Phosphorylation of the alpha subunit of the sodium channel by protein kinase C.
The alpha subunit of the purified voltage-sensitive sodium channel from rat brain is rapidly phosphorylated to the extent of 3-4 mol phosphate/mol by purified protein kinase C. The alpha subunit of the native sodium channel in synaptosomal membranes is also phosphorylated by added protein kinase C as assessed by specific immunoprecipitation and polyacrylamide gel electrophoresis of labeled membranes. Our results suggest coordinate regulation of sodium channel phosphorylation state by cAMP-dependent and calcium/phospholipid-dependent protein kinases.
D000818:Animals; D001921:Brain / Q000201:enzymology; D001923:Brain Chemistry; D002384:Catalysis; D007473:Ion Channels / Q000378:metabolism*; D007700:Kinetics; D009419:Nerve Tissue Proteins / Q000378:metabolism*; D010766:Phosphorylation; D011493:Protein Kinase C; D011494:Protein Kinases / Q000378:metabolism*; D051381:Rats; D013574:Synaptosomes / Q000378:metabolism
D007473:Ion Channels; D009419:Nerve Tissue Proteins; D011494:Protein Kinases; D011493:Protein Kinase C