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Negative interactions between phosphorylation of acetyl‐CoA carboxylase by the cyclic AMP‐dependent and AMP‐activated protein kinases
Author(s) -
Munday Michael R.,
Carling David,
Hardie D.Grahame
Publication year - 1988
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(88)81251-1
Subject(s) - phosphorylation , protein kinase a , acetyl coa carboxylase , protein phosphorylation , cyclin dependent kinase 2 , biochemistry , kinase , chemistry , map2k7 , mitogen activated protein kinase kinase , cgmp dependent protein kinase , biology , pyruvate carboxylase , enzyme
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.