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Related Experiment Videos

Tyr527 is phosphorylated in pp60c-src: implications for regulation.

J A Cooper, K L Gould, C A Cartwright

    Science (New York, N.Y.)
    |March 21, 1986
    PubMed
    Summary

    The Rous sarcoma virus oncogene pp60v-src transforms cells, unlike its counterpart pp60c-src. This study identifies Tyr527 phosphorylation in pp60c-src as a key difference, potentially explaining reduced kinase activity and cell transformation.

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    Area of Science:

    • Molecular Biology
    • Oncology
    • Virology

    Background:

    • pp60v-src, the oncogene product of Rous sarcoma virus, transforms fibroblasts, while its proto-oncogene counterpart, pp60c-src, does not.
    • Both pp60v-src and pp60c-src are protein-tyrosine kinases, but pp60c-src exhibits lower kinase activity.

    Purpose of the Study:

    • To investigate the molecular basis for the differential kinase activity and transforming potential between pp60v-src and pp60c-src.
    • To identify specific structural differences, particularly phosphorylation sites, that distinguish the oncogenic and proto-oncogenic forms of src.

    Main Methods:

    • Comparative analysis of pp60v-src and pp60c-src protein structures and phosphorylation patterns.
    • Site-directed mutagenesis or protein sequencing to identify key residues involved in kinase regulation.

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    Main Results:

    • Identified Tyr527, located six residues from the COOH-terminus, as the specific tyrosine residue phosphorylated in pp60c-src.
    • Observed that the C-terminal region of pp60c-src, including Tyr527, is altered in pp60v-src.
    • The loss of this negatively regulating tyrosine in pp60v-src correlates with increased transforming ability and kinase activity.

    Conclusions:

    • Phosphorylation of Tyr527 in pp60c-src acts as a negative regulator of kinase activity.
    • The structural alteration at the C-terminus, specifically the absence of Tyr527 phosphorylation, is a critical factor in the oncogenic activation of pp60v-src.
    • This finding provides insight into the mechanism of oncogene activation and potential therapeutic targets.