A study of: Selective PP2A enhancement through biased heterotrimer stabilization. Leonard D, Huang W, et al.

Published: 26-02-2020| Version 1 | DOI: 10.17632/5sdnbktpg6.1
Contributor:
Daniel Leonard

Description

Here we define the structural and biological basis by which a class of small molecules (lead compound denoted DT-061), selectively binds and stabilizes a single B-subunit containing Protein Phosphatase 2A (PP2A) heterotrimer to drive the targeted dephosphorylation of select PP2A substrates that include c-MYC. This work provides structural and molecular insights into PP2A holoenzyme regulation, identifies a new therapeutic strategy for protein complex targeting and activation, and presents a basis for phosphatase activating therapeutics.

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