Glucagon regulation of protein phosphorylation. Identification of acetyl coenzyme A carboxylase as a substrate.
A hormonally induced change in the covalent phosphorylation state of several enzymes is generally regarded as an important mechanism for hormonal modulation of enzyme activity. We have previously demonstrated that epinephrine stimulates the phosphorylation of a peptide of Mr = 220,000 in adipocytes. Incubation of 32P-labeled cytosolic proteins from adipocytes and hepatocytes with antisera raised against homogeneous chicken and rat liver acetyl coenzyme A carboxylase results in the specific and complete precipitation of the same phosphopeptide. No other major phosphopeptide is specifically precipitated. In hepatocytes, glucagon stimulates the incorporation of 32P into this peptide associated with an inhibition of enzyme activity. These data, coupled with previous studies in adipocytes, suggest that cyclic AMP-dependent protein phosphorylation plays a major role in the regulation of acetyl-CoA carboxylase activity and of fatty acid biosynthesis in adipose tissue and liver.
D000103:Acetyl-CoA Carboxylase / Q000378:metabolism*; D000273:Adipose Tissue / Q000187:drug effects / Q000201:enzymology*; D000818:Animals; D003600:Cytosol / Q000201:enzymology; D004789:Enzyme Activation; D005934:Glucagon / Q000494:pharmacology*; D008025:Ligases / Q000378:metabolism*; D008099:Liver / Q000187:drug effects / Q000201:enzymology*; D008297:Male; D008970:Molecular Weight; D010766:Phosphorylation; D011494:Protein Kinases / Q000378:metabolism; D051381:Rats
D005934:Glucagon; D011494:Protein Kinases; D008025:Ligases; D000103:Acetyl-CoA Carboxylase