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TitleSelective PP2A Enhancement through Biased Heterotrimer Stabilization.
Journal, issue, pagesCell, Vol. 181, Issue 3, Page 688-701.e16, Year 2020
Publish dateApr 30, 2020
AuthorsDaniel Leonard / Wei Huang / Sudeh Izadmehr / Caitlin M O'Connor / Danica D Wiredja / Zhizhi Wang / Nilesh Zaware / Yinghua Chen / Daniela M Schlatzer / Janna Kiselar / Nikhil Vasireddi / Stefan Schüchner / Abbey L Perl / Matthew D Galsky / Wenqing Xu / David L Brautigan / Egon Ogris / Derek J Taylor / Goutham Narla /
PubMed AbstractImpairment of protein phosphatases, including the family of serine/threonine phosphatases designated PP2A, is essential for the pathogenesis of many diseases, including cancer. The ability of PP2A to ...Impairment of protein phosphatases, including the family of serine/threonine phosphatases designated PP2A, is essential for the pathogenesis of many diseases, including cancer. The ability of PP2A to dephosphorylate hundreds of proteins is regulated by over 40 specificity-determining regulatory "B" subunits that compete for assembly and activation of heterogeneous PP2A heterotrimers. Here, we reveal how a small molecule, DT-061, specifically stabilizes the B56α-PP2A holoenzyme in a fully assembled, active state to dephosphorylate selective substrates, such as its well-known oncogenic target, c-Myc. Our 3.6 Å structure identifies molecular interactions between DT-061 and all three PP2A subunits that prevent dissociation of the active enzyme and highlight inherent mechanisms of PP2A complex assembly. Thus, our findings provide fundamental insights into PP2A complex assembly and regulation, identify a unique interfacial stabilizing mode of action for therapeutic targeting, and aid in the development of phosphatase-based therapeutics tailored against disease specific phospho-protein targets.
External linksCell / PubMed:32315618 / PubMed Central
MethodsEM (single particle)
Resolution3.63 Å
Structure data

0510

6nts

EMDB-0510, PDB-6nts:
Protein Phosphatase 2A (Aalpha-B56alpha-Calpha) holoenzyme in complex with a Small Molecule Activator of PP2A (SMAP)
Method: EM (single particle) / Resolution: 3.63 Å

Chemicals

ChemComp-L2J:
N-[(1R,2R,3S)-2-hydroxy-3-(10H-phenoxazin-10-yl)cyclohexyl]-4-(trifluoromethoxy)benzene-1-sulfonamide

ChemComp-MN:
Unknown entry

Source
  • homo sapiens (human)
KeywordsHYDROLASE/ACTIVATOR / Holoenzyme complex / Phosphatase / Activator / HYDROLASE-ACTIVATOR complex

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