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.

The regulation of the core transcription factor Oct4 by the Aurkb-PP1 axis links the cell cycle to pluripotency programs in embryonic stem cells.

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.

Leaf position, shape and orientation are pre-patterned by cell type boundaries in the shoot meristem.

Nanodomain clustering of cAMP effectors represents a novel mechanism of cAMP compartmentation within an oscillatory signaling circuit.

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

The deacetylase Sir2 fine-tunes transcription of PMA1 and other aging related genes in a cAMP-PKA and CK2 signaling dependent manner.

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.