An amino acid mutation in a potassium channel that prevents inhibition by protein kinase C

Andreas E. Busch, Mihael D. Varnum, R. Alan North, John P. Adelman

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81 Scopus citations

Abstract

A slowly activating, voltage-dependent potassium channel protein cloned from rat kidney was expressed in Xenopus oocytes. Two activators of protein kinase C, 1-oleoyl-2-acetyl-rac-glycerol and phorbol 12,13-didecanoate, inhibited the current. This inhibition was blocked by the kinase inhibitor staurosporine. Inhibition of the current was not seen in channels in which Ser103 was replaced by Ala, although other properties of the current were unchanged. These results indicate that inhibition of the potassium current results from direct phosphorylation of the channel subunit protein at Ser 103.

Original languageEnglish (US)
Pages (from-to)1705-1707
Number of pages3
JournalScience
Volume255
Issue number5052
DOIs
StatePublished - Jan 1 1992

ASJC Scopus subject areas

  • General

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    Busch, A. E., Varnum, M. D., North, R. A., & Adelman, J. P. (1992). An amino acid mutation in a potassium channel that prevents inhibition by protein kinase C. Science, 255(5052), 1705-1707. https://doi.org/10.1126/science.1553557