KCNB1
Potassium voltage-gated channel, Shab-related subfamily, member 1, also known as KCNB1 or Kv2.1, is a protein that, in humans, is encoded by the KCNB1 gene.[1][2][3]
Species and tissue distribution
Kv2.1 channels are widely expressed in various tissues in mammals, including humans. They are found in cardiomyocytes, skeletal muscles, vascular smooth muscles, placental vasculature, retina, and pancreatic β-cells.
Function
Voltage-gated potassium (Kv) channels represent the most complex class of voltage-gated ion channels from both functional and structural standpoints. Their diverse functions include regulating neurotransmitter release, heart rate, insulin secretion, neuronal excitability, epithelial electrolyte transport, smooth muscle contraction, and cell volume. Four sequence-related potassium channel genes - shaker, shaw, shab, and shal - have been identified in Drosophila, and each has been shown to have human homolog(s). This gene encodes a member of the potassium channel, voltage-gated, shab-related subfamily. This member is a delayed rectifier potassium channel and its activity is modulated by some other family members.[1]
In mouse cardiomyocytes, Kv2.1 channel is the molecular substrate of major repolarization current IK-slow2. Transgenic mice, expressing a dominant-negative isoform of Kv2.1, exhibit markedly prolonged action potentials and demonstrate arrhythmia. In mammalian CNS neurons, Kv2.1 is a predominant delayed rectifier K+ current that regulates neuronal excitability, action potential duration, and tonic spiking.[4] In Drosophila photoreceptor cells, the Kv2 channel is the key component of light-induced membrane voltage response. Genetic abolition of this current dramatically decreases photoreceptor information capacity.
Interactions
KCNB1 has been shown to interact with:
See also
References
- ↑ 1.0 1.1 "Entrez Gene: KCNB1 potassium voltage-gated channel, Shab-related subfamily, member 1".
- ↑ Melis R, Stauffer D, Zhao X, Zhu XL, Albrecht B, Pongs O, Brothman A, Leppert M (January 1995). "Physical and genetic localization of a Shab subfamily potassium channel (KCNB1) gene to chromosomal region 20q13.2". Genomics 25 (1): 285–7. doi:10.1016/0888-7543(95)80138-C. PMID 7774931.
- ↑ Gutman GA, Chandy KG, Grissmer S, Lazdunski M, McKinnon D, Pardo LA, Robertson GA, Rudy B, Sanguinetti MC, Stühmer W, Wang X (December 2005). "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.
- ↑ Murakoshi, H; Trimmer JS (March 1999). "Identification of the Kv2.1 K+ channel as a major component of the delayed rectifier K+ current in rat hippocampal neurons.". J Neurosci. 19 (5): 1728–35. PMID 10024359.
- ↑ Ottschytsch N, Raes A, Van Hoorick D, Snyders DJ (June 2002). "Obligatory heterotetramerization of three previously uncharacterized Kv channel alpha-subunits identified in the human genome". Proc. Natl. Acad. Sci. U.S.A. 99 (12): 7986–91. doi:10.1073/pnas.122617999. PMC 123007. PMID 12060745.
- ↑ Peretz A, Gil-Henn H, Sobko A, Shinder V, Attali B, Elson A (August 2000). "Hypomyelination and increased activity of voltage-gated K(+) channels in mice lacking protein tyrosine phosphatase epsilon". EMBO J. 19 (15): 4036–45. doi:10.1093/emboj/19.15.4036. PMC 306594. PMID 10921884.
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.
- Melis R; Stauffer D; Zhao X et al. (1995). "Physical and genetic localization of a Shab subfamily potassium channel (KCNB1) gene to chromosomal region 20q13.2". Genomics 25 (1): 285–7. doi:10.1016/0888-7543(95)80138-C. PMID 7774931.
- Albrecht B, Lorra C, Stocker M, Pongs O (1994). "Cloning and characterization of a human delayed rectifier potassium channel gene". Recept. Channels 1 (2): 99–110. PMID 8081723.
- Hugnot JP; Salinas M; Lesage F et al. (1996). "Kv8.1, a new neuronal potassium channel subunit with specific inhibitory properties towards Shab and Shaw channels". EMBO J. 15 (13): 3322–31. PMC 451895. PMID 8670833.
