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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Phosphorylation of tyrosine-416 is not required for the transforming properties and kinase activity of pp60v-src.

A mutant in src, the oncogene of Rous sarcoma virus, has been constructed in which the major phosphorylated tyrosine (Tyr-416, located in the carboxy-terminal half of the protein) has been replaced by phenylalanine. Mouse cells transformed with this mutant src form foci and grow in soft agar, indicative of a transformed state. Also, the mutant protein retains the wild-type ability to phosphorylate proteins on tyrosine. Partial proteolysis revealed that the carboxy-terminal half of the mutant protein was still phosphorylated, although apparently to a lesser extent. Analysis indicated that this residual phosphorylation was on tyrosine. We conclude that the major tyrosine phosphorylation in pp60v-src is not required for two of the protein's notable properties--protein kinase activity and transformation of cultured cells.[1]

References

  1. Phosphorylation of tyrosine-416 is not required for the transforming properties and kinase activity of pp60v-src. Snyder, M.A., Bishop, J.M., Colby, W.W., Levinson, A.D. Cell (1983) [Pubmed]
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