Administration of insulin to rats caused a transient increase in the amount of hepatic insulin receptor present in clathrin-coated vesicles and endosomes. However, the total ‘in vitro’ insulin stimulated tyrosine kinase activity of the receptor present in endosomes did not vary when expressed per mg of protein and decreased when expressed per β-subunit content. A decrease in the endogenous phospho tyrosine content of the receptor β-subunit was observed in endosomes in response to insulin. This indicates that a fraction of the internalized receptor is dephosphorylated in endosomes, which renders it unable to become stimulated by insulin ‘in vitro’.
