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Characterization of sites for tyrosine phosphorylation in the transforming protein of Rous sarcoma virus (pp60v-src)

J E Smart, H Oppermann, A P Czernilofsky

    Proceedings of the National Academy of Sciences of the United States of America
    |October 1, 1981
    PubMed

    Insights

    The Rous sarcoma virus transforming protein (pp60v-src) and its cellular counterpart (pp60c-src) are tyrosine kinases. This study identifies a key tyrosine phosphorylation site (residue 419) in pp60v-src, crucial for regulating cellular function.

    Area of Science:

    • Molecular Biology
    • Virology
    • Cellular Regulation

    Background:

    • Rous sarcoma virus transforming protein (pp60v-src) and its cellular homologue (pp60c-src) function as protein kinases.
    • Phosphorylation of these proteins on serine and tyrosine residues is implicated in regulating their functions.

    Purpose of the Study:

    • To characterize the specific sites of tyrosine phosphorylation in both pp60v-src and pp60c-src.
    • To understand the regulatory mechanisms governing these protein kinases.

    Main Methods:

    • Analysis of protein phosphorylation sites in infected cells and in vitro phosphotransfer reactions.
    • Peptide sequencing to identify phosphorylated tyrosine residues.

    Main Results:

    • Tyrosine phosphorylation of pp60v-src in vivo predominantly occurs at residue 419, adjacent to acidic amino acids.
    • This specific phosphorylation site (residue 419) was also identified in vitro for pp60v-src.
    • pp60c-src exhibited distinct tyrosine phosphorylation patterns in vivo compared to in vitro, suggesting differential regulation.

    Conclusions:

    • Residue 419 represents a significant site for tyrosine phosphorylation, potentially a common regulatory site in cellular function.
    • pp60v-src and pp60c-src may be subject to different regulatory controls within the cell, impacting their functional responses.

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