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Methylation of the C-terminal leucine residue of the PP2A catalytic subunit is unnecessary for the catalytic activity and the binding of regulatory subunit (PR55/B)
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Structure of the protein phosphatase 2A holoenzyme
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A novel assay for protein phosphatase 2A (PP2A) complexes in vivo reveals differential effects of covalent modifications on different Saccharomyces cerevisiae PP2A heterotrimers
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Protein tyrosine phosphatases in the human genome
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An inactive protein phosphatase 2A population is associated with methylesterase and can be re-activated by the phosphotyrosyl phosphatase activator
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Identification and functional analysis of two Ca2+-binding EF-hand motifs in the B/PR72 subunit of protein phosphatase 2A
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Alterations in protein phosphatase 2A subunit interaction in human carcinomas of the lung and colon with mutations in the Aβ subunit gene
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Initial sequencing and analysis of the human genome
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Inhibition of PP-2A upregulates CaMKII in rat forebrain and induces hyperphosphorylation of tau at Ser 262/356
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Carboxymethylation of the PP2A catalytic subunit in Saccharomyces cerevisiae is required for efficient interaction with the B-type subunits CDC55p and RTS1p
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Disruption of protein phosphatase 2A subunit interaction in human cancers with mutations in the Aα subunit gene
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Methylation of the protein phosphatase 2A catalytic subunit is essential for association of B alpha regulatory subunit but not SG2NA, striatin, or polyomavirus middle tumor antigen
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Crystal structure of a β-catenin/Tcf complex
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Carboxyl methylation of the phosphoprotein phosphatase 2A catalytic subunit promotes its functional association with regulatory subunits in vivo
J Wu et al.
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