CALMODULIN-DEPENDENT MULTIPROTEIN KINASE AND PROTEIN-KINASE-C PHOSPHORYLATE THE SAME SITE ON HMG-COA REDUCTASE AS THE AMP-ACTIVATED PROTEIN-KINASE

被引：13

作者：

CLARKE, PR ^{[1
]}

HARDIE, DG ^{[1
]}

机构：

[1] UNIV DUNDEE,DEPT BIOCHEM,PROT PHOSPHORYLAT GRP,DUNDEE DD1 4HN,SCOTLAND

来源：

FEBS LETTERS | 1990年 / 269卷 / 01期

基金：

英国惠康基金;

关键词：

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

D O I：

10.1016/0014-5793(90)81157-J

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

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. © 1990.

引用

页码：213 / 217

页数：5

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