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.
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.
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.
Distinct PP2A-B56 complexes use isoform-selective interactions to localise to either the centromere or kinetochore and control different processes during mitosis.
Structures of active and inactive conformations of a PP2C family phosphatase reveal a conserved switch that controls enzymatic activity and point to an unexpected relationship between phosphatases and proteasomal proteases.
A comprehensive whole cell proteomic map describing expression time courses of >6,500 viral and cellular proteins during HIV infection identifies Vif-dependent antagonism of key cellular phosphatase PP2A.
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.