A role for tyrosine phosphorylation in both activation and inhibition of the insulin receptor tyrosine kinase in vivo.

@article{Drake1996ARF,
  title={A role for tyrosine phosphorylation in both activation and inhibition of the insulin receptor tyrosine kinase in vivo.},
  author={Paul G. Drake and A. Paul Bevan and J Wesley Burgess and John J. M. Bergeron and Barry I. Posner},
  journal={Endocrinology},
  year={1996},
  volume={137 11},
  pages={4960-8}
}
Upon insulin binding, a conformational change in the insulin receptor (IR) leads to IR beta-subunit autophosphorylation, an increase in IR beta-subunit exogenous tyrosine kinase activity, and the rapid endocytosis of the ligand-receptor complex into endosomes. Previous work has shown that upon internalization, rat hepatic endosomal IRs manifest increased autophosphorylating and exogenous tyrosine kinase activity compared to IRs located at the plasma membrane. As this period of enhanced activity… CONTINUE READING

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