Specificity of different isoforms of protein phosphatase-2A and protein phosphatase-2C studied using site-directed mutagenesis of HMG-CoA reductase

Yick Pang Ching, Takayasu Kobayashi, Shinri Tamura, D. Grahame Hardie

Research output: Contribution to journalArticle

7 Citations (Scopus)

Abstract

We have expressed the catalytic domain of Chinese hamster HMG-CoA reductase, and 13 point mutations involving the region around the single phosphorylation site for AMP-activated protein kinase. After phosphorylation, these were used to test the specificity of isoforms of protein phosphatase-2A [bovine PP2A(C) (catalytic subunit) and PP2A1 (ABC heterotrimer)] and protein phosphatase-2C (human α; mouse α, β1, β2, β3, β4, β5). PP2A1 had > 50-fold higher activity for HMG-CoA reductase variants than PP2A(C), but their relative selectivity for different variants was similar. Although the specificities of PP2A and PP2C were distinct, no dramatic differences in selectivity were observed between different PP2C isoforms.

Original languageEnglish
Pages (from-to)265-268
Number of pages4
JournalFEBS Letters
Volume411
Issue number2-3
DOIs
Publication statusPublished - 1997 Jul 14

Keywords

  • AMP-activated protein kinase
  • Dephosphorylation
  • HMG-CoA reductase
  • Protein phosphatase-2A
  • Protein phosphatase-2C
  • Site-directed mutagenesis

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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