Premium
Specificity of different isoforms of protein phosphatase‐2A and protein phosphatase‐2C studied using site‐directed mutagenesis of HMG‐CoA reductase
Author(s) -
Pang Ching Yick,
Kobayashi Takayasu,
Tamura Shinri,
Grahame Hardie D
Publication year - 1997
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(97)00712-6
Subject(s) - protein phosphatase 2 , phosphatase , gene isoform , phosphorylation , protein subunit , biochemistry , reductase , chemistry , microbiology and biotechnology , mutagenesis , protein kinase a , biology , enzyme , mutant , gene
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 PP2A 1 (ABC heterotrimer)] and protein phosphatase‐2C (human α; mouse α, β1, β2, β3, β4, β5). PP2A 1 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.