Skip to main content
PMC home page
Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1995 Jul 18;92(15):6763–6767. doi: 10.1073/pnas.92.15.6763

A potassium channel beta subunit related to the aldo-keto reductase superfamily is encoded by the Drosophila hyperkinetic locus.

S W Chouinard 1, G F Wilson 1, A K Schlimgen 1, B Ganetzky 1
PMCID: PMC41409  PMID: 7542775

Abstract

Genetic and physiological studies of the Drosophila Hyperkinetic (Hk) mutant revealed defects in the function or regulation of K+ channels encoded by the Shaker (Sh) locus. The Hk polypeptide, determined from analysis of cDNA clones, is a homologue of mammalian K+ channel beta subunits (Kv beta). Coexpression of Hk with Sh in Xenopus oocytes increases current amplitudes and changes the voltage dependence and kinetics of activation and inactivation, consistent with predicted functions of Hk in vivo. Sequence alignments show that Hk, together with mammalian Kv beta, represents an additional branch of the aldo-keto reductase superfamily. These results are relevant to understanding the function and evolutionary origin of Kv beta.

Full text

PDF
6763

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Atkinson N. S., Robertson G. A., Ganetzky B. A component of calcium-activated potassium channels encoded by the Drosophila slo locus. Science. 1991 Aug 2;253(5019):551–555. doi: 10.1126/science.1857984. [DOI] [PubMed] [Google Scholar]
  2. Borhani D. W., Harter T. M., Petrash J. M. The crystal structure of the aldose reductase.NADPH binary complex. J Biol Chem. 1992 Dec 5;267(34):24841–24847. doi: 10.2210/pdb1abn/pdb. [DOI] [PubMed] [Google Scholar]
  3. Bruce N. C., Willey D. L., Coulson A. F., Jeffery J. Bacterial morphine dehydrogenase further defines a distinct superfamily of oxidoreductases with diverse functional activities. Biochem J. 1994 May 1;299(Pt 3):805–811. doi: 10.1042/bj2990805. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Chung S., LaMendola J. Cloning and sequence determination of human placental aldose reductase gene. J Biol Chem. 1989 Sep 5;264(25):14775–14777. [PubMed] [Google Scholar]
  5. Fujii Y., Watanabe K., Hayashi H., Urade Y., Kuramitsu S., Kagamiyama H., Hayaishi O. Purification and characterization of rho-crystallin from Japanese common bullfrog lens. J Biol Chem. 1990 Jun 15;265(17):9914–9923. [PubMed] [Google Scholar]
  6. Grindley J. F., Payton M. A., van de Pol H., Hardy K. G. Conversion of Glucose to 2-Keto-l-Gulonate, an Intermediate in l-Ascorbate Synthesis, by a Recombinant Strain of Erwinia citreus. Appl Environ Microbiol. 1988 Jul;54(7):1770–1775. doi: 10.1128/aem.54.7.1770-1775.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Hoog S. S., Pawlowski J. E., Alzari P. M., Penning T. M., Lewis M. Three-dimensional structure of rat liver 3 alpha-hydroxysteroid/dihydrodiol dehydrogenase: a member of the aldo-keto reductase superfamily. Proc Natl Acad Sci U S A. 1994 Mar 29;91(7):2517–2521. doi: 10.1073/pnas.91.7.2517. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Hoshi T., Zagotta W. N., Aldrich R. W. Biophysical and molecular mechanisms of Shaker potassium channel inactivation. Science. 1990 Oct 26;250(4980):533–538. doi: 10.1126/science.2122519. [DOI] [PubMed] [Google Scholar]
  9. Hoshi T., Zagotta W. N., Aldrich R. W. Two types of inactivation in Shaker K+ channels: effects of alterations in the carboxy-terminal region. Neuron. 1991 Oct;7(4):547–556. doi: 10.1016/0896-6273(91)90367-9. [DOI] [PubMed] [Google Scholar]
  10. Isom L. L., De Jongh K. S., Catterall W. A. Auxiliary subunits of voltage-gated ion channels. Neuron. 1994 Jun;12(6):1183–1194. doi: 10.1016/0896-6273(94)90436-7. [DOI] [PubMed] [Google Scholar]
  11. Iverson L. E., Rudy B. The role of the divergent amino and carboxyl domains on the inactivation properties of potassium channels derived from the Shaker gene of Drosophila. J Neurosci. 1990 Sep;10(9):2903–2916. doi: 10.1523/JNEUROSCI.10-09-02903.1990. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Kamb A., Iverson L. E., Tanouye M. A. Molecular characterization of Shaker, a Drosophila gene that encodes a potassium channel. Cell. 1987 Jul 31;50(3):405–413. doi: 10.1016/0092-8674(87)90494-6. [DOI] [PubMed] [Google Scholar]
