Negative interactions between phosphorylation of acetyl-CoA carboxylase by the cyclic AMP-dependent and AMP-activated protein kinases

FEBS Lett. 1988 Aug 1;235(1-2):144-8. doi: 10.1016/0014-5793(88)81251-1.

Abstract

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acetyl-CoA Carboxylase / metabolism*
  • Adenosine Monophosphate / pharmacology*
  • Amino Acid Sequence
  • Animals
  • Cattle
  • Chromatography, High Pressure Liquid
  • Chymotrypsin / metabolism
  • Cyclic AMP / pharmacology*
  • Female
  • Isoelectric Focusing
  • Kinetics
  • Ligases / metabolism*
  • Mammary Glands, Animal / enzymology
  • Molecular Sequence Data
  • Peptide Fragments / metabolism
  • Phosphorylation
  • Protein Kinases / metabolism*
  • Rats
  • Trypsin / metabolism

Substances

  • Peptide Fragments
  • Adenosine Monophosphate
  • Cyclic AMP
  • Protein Kinases
  • Chymotrypsin
  • Trypsin
  • Ligases
  • Acetyl-CoA Carboxylase