Carboxyl methylation regulates phosphoprotein phosphatase 2A by controlling the association of regulatory B subunits

Tatiana Tolstykh, Jookyung Lee, Scott Vafai, Jeffry B. Stock

Research output: Contribution to journalArticle

176 Scopus citations

Abstract

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.

Original languageEnglish (US)
Pages (from-to)5682-5691
Number of pages10
JournalEMBO Journal
Volume19
Issue number21
DOIs
StatePublished - Nov 1 2000

All Science Journal Classification (ASJC) codes

  • Neuroscience(all)
  • Molecular Biology
  • Biochemistry, Genetics and Molecular Biology(all)
  • Immunology and Microbiology(all)

Keywords

  • Phosphoprotein phosphatase 2a regulation
  • Protein methylesterase
  • Protein methyltransferase
  • Signal transduction

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