  13. Kamb A., Tseng-Crank J., Tanouye M. A. Multiple products of the Drosophila Shaker gene may contribute to potassium channel diversity. Neuron. 1988 Jul;1(5):421–430. doi: 10.1016/0896-6273(88)90192-4. [DOI] [PubMed] [Google Scholar]
  14. Kaplan W. D., Trout W. E., 3rd The behavior of four neurological mutants of Drosophila. Genetics. 1969 Feb;61(2):399–409. doi: 10.1093/genetics/61.2.399. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Liman E. R., Tytgat J., Hess P. Subunit stoichiometry of a mammalian K+ channel determined by construction of multimeric cDNAs. Neuron. 1992 Nov;9(5):861–871. doi: 10.1016/0896-6273(92)90239-a. [DOI] [PubMed] [Google Scholar]
  16. McCormack T., McCormack K. Shaker K+ channel beta subunits belong to an NAD(P)H-dependent oxidoreductase superfamily. Cell. 1994 Dec 30;79(7):1133–1135. doi: 10.1016/0092-8674(94)90004-3. [DOI] [PubMed] [Google Scholar]
  17. Parcej D. N., Scott V. E., Dolly J. O. Oligomeric properties of alpha-dendrotoxin-sensitive potassium ion channels purified from bovine brain. Biochemistry. 1992 Nov 17;31(45):11084–11088. doi: 10.1021/bi00160a018. [DOI] [PubMed] [Google Scholar]
  18. Rettig J., Heinemann S. H., Wunder F., Lorra C., Parcej D. N., Dolly J. O., Pongs O. Inactivation properties of voltage-gated K+ channels altered by presence of beta-subunit. Nature. 1994 May 26;369(6478):289–294. doi: 10.1038/369289a0. [DOI] [PubMed] [Google Scholar]
  19. Robertson H. M., Preston C. R., Phillis R. W., Johnson-Schlitz D. M., Benz W. K., Engels W. R. A stable genomic source of P element transposase in Drosophila melanogaster. Genetics. 1988 Mar;118(3):461–470. doi: 10.1093/genetics/118.3.461. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Rondeau J. M., Tête-Favier F., Podjarny A., Reymann J. M., Barth P., Biellmann J. F., Moras D. Novel NADPH-binding domain revealed by the crystal structure of aldose reductase. Nature. 1992 Jan 30;355(6359):469–472. doi: 10.1038/355469a0. [DOI] [PubMed] [Google Scholar]
  21. Salkoff L., Baker K., Butler A., Covarrubias M., Pak M. D., Wei A. An essential 'set' of K+ channels conserved in flies, mice and humans. Trends Neurosci. 1992 May;15(5):161–166. doi: 10.1016/0166-2236(92)90165-5. [DOI] [PubMed] [Google Scholar]
  22. Schwarz T. L., Tempel B. L., Papazian D. M., Jan Y. N., Jan L. Y. Multiple potassium-channel components are produced by alternative splicing at the Shaker locus in Drosophila. Nature. 1988 Jan 14;331(6152):137–142. doi: 10.1038/331137a0. [DOI] [PubMed] [Google Scholar]
  23. Stern M., Ganetzky B. Altered synaptic transmission in Drosophila hyperkinetic mutants. J Neurogenet. 1989 Aug;5(4):215–228. doi: 10.3109/01677068909066209. [DOI] [PubMed] [Google Scholar]
  24. Stern M., Ganetzky B. Identification and characterization of inebriated, a gene affecting neuronal excitability in Drosophila. J Neurogenet. 1992 Sep;8(3):157–172. doi: 10.3109/01677069209083445. [DOI] [PubMed] [Google Scholar]
  25. Warmke J., Drysdale R., Ganetzky B. A distinct potassium channel polypeptide encoded by the Drosophila eag locus. Science. 1991 Jun 14;252(5012):1560–1562. doi: 10.1126/science.1840699. [DOI] [PubMed] [Google Scholar]
  26. Watanabe K., Fujii Y., Nakayama K., Ohkubo H., Kuramitsu S., Kagamiyama H., Nakanishi S., Hayaishi O. Structural similarity of bovine lung prostaglandin F synthase to lens epsilon-crystallin of the European common frog. Proc Natl Acad Sci U S A. 1988 Jan;85(1):11–15. doi: 10.1073/pnas.85.1.11. [DOI] [PMC free article] [PubMed] [Google Scholar]
  27. Wilson D. K., Bohren K. M., Gabbay K. H., Quiocho F. A. An unlikely sugar substrate site in the 1.65 A structure of the human aldose reductase holoenzyme implicated in diabetic complications. Science. 1992 Jul 3;257(5066):81–84. doi: 10.1126/science.1621098. [DOI] [PubMed] [Google Scholar]

Articles from Proceedings of the National Academy of Sciences of the United States of America are provided here courtesy of National Academy of Sciences

RESOURCES