[HTML][HTML] Insulin receptor-mediated p62dok tyrosine phosphorylation at residues 362 and 398 plays distinct roles for binding GTPase-activating protein and Nck and is …
A GTPase-activating protein (GAP)-associated 60-kDa protein has been found to undergo
rapid tyrosine phosphorylation in response to insulin stimulation. However, whether this
protein is a direct in vivo substrate for the insulin receptor (IR) tyrosine kinase and whether
the tyrosine phosphorylation plays a role in insulin signaling remain to be established. Here
we show that the insulin-stimulated tyrosine phosphorylation of the GAP-associated protein,
now identified as p62 dok, is inhibited by Grb10, an adaptor protein that binds directly to the …
rapid tyrosine phosphorylation in response to insulin stimulation. However, whether this
protein is a direct in vivo substrate for the insulin receptor (IR) tyrosine kinase and whether
the tyrosine phosphorylation plays a role in insulin signaling remain to be established. Here
we show that the insulin-stimulated tyrosine phosphorylation of the GAP-associated protein,
now identified as p62 dok, is inhibited by Grb10, an adaptor protein that binds directly to the …