DOI: 10.1126/science.2420005. Tyr 527 Is Phosphorylated in pp60 c- src : Implications for Regulation

Tyr 527 Is Phosphorylated in pp60 c- src : Implications for Regulation

10.1126/science.2420005

Crossref journal-article

American Association for the Advancement of Science (AAAS)

Science (221)

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.

Bibliography

Cooper, J. A., Gould, K. L., Cartwright, C. A., & Hunter, T. (1986). Tyr 527 Is Phosphorylated in pp60 c- src â¯: Implications for Regulation. Science, 231(4744), 1431â1434.

Authors 4

Jonathan A. Cooper (first)
Kathleen L. Gould (additional)
Christine A. Cartwright (additional)
Tony Hunter (additional)

References 41 Referenced 409

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Dates

Type	When
Created	18 years, 10 months ago (Oct. 5, 2006, 4:28 p.m.)
Deposited	1 year, 7 months ago (Jan. 12, 2024, 11:33 a.m.)
Indexed	1 month, 4 weeks ago (July 2, 2025, 2:46 p.m.)
Issued	39 years, 5 months ago (March 21, 1986)
Published	39 years, 5 months ago (March 21, 1986)
Published Print	39 years, 5 months ago (March 21, 1986)

Funders 0

None

BibTeX

@article{Cooper_1986, title={Tyr 527 Is Phosphorylated in pp60 c- src  : Implications for Regulation}, volume={231}, ISSN={1095-9203}, url={http://dx.doi.org/10.1126/science.2420005}, DOI={10.1126/science.2420005}, number={4744}, journal={Science}, publisher={American Association for the Advancement of Science (AAAS)}, author={Cooper, Jonathan A. and Gould, Kathleen L. and Cartwright, Christine A. and Hunter, Tony}, year={1986}, month=mar, pages={1431–1434} }

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  "abstract": "<jats:p>\n            The Rous sarcoma virus oncogene product, pp60\n            <jats:sup>\n              v-\n              <jats:italic>src</jats:italic>\n            </jats:sup>\n            , transforms cultured fibroblasts but its corresponding proto-oncogene product, pp60\n            <jats:sup>\n              c-\n              <jats:italic>src</jats:italic>\n            </jats:sup>\n            , does not. Both proteins are known to be protein-tyrosine kinases. Published results suggest that the kinase activity of pp60\n            <jats:sup>\n              c-\n              <jats:italic>src</jats:italic>\n            </jats:sup>\n            is inhibited relative to that of pp60\n            <jats:sup>\n              v-\n              <jats:italic>src</jats:italic>\n            </jats:sup>\n            , due perhaps to phosphorylation of a tyrosine in pp60\n            <jats:sup>\n              c-\n              <jats:italic>src</jats:italic>\n            </jats:sup>\n            that is not phosphorylated in pp60\n            <jats:sup>\n              v-\n              <jats:italic>src</jats:italic>\n            </jats:sup>\n            . In this study, it was observed that the tyrosine phosphorylated in pp60\n            <jats:sup>\n              c-\n              <jats:italic>src</jats:italic>\n            </jats:sup>\n            is Tyr\n            <jats:sup>527</jats:sup>\n            , six residues from the COOH-terminus of the protein. The region of pp60\n            <jats:sup>\n              c-\n              <jats:italic>src</jats:italic>\n            </jats:sup>\n            from residue 515 to the COOH-terminus, including Tyr\n            <jats:sup>527</jats:sup>\n            , has been replaced with a different sequence in pp60\n            <jats:sup>\n              v-\n              <jats:italic>src</jats:italic>\n            </jats:sup>\n            . Thus, the increase in transforming ability and kinase activity that occurred in the genesis of pp60\n            <jats:sup>\n              v-\n              <jats:italic>src</jats:italic>\n            </jats:sup>\n            may have resulted from the loss of a tyrosine involved in negative regulation.\n          </jats:p>",
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