Phosphorylation of tyrosine-416 is not required for the transforming properties and kinase activity of pp60v-src |
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Authors: | M A Snyder J M Bishop W W Colby A D Levinson |
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Institution: | 1. Department of Microbiology University of California San Francisco, California 94143 USA;2. Department of Molecular Biology Genentech Inc. 460 Pt. San Bruno Blvd. South San Francisco, California 94080 USA |
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Abstract: | 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in which the major phosphorylated tyrosine (Tyr-416, located in the carboxy-terminal half of the protein) has been replaced by phenylalanine.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. |
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