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

Abstract

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… (More)

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Cite this paper

@article{Drake1996ARF, title={A role for tyrosine phosphorylation in both activation and inhibition of the insulin receptor tyrosine kinase in vivo.}, author={Peter Drake and Amanda Bevan and J Wesley Burgess and Jay Bergeron and Bruce Posner}, journal={Endocrinology}, year={1996}, volume={137 11}, pages={4960-8} }