The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)



Gene Review

Kcna3  -  potassium voltage-gated channel, shaker...

Mus musculus

Synonyms: Kca1-3, Kv1.3, MK3, Mk-3, Potassium voltage-gated channel subfamily A member 3, ...
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

Disease relevance of Kcna3


High impact information on Kcna3

  • A family of three closely related potassium channel genes (MK1, MK2, and MK3) that are encoded at distinct genomic loci has been isolated [6].
  • The murine gamma-herpesvirus-68 MK3 protein inhibits CD8(+) T cell recognition by ubiquitinating the cytoplasmic tails of classical MHC class I heavy chains [7].
  • However, TAP degradation also broadened the MK3 inhibitory repertoire and achieved a remarkable resistance to MHC class I upregulation by interferon-gamma, suggesting that it represents a specific adaptation to immune evasion in lymphoid tissue [7].
  • In accordance with this heightened sense of smell, Kv1.3-/- mice have glomeruli or olfactory coding units that are smaller and more numerous than those of wild-type mice [8].
  • Inhibition of Kv1.3 activity facilitates the translocation of the glucose transporter, GLUT4, to the plasma membrane [1].

Chemical compound and disease context of Kcna3

  • The 5-HT-mediated suppression of Kv1.3 currents proceeds via activation of a pertussis toxin-sensitive G protein and a subsequent rise in intracellular Ca2+, but Ca2+ does not directly block the channel [9].

Biological context of Kcna3

  • These data suggest that Kv1.3 plays a far more reaching role in signal transduction, development, and olfactory coding than that of the classically defined role of a potassium channel-to shape excitability by influencing membrane potential [8].
  • Potassium currents in olfactory bulb mitral cells from Kv1.3 null mice have slow inactivation kinetics, a modified voltage dependence, and a dampened C-type inactivation and fail to be modulated by activators of receptor tyrosine signaling cascades [8].
  • These results pinpoint a pathway through which K channels regulate peripheral glucose homeostasis, and identify Kv1.3 as a pharmacologic target for the treatment of diabetes [1].
  • Gene inactivation causes mice (Kv1.3-/-) exposed to a high-fat diet to gain less weight and be less obese than littermate control [1].
  • Here we show that Kv1.3 gene deletion and channel inhibition increase peripheral insulin sensitivity in vivo [1].

Anatomical context of Kcna3

  • We conclude that Kv1.3 inhibition improves insulin sensitivity by increasing the amount of GLUT4 at the plasma membrane [1].
  • Kv1.3 is a voltage-gated potassium (K) channel expressed in a number of tissues, including fat and skeletal muscle [1].
  • Kv1.3 channels are expressed in several tissues and believed to participate in cell volume regulation, apoptosis, T cell activation and renal solute homeostasis [2].
  • 3. Immunohistochemical localization showed each channel to have a unique subcellular distribution: Kv1.1 immunoreactivity was detected in the dendrites and axons terminal, whereas Kv1.2 and Kv1.3 subunits were localized to the axon and the postsynaptic membrane of the rod ribbon synapse, respectively [10].
  • Functional Kv1.3 expression levels increased substantially in a myelin-specific rat T cell line following myelin antigen stimulation, peaking at 15-20 h and then declining to baseline over the next 7 days, in parallel with the acquisition and loss of encephalitogenicity [4].

Associations of Kcna3 with chemical compounds

  • Removal of K+o had a similar effect on current through Kv1.3 when the histidine at the homologous position (H404) was protonated (pH 6.0) [11].
  • Angiotensin II (AngII) upregulated Pax-2 protein and Pax-2 mRNA expression via the AngII type 2 (AT(2)) receptor in MK4 but not in MK3 cells [12].
  • We characterized the action of verapamil and N-methyl-verapamil on current through the delayed-rectifier potassium channel Kv1.3 mouse (mKv1.3) [13].
  • The two T-cell K+ channels, Kv3.1 and Kv1.3, with widely divergent pore properties, differ by a single residue in this internal P-region, leucine 401 in Kv3.1 corresponding to valine 398 in Kv1 [14].
  • Ceramide inhibited Kv1.3 potassium channels, store operated Ca2+ -entry (SOC) and depolarized the plasma membrane to which contribution of spontaneously formed ceramide channels is possible [15].

