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.
Interaction of cofactor Phactr1 with PP1 creates a composite substrate-binding surface that defines the sequence specificity of the Phactr1/PP1 holoenzyme.
A complex interplay between MAST3 and PKA protein kinases and the regulatory protein ARPP-16 allows cAMP to control the activity of protein phosphatase 2A.
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.