MOLECULAR MECHANISMS OF THE PROTEIN-SERINE THREONINE PHOSPHATASES

The dephosphorylation of proteins on their serine, threonine and tyros ine residues is catalysed by three families of protein phosphatases th at regulate numerous intracellular processes. Diversity of structure w ithin a family is generated by targeting and regulatory subunits and d omains. Structural studies of these enzymes have revealed that althoug h the two families of protein Ser/Thr phosphatases are unrelated in se quence, the architecture of their catalytic domains is remarkably simi lar and distinct from the protein tyrosine phosphatases. Insights into the molecular mechanisms of catalysis and regulation of these enzymes have been obtained.