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

FEBS Letters

Hardie, D.Grahame¹  Carling, David¹  Munday, Michael R.¹ 

[1] MRC Protein Phosphorylation Group, Department of Biochemistry, The University, Dundee DD1 4HN, Scotland

关键词: Acetyl-CoA carboxylase;    cyclic AMP-dependent protein kinase;    AMP-activated protein kinase;    Phosphorylation site;    Interaction;    (Rat);   

DOI  :  10.1016/0014-5793(88)81251-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown