Regulation of fast inactivation of cloned mammalian IK(A) channels by cysteine oxidation - PubMed (original) (raw)

. 1991 Aug 22;352(6337):711-4.

doi: 10.1038/352711a0.

Affiliations

• PMID: 1908562
• DOI: 10.1038/352711a0

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

J P Ruppersberg et al. Nature. 1991.

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.

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