The insulin receptor with phenylalanine replacing tyrosine-1146 provides evidence for separate signals regulating cellular metabolism and growth.

@article{Wilden1990TheIR,
  title={The insulin receptor with phenylalanine replacing tyrosine-1146 provides evidence for separate signals regulating cellular metabolism and growth.},
  author={Peter A. Wilden and Jonathan M. Backer and C Ronald Kahn and Deborah A Cahill and Gene J. Schroeder and Morris F. White},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={1990},
  volume={87 9},
  pages={3358-62}
}
We have studied the function of a mutant insulin receptor (IR) molecule in which Tyr-1146, one of the first autophosphorylation sites in the beta subunit, was replaced with phenylalanine (IRF1146). Autophosphorylation of the partially purified IRF1146 was reduced 60-70% when compared to the wild-type IR but was still stimulated by insulin. The phosphotransferase activity of the dephospho form of both the IR and IRF1146 toward exogenous substrates was stimulated 3- to 4-fold by insulin. However… CONTINUE READING

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