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

1988; Wiley; Volume: 235; Issue: 1-2 Linguagem: Inglês

10.1016/0014-5793(88)81251-1

1873-3468

Michael R. Munday, David Carling, D. Grahame Hardie,

Neurological diseases and metabolism

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 V max 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.