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 language | English (US) |
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Pages (from-to) | 595-597 |
Number of pages | 3 |
Journal | Trends in pharmacological sciences |
Volume | 41 |
Issue number | 9 |
DOIs | |
State | Published - Sep 2020 |
Keywords
- MYC
- SMAP
- cancer
- phosphatase
ASJC Scopus subject areas
- Toxicology
- Pharmacology