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

FEBS Lett. 1990 Aug 20;269(1):213-7. doi: 10.1016/0014-5793(90)81157-j.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Calcium-Calmodulin-Dependent Protein Kinases
  • Hydrogen-Ion Concentration
  • Hydroxymethylglutaryl CoA Reductases / metabolism*
  • Microsomes / enzymology
  • Molecular Sequence Data
  • Peptide Fragments / analysis
  • Phosphorylation
  • Phosphoserine / metabolism
  • Protein Kinase C / metabolism*
  • Protein Kinases / metabolism*
  • Rats

Substances

  • Peptide Fragments
  • Phosphoserine
  • Hydroxymethylglutaryl CoA Reductases
  • Protein Kinases
  • Protein Kinase C
  • Calcium-Calmodulin-Dependent Protein Kinases