Regulatory relationships of Kcna3


Other interactions of Kcna3

  • While Kv1.3 was further induced, Kir2.1 was down-regulated [17].
  • MTX-HsTx1 displays the activity of MTX on SK channel, whereas it exhibits the pharmacological profile of HsTx1 on Kv1.1, Kv1.2, Kv1.3, and IK channels [18].
  • Here we report that KChAP is a chaperone for Kv1.3 and Kv4 [19].
  • In accordance with the observed changes in DR current density, the mRNA level for Kv1.3 (assessed by competitive RT-PCR) increased fivefold after treatment of microglia with TGF-beta [16].
  • Pharmacological characterization of the pneumococcal cell wall- and lipopolysaccharide-induced currents with specific ion channel blockers indicated for both cases expression of the charybdotoxin/margatoxin-sensitive Kv1.3 subtype of the Shaker family of voltage-dependent potassium channels [20].
  • Taken together, our results demonstrate that Kv1.5 co-associates with Kv1.3, generating functional heterotetramers in macrophages [21].

Analytical, diagnostic and therapeutic context of Kcna3


  1. The voltage-gated potassium channel Kv1.3 regulates peripheral insulin sensitivity. Xu, J., Wang, P., Li, Y., Li, G., Kaczmarek, L.K., Wu, Y., Koni, P.A., Flavell, R.A., Desir, G.V. Proc. Natl. Acad. Sci. U.S.A. (2004) [Pubmed]
  2. The voltage-gated potassium channel Kv1.3 regulates energy homeostasis and body weight. Xu, J., Koni, P.A., Wang, P., Li, G., Kaczmarek, L., Wu, Y., Li, Y., Flavell, R.A., Desir, G.V. Hum. Mol. Genet. (2003) [Pubmed]
  3. The systemic inflammatory response is involved in the regulation of K(+) channel expression in brain via TNF-alpha-dependent and -independent pathways. Vicente, R., Coma, M., Busquets, S., Moore-Carrasco, R., López-Soriano, F.J., Argilés, J.M., Felipe, A. FEBS Lett. (2004) [Pubmed]
  4. A novel fluorescent toxin to detect and investigate Kv1.3 channel up-regulation in chronically activated T lymphocytes. Beeton, C., Wulff, H., Singh, S., Botsko, S., Crossley, G., Gutman, G.A., Cahalan, M.D., Pennington, M., Chandy, K.G. J. Biol. Chem. (2003) [Pubmed]
  5. Colocalization and nonrandom distribution of Kv1.3 potassium channels and CD3 molecules in the plasma membrane of human T lymphocytes. Panyi, G., Bagdány, M., Bodnár, A., Vámosi, G., Szentesi, G., Jenei, A., Mátyus, L., Varga, S., Waldmann, T.A., Gáspar, R., Damjanovich, S. Proc. Natl. Acad. Sci. U.S.A. (2003) [Pubmed]
  6. A family of three mouse potassium channel genes with intronless coding regions. Chandy, K.G., Williams, C.B., Spencer, R.H., Aguilar, B.A., Ghanshani, S., Tempel, B.L., Gutman, G.A. Science (1990) [Pubmed]
  7. Viral degradation of the MHC class I peptide loading complex. Boname, J.M., de Lima, B.D., Lehner, P.J., Stevenson, P.G. Immunity (2004) [Pubmed]
  8. Kv1.3 channel gene-targeted deletion produces "Super-Smeller Mice" with altered glomeruli, interacting scaffolding proteins, and biophysics. Fadool, D.A., Tucker, K., Perkins, R., Fasciani, G., Thompson, R.N., Parsons, A.D., Overton, J.M., Koni, P.A., Flavell, R.A., Kaczmarek, L.K. Neuron (2004) [Pubmed]
  9. Full-length and truncated Kv1.3 K+ channels are modulated by 5-HT1c receptor activation and independently by PKC. Aiyar, J., Grissmer, S., Chandy, K.G. Am. J. Physiol. (1993) [Pubmed]
