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

Paul R. Clarke, D. Grahame Hardie (Lead / Corresponding author)

Research output: Contribution to journalArticle

11 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)213-217
Number of pages5
JournalFEBS Letters
Volume269
Issue number1
DOIs
Publication statusPublished - 20 Aug 1990

Keywords

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

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