Select Stabilization of a Tumor-Suppressive PP2A Heterotrimer. (September 2020)

• Record Type: Journal Article
• Authors: Shah, Vidhi M.; English, Isabel A.; Sears, Rosalie C.
• Is Part Of: Trends in pharmacological sciences. Volume 41:Number 9(2020)
• Page Start: 595
• Page End: 597
• Publication Date: 2020-09
• Subjects: phosphatase -- cancer -- MYC -- SMAP; Pharmacology -- Periodicals; Pharmacology -- trends -- Periodicals; Pharmacologie -- Périodiques; Pharmacology; Electronic journals; Periodicals; 615.1
• DOI: 10.1016/j.tips.2020.06.008
• Languages: English
• ISSNs: 0165-6147

Abstract

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.