  10. The Shaker-like potassium channels of the mouse rod bipolar cell and their contributions to the membrane current. Klumpp, D.J., Song, E.J., Ito, S., Sheng, M.H., Jan, L.Y., Pinto, L.H. J. Neurosci. (1995) [Pubmed]
  11. Regulation of mammalian Shaker-related K+ channels: evidence for non-conducting closed and non-conducting inactivated states. Jäger, H., Rauer, H., Nguyen, A.N., Aiyar, J., Chandy, K.G., Grissmer, S. J. Physiol. (Lond.) (1998) [Pubmed]
  12. Angiotensin II increases Pax-2 expression in fetal kidney cells via the AT2 receptor. Zhang, S.L., Moini, B., Ingelfinger, J.R. J. Am. Soc. Nephrol. (2004) [Pubmed]
  13. Evidence for an internal phenylalkylamine action on the voltage-gated potassium channel Kv1.3. Rauer, H., Grissmer, S. Mol. Pharmacol. (1996) [Pubmed]
  14. The P-region and S6 of Kv3.1 contribute to the formation of the ion conduction pathway. Aiyar, J., Nguyen, A.N., Chandy, K.G., Grissmer, S. Biophys. J. (1994) [Pubmed]
  15. Death or survival: membrane ceramide controls the fate and activation of antigen-specific T-cells depending on signal strength and duration. Detre, C., Kiss, E., Varga, Z., Ludányi, K., Pászty, K., Enyedi, A., Kövesdi, D., Panyi, G., Rajnavölgyi, E., Matkó, J. Cell. Signal. (2006) [Pubmed]
  16. Upregulation of Kv1.3 K(+) channels in microglia deactivated by TGF-beta. Schilling, T., Quandt, F.N., Cherny, V.V., Zhou, W., Heinemann, U., Decoursey, T.E., Eder, C. Am. J. Physiol., Cell Physiol. (2000) [Pubmed]
  17. Differential voltage-dependent K+ channel responses during proliferation and activation in macrophages. Vicente, R., Escalada, A., Coma, M., Fuster, G., Sánchez-Tilló, E., López-Iglesias, C., Soler, C., Solsona, C., Celada, A., Felipe, A. J. Biol. Chem. (2003) [Pubmed]
  18. Evidence for domain-specific recognition of SK and Kv channels by MTX and HsTx1 scorpion toxins. Regaya, I., Beeton, C., Ferrat, G., Andreotti, N., Darbon, H., De Waard, M., Sabatier, J.M. J. Biol. Chem. (2004) [Pubmed]
  19. KChAP as a chaperone for specific K(+) channels. Kuryshev, Y.A., Gudz, T.I., Brown, A.M., Wible, B.A. Am. J. Physiol., Cell Physiol. (2000) [Pubmed]
  20. Induction of potassium channels in mouse brain microglia: cells acquire responsiveness to pneumococcal cell wall components during late development. Draheim, H.J., Prinz, M., Weber, J.R., Weiser, T., Kettenmann, H., Hanisch, U.K. Neuroscience (1999) [Pubmed]
  21. Association of Kv1.5 and Kv1.3 contributes to the major voltage-dependent K+ channel in macrophages. Vicente, R., Escalada, A., Villalonga, N., Texidó, L., Roura-Ferrer, M., Martín-Satué, M., López-Iglesias, C., Soler, C., Solsona, C., Tamkun, M.M., Felipe, A. J. Biol. Chem. (2006) [Pubmed]
  22. Identification of Kv1.1 expression by murine CD4-CD8- thymocytes. A role for voltage-dependent K+ channels in murine thymocyte development. Freedman, B.D., Fleischmann, B.K., Punt, J.A., Gaulton, G., Hashimoto, Y., Kotlikoff, M.I. J. Biol. Chem. (1995) [Pubmed]
  23. Tityustoxin-K(alpha) blockade of the voltage-gated potassium channel Kv1.3. Rodrigues, A.R., Arantes, E.C., Monje, F., Stühmer, W., Varanda, W.A. Br. J. Pharmacol. (2003) [Pubmed]
WikiGenes - Universities