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Article

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).

Biochemical and biophysical research communications - 23 Mar 2007

Ikehara Tsuyoshi, Ikehara Satsuki, Imamura Shihoko, Shinjo Fukiko, Yasumoto Takeshi

Abstract excerpt

Protein phosphatase 2A (PP2A) is composed of structural (A), catalytic (C), and regulatory (B) subunits. The catalytic subunit (PP2A(C)) undergoes reversible carboxyl-methylation and -demethylation at its C-terminal leucine residue (Leu309), catalyzed by PP2A-methyltransferase (PMT) and PP2A methylesterase (PME-1), respectively. In this study, we observed that the activity of PP2A was largely unaffected by the...

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Identifiers

PMID: 17274953
DOI: 10.1016/j.bbrc.2007.01.085

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

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