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- W243055719 abstract "G protein-activated inwardly rectifying K + channels (GIRK) are inhibited by activation of protein kinase C (PKC), but the exact mechanisms are not known. GIRK channels in the heart are heterotetrama composed of GIRKI andGIRK4 subunits. We investigated the phosphorylation sites by site-directed mutagenesis procedure in GIRK4 subunits heterologously expressed in Xenopus oocytes. Homomeric wild type (WT) GIRK4 current amplitude was inhibited by phorbor-1,2 myrisitate-acetate (PMA: a PKC activator), by 45.5′1.8% (n=5). Serine or theorine at five potential phosphorylation sites of GIRK4 channel were replaced by alanine to prepare five different single mutants and a penta mutant with replacement of all the sites. PMA (I μM) application to these mutant GIRK4 channels resulted in a similar reduction of current amplitude (by 45-62%) as observed in WT channels (by 45.5′1.8%). From these observations, it is suggested that an inhibition of GIRK4 channels by PKC activation is not mediated by direct phosphorylation of the channel protein. Instead, some indirect PKC actions on other molecules may be involved." @default.
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- W243055719 date "2002-12-01" @default.
- W243055719 modified "2023-09-28" @default.
- W243055719 title "Molecular Mechanisms for Regulation of the G Protein-activated Inwardly Rectifying K^+ (GIRK) Channels by Protein Kinase C" @default.
- W243055719 doi "https://doi.org/10.18999/envm.46.81" @default.
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