ST recruitment of STRIPAK facilitates PP2A-mediated dephosphorylation of MAP4K4 and induces cell transformation highlighting that STRIPAK complex plays a key role in defining PP2A specificity and activity.

Molecular, cellular, and computational analyses reveal key insights into PP2A/B55α's mechanisms of substrate recruitment and active site engagement, and facilitate identification/validation of new substrates, a step towards understanding PP2A/B55α's role in multiple cellular processes.

The coupling of the enzyme/structure core to different short linear motifs represents a novel mechanism to diversify and expand the function of signaling proteins.

Systematic screen of HIV-1 Vif mutants identifies synthetic and naturally occurring amino acid polymorphisms separating PPP2R5 and APOBEC3 family protein depletion and uncovers the mechanism of Vif-dependent cell cycle arrest.

Pre-RC component Cdc6 is primed for origin licensing by phosphatases and Cdk1 inhibitor.

Time-course phosphoproteomics reveals that selective dephosphorylation is critical for directing the MI/MII transition and that, through its inherent phospho-threonine preference, PP2A-B55 imposes specific phosphoregulated behaviors that distinguish the two meiotic divisions.

A novel dynamic charge-charge interaction between B56 and a subset of PP2A-B56 substrates is essential for substrate specificity, dephosphorylation and, for KIF4A, binding condensin I.

The mechanism of inhibition by unfair competition is central to determining the protein phosphorylation states that govern cell cycle transitions between M phase and interphase.

The phosphatase Fcp1 inactivates Greatwall kinase at the end of mitosis.

DNA concentration, cyclin levels, phosphatase activity, and CDK phosphorylation combine to directly link cell size to cell division.