Negative interactions between phosphorylation of acetyl-CoA carboxylase by the cyclic AMP-dependent and AMP-activated protein kinases.
We have reported previously that cyclic AMP-dependent protein kinase phosphorylates two sites on acetyl-CoA carboxylase (site 1: Arg-Met-Ser(P)-Phe, and site 2: Ser-Ser(P)-Met-Ser-Gly-Leu), while the AMP-activated protein kinase also phosphorylates site 1, plus site 3 (Ser-Ser-Met-Ser(P)-Gly-Leu), the latter being two residues C-terminal to site 2. We now report that prior phosphorylation of site 2 by cyclic AMP-dependent protein kinase prevents the subsequent phosphorylation of site 3 and the consequent large decrease in Vmax produced by the AMP-activated protein kinase. Similarly, prior phosphorylation of site 3 by the AMP-activated protein kinase prevents subsequent phosphorylation of site 2 by cyclic AMP-dependent protein kinase.
D000103:Acetyl-CoA Carboxylase / Q000378:metabolism*; D000249:Adenosine Monophosphate / Q000494:pharmacology*; D000595:Amino Acid Sequence; D000818:Animals; D002417:Cattle; D002851:Chromatography, High Pressure Liquid; D002918:Chymotrypsin / Q000378:metabolism; D000242:Cyclic AMP / Q000494:pharmacology*; D005260:Female; D007525:Isoelectric Focusing; D007700:Kinetics; D008025:Ligases / Q000378:metabolism*; D008321:Mammary Glands, Animal / Q000201:enzymology; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000378:metabolism; D010766:Phosphorylation; D011494:Protein Kinases / Q000378:metabolism*; D051381:Rats; D014357:Trypsin / Q000378:metabolism
D010446:Peptide Fragments; D000249:Adenosine Monophosphate; D000242:Cyclic AMP; D011494:Protein Kinases; D002918:Chymotrypsin; D014357:Trypsin; D008025:Ligases; D000103:Acetyl-CoA Carboxylase