Phosphorylation-dephosphorylation states at different sites affect phosphoprotein phosphatase 1 activity.

We have previously reported that the binding of type I collagen to its receptor initiates platelet aggregation involving phosphoprotein phosphatase 1 (PP 1), which coprecipitates with the 65-kDa platelet type I collagen receptor. Phosphorylation of the anti-PP1 precipitation PP1 decreases its enzyme activity. In the present investigation, the mechanism of the decreased enzyme activity was studied by examining the phosphorylation of PP 1 on serine/threonine or tyrosine residues. Phosphoamino acid analysis of the PP 1 indicates that serine, threonine, and tyrosine can all be phosphorylated. We find that the activity of PP 1 decreases with serine/threonine phosphorylation but that phosphorylation of tyrosine residue activates enzyme activity. These results indicate that the activity of platelet phosphoprotein phosphatase 1 is controlled by phosphorylation and dephosphorylation states at multiple, different site(s).