Analysis of mutant forms of the c-src gene product containing a phenylalanine substitution for tyrosine 416.

@article{Ferracini1990AnalysisOM,
  title={Analysis of mutant forms of the c-src gene product containing a phenylalanine substitution for tyrosine 416.},
  author={R Ferracini and Joan S. Brugge},
  journal={Oncogene research},
  year={1990},
  volume={5 3},
  pages={205-19}
}
Several lines of evidence suggest that phosphorylation of tyrosine residue 416 (Tyr416) has a positive regulatory influence on the functional activity of the protein tyrosine kinase pp60c-src. To further examine the functional importance of phosphorylation at Tyr416, we have eliminated this phosphoacceptor site in four functionally unique mutant forms of the c-src gene product that are phosphorylated on Tyr416 in vivo. Substitution of phenylalanine for Tyr416 suppressed the biological activity… CONTINUE READING

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