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XB-ART-24600
Nature 1991 Aug 22;3526337:711-4. doi: 10.1038/352711a0.
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Regulation of fast inactivation of cloned mammalian IK(A) channels by cysteine oxidation.

Ruppersberg JP, Stocker M, Pongs O, Heinemann SH, Frank R, Koenen M.


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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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