Select Stabilization of a Tumor-Suppressive PP2A Heterotrimer

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 re...

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Bibliographic Details
Published in:Trends in pharmacological sciences (Regular ed.) 2020-09, Vol.41 (9), p.595-597
Main Authors: Shah, Vidhi M., English, Isabel A., Sears, Rosalie C.
Format: Article
Language:English
Subjects:
cancer
Cryoelectron Microscopy
Humans
MYC
Neoplasms - drug therapy
phosphatase
Protein Phosphatase 2 - metabolism
Signal Transduction
SMAP
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Summary: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.
ISSN:0165-6147
1873-3735
DOI:10.1016/j.tips.2020.06.008