Select Stabilization of a Tumor-Suppressive PP2A Heterotrimer

Vidhi M. Shah, Isabel A. English, Rosalie C. Sears

Research output: Contribution to journalShort surveypeer-review

Abstract

In cancer, suppression of protein phosphatases, such as protein phosphatase 2A (PP2A), that normally counteract kinases, contributes to aberrant signaling. Leonard et al. recently demonstrated that a novel small-molecule activator of PP2A, DT-061, selectively stabilizes a specific PP2A holoenzyme responsible for dephosphorylating critical oncogenic targets, including MYC. The 3.6-Å cryo-electron microscopy map of the heterotrimer assembly provides insight into the druggable structure of PP2A, guiding future phosphatase therapeutics.

Original languageEnglish (US)
Pages (from-to)595-597
Number of pages3
JournalTrends in pharmacological sciences
Volume41
Issue number9
DOIs
StatePublished - Sep 2020

Keywords

  • MYC
  • SMAP
  • cancer
  • phosphatase

ASJC Scopus subject areas

  • Toxicology
  • Pharmacology

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