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Dephosphorylation of PKCδ by protein phosphatase 2Ac and its inhibition by nucleotides
Author(s) -
Srivastava Jyoti,
Goris Jozef,
Dilworth Stephen M,
Parker Peter J
Publication year - 2002
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(02)02500-0
Subject(s) - dephosphorylation , phosphatase , protein phosphatase 2 , phosphorylation , chemistry , protein kinase c , immunoprecipitation , biochemistry , protein kinase a , in vitro , in vivo , kinase , nucleotide , enzyme , microbiology and biotechnology , biology , gene
The protein phosphatases PP1 c , PP2A c and PP2Cα are shown to dephosphorylate protein kinase Cδ (PKCδ) in vitro; of these PP2A c displayed the highest specific activity towards PKCδ. The role of PP2A c in the dephosphorylation of PKCδ in cells was supported by the demonstration that these proteins could be co‐immunoprecipitated from NIH3T3 cells. However the observation that binding of Mg‐ATP to PKCδ could protect the enzyme from dephosphorylation by PP2A c in vitro indicates that an additional input/factor is required for dephosphorylation in vivo.