Proceedings of the National Academy of Sciences · 1995 · 141 citations · 24 references
Natural SciencesBiochemistryMolecular BiologyIon Channel BiophysicsMolecular EvolutionMolecular PhysiologyChannel StructureChannelopathiesIon Channel PhysiologyIon Channel RegulationIon ChannelsPotassium Channel BiophysicsAldo-keto ReductasesCdna CloningChannelsIon Channel Voltage DependencePotassium Channel FunctionPotassium Channel PhysiologyPotassium Channel RegulationVoltage-gated Potassium Channels
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.
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The Ionic Channels in Excitable Membranes
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A stable genomic source of P element transposase in Drosophila melanogaster.
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