Stimulation of the insulin receptor by ligand binding and autophosphorylation eventually leads to the activation of glycogen synthase and the translocation of glucose transporters to the plasma membrane. One strategy for treating diabetes is to develop drugs that act as inhibitors of the phosphatase enzymes that remove phosphate groups from the phosphorylated tyrosines on the insulin receptor. Why might this be an effective treatment for diabetes

By inhibiting the phosphates enzymes, the results of signal transduction will be maintained, even when insulin binding has ceased. The tyrosine of the insulin receptor will remain phosphorylated allowing for continued activation of PDK1, which will continue to phosphorylated and activate protein kinases. These protein kinases will phosphorylation and deactivate glycogen synthase kinase, allowing for continued activation of glycogen synthase. Inhibition of the phosphorylase will also allow continued translocation of glucose transporters to the plasma membrane through the continued activation of protein kinases. These responses will be allowed to occur continuously following a single binding of insulin. This would be an effective treatment for diabetes because it will amplify the cellular response to insulin.