocytes of a human insulinoma and islet potassium channel". Proc. Natl. Acad. Sci. U.S.A. 88 (1): 53–7. doi:10.1073/pnas.88.1.53. PMC 50746. PMID 1986382.
- Tamkun MM, Knoth KM, Walbridge JA et al. (1991). "Molecular cloning and characterization of two voltage-gated K+ channel cDNAs from human ventricle". FASEB J. 5 (3): 331–7. PMID 2001794.
- Mays DJ, Foose JM, Philipson LH, Tamkun MM (1995). "Localization of the Kv1.5 K+ channel protein in explanted cardiac tissue". J. Clin. Invest. 96 (1): 282–92. doi:10.1172/JCI118032. PMC 185199. PMID 7615797.
- Crumb WJ, Wible B, Arnold DJ et al. (1995). "Blockade of multiple human cardiac potassium currents by the antihistamine terfenadine: possible mechanism for terfenadine-associated cardiotoxicity". Mol. Pharmacol. 47 (1): 181–90. PMID 7838127.
- Phromchotikul T, Browne DL, Curran ME et al. (1993). "Dinucleotide repeat polymorphism at the KCNA5 locus". Hum. Mol. Genet. 2 (9): 1512. doi:10.1093/hmg/2.9.1512-a. PMID 8242092.
- Albrecht B, Weber K, Pongs O (1996). "Characterization of a voltage-activated K-channel gene cluster on human chromosome 12p13". Recept. Channels 3 (3): 213–20. PMID 8821794.
- Holmes TC, Fadool DA, Ren R, Levitan IB (1997). "Association of Src tyrosine kinase with a human potassium channel mediated by SH3 domain". Science 274 (5295): 2089–91. doi:10.1126/science.274.5295.2089. PMID 8953041.
- Lacerda AE, Roy ML, Lewis EW, Rampe D (1997). "Interactions of the nonsedating antihistamine loratadine with a Kv1.5-type potassium channel cloned from human heart". Mol. Pharmacol. 52 (2): 314–22. PMID 9271355.
- Kääb S, Dixon J, Duc J et al. (1998). "Molecular basis of transient outward potassium current downregulation in human heart failure: a decrease in Kv4.3 mRNA correlates with a reduction in current density". Circulation 98 (14): 1383–93. doi:10.1161/01.cir.98.14.1383. PMID 9760292.
- Maruoka ND, Steele DF, Au BP et al. (2000). "alpha-actinin-2 couples to cardiac Kv1.5 channels, regulating current density and channel localization in HEK cells". FEBS Lett. 473 (2): 188–94. doi:10.1016/S0014-5793(00)01521-0. PMID 10812072.
- Peretz A, Gil-Henn H, Sobko A et al. (2000). "Hypomyelination and increased activity of voltage-gated K+ channels in mice lacking protein tyrosine phosphatase ε". EMBO J. 19 (15): 4036–45. doi:10.1093/emboj/19.15.4036. PMC 306594. PMID 10921884.
- Nitabach MN, Llamas DA, Araneda RC et al. (2001). "A mechanism for combinatorial regulation of electrical activity: Potassium channel subunits capable of functioning as Src homology 3-dependent adaptors". Proc. Natl. Acad. Sci. U.S.A. 98 (2): 705–10. doi:10.1073/pnas.031446198. PMC 14652. PMID 11149959.
- Cukovic D, Lu GW, Wible B et al. (2001). "A discrete amino terminal domain of Kv1.5 and Kv1.4 potassium channels interacts with the spectrin repeats of alpha-actinin-2". FEBS Lett. 498 (1): 87–92. doi:10.1016/S0014-5793(01)02505-4. PMID 11389904.
- Kurata HT, Soon GS, Eldstrom JR et al. (2002). "Amino-terminal determinants of U-type inactivation of voltage-gated K+ channels". J. Biol. Chem. 277 (32): 29045–53. doi:10.1074/jbc.M111470200. PMID 12021261.
- Williams CP, Hu N, Shen W et al. (2002). "Modulation of the human Kv1.5 channel by protein kinase C activation: role of the Kvbeta1.2 subunit". J. Pharmacol. Exp. Ther. 302 (2): 545–50. doi:10.1124/jpet.102.033357. PMID 12130714.
- Eldstrom J, Doerksen KW, Steele DF, Fedida D (2002). "N-terminal PDZ-binding domain in Kv1 potassium channels". FEBS Lett. 531 (3): 529–37. doi:10.1016/S0014-5793(02)03572-X. PMID 12435606.
- Strausberg RL, Feingold EA, Grouse LH et al. (2003). "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. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
- Zhang S, Kurata HT, Kehl SJ, Fedida D (2003). "Rapid Induction of P/C-type Inactivation Is the Mechanism for Acid-induced K+ Current Inhibition". J. Gen. Physiol. 121 (3): 215–25. doi:10.1085/jgp.20028760. PMC 2217332. PMID 12601085.
External links
- Kv1.5 Potassium Channel at the US National Library of Medicine Medical Subject Headings (MeSH)
- KCNA5 protein, human at the US National Library of Medicine Medical Subject Headings (MeSH)
This article incorporates text from the United States National Library of Medicine, which is in the public domain.
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