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Updated: Mar 28, 2026

Recombinant α- β- and γ-Synucleins Stimulate Protein Phosphatase 2A Catalytic Subunit Activity in Cell Free Assays
Published on: August 13, 2017
11 Reversible methylation of protein phosphatase 2A
1Afdeling Biochemie, Faculteit Geneeskunde Campus Gasthuisberg O&N Katholieke Universiteit Leuven Herestraat 49 bus 901 Leuven B-3000, Belgium.
Abstract:
PP2A has been shown to be methylated at the C-terminal leucine residue of the catalytic subunit by a specific 38 kDa methyltransferase (LCMT1) and demethylated by a specific 44-kDa methylesterase (PME-1). This reversible methylation does not seem to drastically change the PP2A activity but is shown to be a modulating factor in the binding of the third regulatory subunit. The structure of LCMT1 is solved and a model for the catalysis of the methylation reaction is presented. By purifying the PP2A-methylesterase, inactive dimeric (PP2AiD) and trimeric (PP2AiT55) holoenzymes were found to be associated with PME-1. Activation of this inactive complex is possible by the action of a ubiquitous and highly conserved activatory protein, PTPA. The function of PME-1in this system seems to be independent of its demethylating activity. A large proportion of cellular PP2A is found methylated and the subject of regulation. Aberrant (de)methylation seems to be involved in the causes of diseases such as Alzheimer's disease and diabetes.
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