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Gene Review

KCNAB1  -  potassium channel, voltage gated subfamily...

Homo sapiens

Synonyms: AKR6A3, K(+) channel subunit beta-1, KCNA1B, KV-BETA-1, Kv-beta-1, ...
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High impact information on KCNAB1

  • We report here the cloning of a voltage-gated K+ channel beta subunit, hKv beta 3, from adult human left ventricle that shows 84% and 74% amino acid sequence identity with the previously cloned rat Kv beta 1 and Kv beta 2 subunits, respectively [1].
  • Coinjection of hKv beta 3 with a human cardiac delayed rectifier, hKv1.5, in Xenopus oocytes increased inactivation, induced an 18-mV hyperpolarizing shift in the activation curve, and slowed deactivation (tau = 8.0 msec vs. 35.4 msec at -50 mV). hKv beta 3 was localized to human chromosome 3 by using a human/rodent cell hybrid mapping panel [1].
  • We found that all Kv beta subunits promote cell surface expression of coexpressed Kv1.2 alpha subunits in transfected COS-1 cells [2].
  • Together, these data suggest that NADP(+) binding and/or the integrity of the binding pocket structure, but not catalytic activity, of Kv beta subunits is required for intracellular trafficking of Kv1 channel complexes in mammalian cells and for axonal targeting in neurons [2].
  • This phenotype can be transferred to co-assembled Kv1 alpha- and Kv beta-subunits associated with Kv1.1 in neurons [3].

Biological context of KCNAB1


Anatomical context of KCNAB1

  • Our results indicate that the hKv1.3 lymphocyte channel retains its electrophysiological characteristics when transfected in the Kv beta-negative HEK 293 cell line but its sensitivity to modulation by PKA and PKC is significantly reduced [7].

Associations of KCNAB1 with chemical compounds

  • The beta subunit, Kv beta 1.2, acts as a rapid open channel blocker of NH2-terminal deleted Kv1.4 alpha-subunits [8].

Other interactions of KCNAB1


Analytical, diagnostic and therapeutic context of KCNAB1


  1. Characterization of a voltage-gated K+ channel beta subunit expressed in human heart. England, S.K., Uebele, V.N., Shear, H., Kodali, J., Bennett, P.B., Tamkun, M.M. Proc. Natl. Acad. Sci. U.S.A. (1995) [Pubmed]
  2. Kv beta subunit oxidoreductase activity and Kv1 potassium channel trafficking. Campomanes, C.R., Carroll, K.I., Manganas, L.N., Hershberger, M.E., Gong, B., Antonucci, D.E., Rhodes, K.J., Trimmer, J.S. J. Biol. Chem. (2002) [Pubmed]
  3. Episodic ataxia type-1 mutations in the Kv1.1 potassium channel display distinct folding and intracellular trafficking properties. Manganas, L.N., Akhtar, S., Antonucci, D.E., Campomanes, C.R., Dolly, J.O., Trimmer, J.S. J. Biol. Chem. (2001) [Pubmed]
  4. Selective interaction of voltage-gated K+ channel beta-subunits with alpha-subunits. Nakahira, K., Shi, G., Rhodes, K.J., Trimmer, J.S. J. Biol. Chem. (1996) [Pubmed]
  5. Localization of two potassium channel beta subunit genes, KCNA1B and KCNA2B. Schultz, D., Litt, M., Smith, L., Thayer, M., McCormack, K. Genomics (1996) [Pubmed]
  6. Structural and functional characterization of human potassium channel subunit beta 1 (KCNA1B). Leicher, T., Roeper, J., Weber, K., Wang, X., Pongs, O. Neuropharmacology (1996) [Pubmed]
  7. The sensitivity of the human Kv1.3 (hKv1.3) lymphocyte K+ channel to regulation by PKA and PKC is partially lost in HEK 293 host cells. Martel, J., Dupuis, G., Deschênes, P., Payet, M.D. J. Membr. Biol. (1998) [Pubmed]
  8. The beta subunit, Kv beta 1.2, acts as a rapid open channel blocker of NH2-terminal deleted Kv1.4 alpha-subunits. Rasmusson, R.L., Wang, S., Castellino, R.C., Morales, M.J., Strauss, H.C. Adv. Exp. Med. Biol. (1997) [Pubmed]
  9. Alternative splicing of the human Shaker K+ channel beta 1 gene and functional expression of the beta 2 gene product. McCormack, K., McCormack, T., Tanouye, M., Rudy, B., Stühmer, W. FEBS Lett. (1995) [Pubmed]
  10. Subunit combinations defined for K+ channel Kv1 subtypes in synaptic membranes from bovine brain. Shamotienko, O.G., Parcej, D.N., Dolly, J.O. Biochemistry (1997) [Pubmed]
  11. Functional differences in Kv1.5 currents expressed in mammalian cell lines are due to the presence of endogenous Kv beta 2.1 subunits. Uebele, V.N., England, S.K., Chaudhary, A., Tamkun, M.M., Snyders, D.J. J. Biol. Chem. (1996) [Pubmed]
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