Regulation of fast inactivation of cloned mammalian IK(A) channels by cysteine oxidation

Nature. 1991 Aug 22;352(6337):711-4. doi: 10.1038/352711a0.

Abstract

Modulation of neuronal excitability by regulation of K+ channels potentially plays a part in short-term memory but has not yet been studied at the molecular level. Regulation of K+ channels by protein phosphorylation and oxygen has been described for various tissues and cell types; regulation of fast-inactivating K+ channels mediating IK(A) currents has not yet been described. Functional expression of cloned mammalian K+ channels has provided a tool for studying their regulation at the molecular level. We report here that fast-inactivating K+ currents mediated by cloned K+ channel subunits derived from mammalian brain expressed in Xenopus oocytes are regulated by the reducing agent glutathione. This type of regulation may have a role in vivo to link metabolism to excitability and to regulate excitability in specific membrane areas of mammalian neurons.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Cloning, Molecular
  • Cysteine
  • Drosophila melanogaster
  • Glutathione / physiology
  • In Vitro Techniques
  • Ion Channel Gating
  • Kinetics
  • Molecular Sequence Data
  • Oligonucleotides / chemistry
  • Oocytes
  • Oxidation-Reduction
  • Potassium Channels / chemistry*
  • Recombinant Proteins
  • Xenopus laevis

Substances

  • Oligonucleotides
  • Potassium Channels
  • Recombinant Proteins
  • Glutathione
  • Cysteine