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Tyr 527 Is Phosphorylated in pp60 c- src : Implications for Regulation
Abstract
The Rous sarcoma virus oncogene product, pp60 v- src , transforms cultured fibroblasts but its corresponding proto-oncogene product, pp60 c- src , does not. Both proteins are known to be protein-tyrosine kinases. Published results suggest that the kinase activity of pp60 c- src is inhibited relative to that of pp60 v- src , due perhaps to phosphorylation of a tyrosine in pp60 c- src that is not phosphorylated in pp60 v- src . In this study, it was observed that the tyrosine phosphorylated in pp60 c- src is Tyr 527 , six residues from the COOH-terminus of the protein. The region of pp60 c- src from residue 515 to the COOH-terminus, including Tyr 527 , has been replaced with a different sequence in pp60 v- src . Thus, the increase in transforming ability and kinase activity that occurred in the genesis of pp60 v- src may have resulted from the loss of a tyrosine involved in negative regulation.
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Cites
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Irby, R. B., Mao, W., Coppola, D., Kang, J., Loubeau, J. M., Trudeau, W., Karl, R., Fujita, D. J., Jove, R., & Yeatman, T. J. (1999) · Nature Genetics · doi:10.1038/5971 · Cited by 489
Metadata
- Authors
- Cooper, J. A., Gould, K. L., Cartwright, C. A., & Hunter, T.
- Venue
- Science
- Published
- 1986-03-21
- Volume
- 231
- Issue
- 4744
- Pages
- 1431-1434
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2030577752
- Cited by
- 540
- References
- 1
- FWCI
- 21.55
- Type
- journal article
- Language
- en
- Open access
- closed
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- Cooper, J. A., Gould, K. L., Cartwright, C. A., & Hunter, T. (1986). Tyr 527 Is Phosphorylated in pp60 c- src : Implications for Regulation. Science. https://doi.org/10.1126/science.2420005
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