PKC modulation of minK current involves multiple phosphorylation sites.
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Wyeth-Ayerst Research, Princeton, New Jersey 08543-8000, USA.
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D000818:Animals; D003001:Cloning, Molecular; D004075:Diglycerides / Q000494:pharmacology; D006801:Humans; D051656:KCNQ Potassium Channels; D051657:KCNQ1 Potassium Channel; D008845:Microinjections; D016297:Mutagenesis, Site-Directed; D009865:Oocytes / Q000378:metabolism; D010703:Phorbol Esters / Q000494:pharmacology; D010766:Phosphorylation; D015221:Potassium Channels / Q000235:genetics* / Q000378:metabolism; D024642:Potassium Channels, Voltage-Gated; D011493:Protein Kinase C / Q000378:metabolism*; D012333:RNA, Messenger / Q000378:metabolism; D014981:Xenopus
D004075:Diglycerides; D051656:KCNQ Potassium Channels; D051657:KCNQ1 Potassium Channel; C496909:KCNQ1 protein, human; D010703:Phorbol Esters; D015221:Potassium Channels; D024642:Potassium Channels, Voltage-Gated; D012333:RNA, Messenger; C059983:potassium channel protein I(sk); C008876:phorbol-12,13-didecanoate; C038237:1-oleoyl-2-acetylglycerol; D011493:Protein Kinase C