Calmodulin‐dependent multiprotein kinase and protein kinase C phosphorylate the same site on HMG‐CoA reductase as the AMP‐activated protein kinase

FEBS Letters

Grahame Hardie, D.¹  Clarke, Paul R.¹ 

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

关键词: HMG-CoA reductase;    Cholesterol synthesis;    Protein kinase;    Phosphorylation site;    Protein phosphorylation;   

DOI  :  10.1016/0014-5793(90)81157-J

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Calmodulin-dependent multiprotein kinase and protein kinase C phosphorylate and inactivate both intact, microsomal HMG-CoA reductase, and the purified 53 kDa catalytic fragment. Isolation of the single phosphopeptide produced by combined cleavage with cyanogen bromide and Lys-C proteinase reveals that this is due to phosphorylation of a single serine residue near the C-terminus, corresponding to serine-872 in the human enzyme. This is identical with the single serine phosphorylated by the AMP-activated protein kinase. The nature of the protein kinase responsible for phosphorylation of this site in vivo is discussed.

【 授权许可】

Unknown