Evolutionary crossroads of cell signaling: PP1 and PP2A substrate sites in intrinsically disordered regions

Hoermann B, Köhn M.

Biochem Soc Trans. 2021; doi: 10.1042/BST20200175.

PP1 and PP2A dephosphorylate the majority of phosphorylation sites on serine and threonine. Here, we investigate the influence of protein structure and disorder on substrate amino acid recognition of the phosphatases around the phosphorylation site.