Journal
EMBO JOURNAL
Volume 19, Issue 21, Pages 5682-5691Publisher
WILEY
DOI: 10.1093/emboj/19.21.5682
Keywords
phosphoprotein phosphatase 2A regulation; protein methylesterase; protein methyltransferase; signal transduction
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Funding
- NIGMS NIH HHS [GM61284, R01 GM061284] Funding Source: Medline
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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 13 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 diners.
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