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

Naturevolume 352pages711714 (1991) | Download Citation

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Abstract

MODULATION of neuronal excitability by regulation of K+ channels potentially plays a part in short-term memory1 but has not yet been studied at the molecular level. Regulation of K+ channels by protein phosphorylation2–5 and oxygen6 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+ channels7–13 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.

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Author information

Author notes

  1. Martin Stacker and Olaf Pongs: Ruhr Universität Bochum, Lehrstuhl für Biochemie, D-4600 Bochum, Germany

  2. Stefan H. Heinemann: Max-Planck-lnstitut für Biophysikalische Chemie, Abteilung Membranbiophysik, D-3400 Göttingen, Germany

  3. Rainer Frank: Zentrum für Molekulare Biologie, D-6900 Heidelberg, Germany

Affiliations

  1. Max-Planck-lnstitut für medizinische Forschung, Abteilung Zellphysiologie, Jahnstrasse 29, D-6900, Heidelberg, Germany

    • J. Peter Ruppersberg
    • , Martin Stacker
    • , Olaf Pongs
    • , Stefan H. Heinemann
    • , Rainer Frank
    •  & Michael Koenen

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https://doi.org/10.1038/352711a0

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