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Carboxyl methylation regulates phosphoprotein phosphatase 2A by controlling the association of regulatory B subunits
Author(s) -
Tolstykh Tatiana,
Lee Jookyung,
Vafai Scott,
Stock Jeffry B.
Publication year - 2000
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1093/emboj/19.21.5682
Subject(s) - protein phosphatase 2 , biology , protein subunit , heterotrimeric g protein , methylation , phosphatase , biochemistry , phosphoserine , phosphoprotein , dephosphorylation , dusp6 , serine , demethylation , methyltransferase , phosphorylation , microbiology and biotechnology , signal transduction , dna methylation , g protein , gene , gene expression
Phosphoprotein phosphatase 2A (PP2A) is a major phosphoserine/threonine protein phosphatase in all eukaryotes. It has been isolated as a heterotrimeric holoenzyme composed of a 65 kDa A subunit, which serves as a scaffold for the association of the 36 kDa catalytic C subunit, and a variety of B subunits that control phosphatase specificity. The C subunit is reversibly methyl esterified by specific methyltransferase and methylesterase enzymes at a completely conserved C‐terminal leucine residue. Here we show that methylation plays an essential role in promoting PP2A holoenzyme assembly and that demethylation has an opposing effect. Changes in methylation indirectly regulate PP2A phosphatase activity by controlling the binding of regulatory B subunits to AC dimers.