- Post MA, Kirsch GE, Brown AM (1997). "Kv2.1 and electrically silent Kv6.1 potassium channel subunits combine and express a novel current". FEBS Lett. 399 (1–2): 177–82. doi:10.1016/S0014-5793(96)01316-6. PMID 8980147.
- Patel AJ, Lazdunski M, Honoré E (1998). "Kv2.1/Kv9.3, a novel ATP-dependent delayed-rectifier K+ channel in oxygen-sensitive pulmonary artery myocytes". EMBO J. 16 (22): 6615–25. doi:10.1093/emboj/16.22.6615. PMC 1170266. PMID 9362476.
- Shepard AR, Rae JL (1999). "Electrically silent potassium channel subunits from human lens epithelium". Am. J. Physiol. 277 (3 Pt 1): C412–24. PMID 10484328.
- Zhu XR; Netzer R; Böhlke K et al. (1999). "Structural and functional characterization of Kv6.2 a new gamma-subunit of voltage-gated potassium channel". Recept. Channels 6 (5): 337–50. PMID 10551266.
- 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.
- Deloukas P; Matthews LH; Ashurst J et al. (2002). "The DNA sequence and comparative analysis of human chromosome 20". Nature 414 (6866): 865–71. doi:10.1038/414865a. PMID 11780052.
- Sano Y; Mochizuki S; Miyake A et al. (2002). "Molecular cloning and characterization of Kv6.3, a novel modulatory subunit for voltage-gated K(+) channel Kv2.1". FEBS Lett. 512 (1–3): 230–4. doi:10.1016/S0014-5793(02)02267-6. PMID 11852086.
- 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.
- Ottschytsch N, Raes A, Van Hoorick D, Snyders DJ (2002). "Obligatory heterotetramerization of three previously uncharacterized Kv channel α-subunits identified in the human genome". Proc. Natl. Acad. Sci. U.S.A. 99 (12): 7986–91. doi:10.1073/pnas.122617999. PMC 123007. PMID 12060745.
- MacDonald PE; Wang G; Tsuk S et al. (2003). "Synaptosome-associated protein of 25 kilodaltons modulates Kv2.1 voltage-dependent K(+) channels in neuroendocrine islet beta-cells through an interaction with the channel N terminus". Mol. Endocrinol. 16 (11): 2452–61. doi:10.1210/me.2002-0058. PMID 12403834.
- 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.
- Ju M, Stevens L, Leadbitter E, Wray D (2003). "The Roles of N- and C-terminal determinants in the activation of the Kv2.1 potassium channel". J. Biol. Chem. 278 (15): 12769–78. doi:10.1074/jbc.M212973200. PMID 12560340.
- Tiran Z, Peretz A, Attali B, Elson A (2003). "Phosphorylation-dependent regulation of Kv2.1 Channel activity at tyrosine 124 by Src and by protein-tyrosine phosphatase epsilon". J. Biol. Chem. 278 (19): 17509–14. doi:10.1074/jbc.M212766200. PMID 12615930.
- Consiglio JF, Korn SJ (2004). "Influence of Permeant Ions on Voltage Sensor Function in the Kv2.1 Potassium Channel". J. Gen. Physiol. 123 (4): 387–400. doi:10.1085/jgp.200308976. PMC 2217458. PMID 15024041.
- Thébaud B; Michelakis ED; Wu XC et al. (2005). "Oxygen-sensitive Kv channel gene transfer confers oxygen responsiveness to preterm rabbit and remodeled human ductus arteriosus: implications for infants with patent ductus arteriosus". Circulation 110 (11): 1372–9. doi:10.1161/01.CIR.0000141292.28616.65. PMID 15353504.
- Kerschensteiner D, Soto F, Stocker M (2005). "Fluorescence measurements reveal stoichiometry of K+ channels formed by modulatory and delayed rectifier α-subunits". Proc. Natl. Acad. Sci. U.S.A. 102 (17): 6160–5. doi:10.1073/pnas.0500468102. PMC 1087924. PMID 15827117.
External links
- Kv2.1 Potassium Channel at the US National Library of Medicine Medical Subject Headings (MeSH)
- KCNB1 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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