[Phosphorylation of the receptor insulin and insulin-like growth factors].
We have found that the beta-subunit of the insulin receptor is a phosphoprotein and that the degree of phosphorylation is increased by the binding of insulin to its receptor. Furthermore we have found that the beta-subunit of the insulin receptor itself is a tyrosine-specific protein kinase. Tyrosine-specific protein kinases have been reported to be associated with the transforming gene product of RNA tumor viruses, the EGF receptor, the IGF-I receptor and a protein believed to be the receptor for PDGF. These findings suggest that determination of the endogenous substrated for these tyrosine-specific protein kinases may yield a sequence of regulatory proteins for cell growth and transformation. From this point of view, our recent findings that the purified insulin receptor-kinase can phosphorylate purified microtubule protein (tubulin, MAP2, tau) are interesting.
D000818:Animals; D002455:Cell Division; D002471:Cell Transformation, Neoplastic; D004267:DNA Viruses / Q000378:metabolism; D007328:Insulin / Q000378:metabolism*; D008114:Liver Neoplasms, Experimental / Q000378:metabolism / Q000473:pathology; D010455:Peptides / Q000378:metabolism*; D010766:Phosphorylation; D010982:Platelet-Derived Growth Factor; D011494:Protein Kinases / Q000096:biosynthesis; D011505:Protein-Tyrosine Kinases; D051381:Rats; D011972:Receptor, Insulin / Q000378:metabolism*; D012190:Retroviridae / Q000378:metabolism; D013002:Somatomedins / Q000378:metabolism*
D007328:Insulin; D010455:Peptides; D010982:Platelet-Derived Growth Factor; D013002:Somatomedins; D011494:Protein Kinases; D011505:Protein-Tyrosine Kinases; D011972:Receptor, Insulin