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Related Experiment Videos

Structurally and functionally modified forms of pp60v-src in Rous sarcoma virus-transformed cell lysates.

M S Collett, S K Belzer, A F Purchio

    Molecular and Cellular Biology
    |July 1, 1984
    PubMed
    Summary

    Variant forms of pp60v-src (Rous sarcoma virus src gene product) with enhanced kinase activity were identified in transformed cells. These forms, characterized by amino-terminal tyrosine phosphorylation, are transient and regulated by dephosphorylation.

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    Area of Science:

    • Molecular Biology
    • Virology
    • Biochemistry

    Background:

    • pp60v-src is the 60,000 MW protein product of the Rous sarcoma virus src gene.
    • Typically, pp60v-src is phosphorylated at serine and tyrosine residues.
    • Transformed cells often exhibit altered pp60v-src forms.

    Purpose of the Study:

    • To identify and characterize variant forms of pp60v-src in transformed cells.
    • To investigate the structural modifications and enzymatic activity of these variants.
    • To understand the regulatory mechanisms of pp60v-src function.

    Main Methods:

    • Analysis of transformed cell lysates using SDS-PAGE.
    • Detection of pp60v-src variants under specific treatment conditions (vanadium ions, Mg2+, ATP-Mg2+).

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  • Correlation of structural changes with protein kinase activity.

    • Main Results:

    • Variant pp60v-src forms with altered electrophoretic mobility were identified.
    • These variants exhibit increased amino-terminal tyrosine phosphorylation.
    • Structural modifications correlated with a significant increase in pp60v-src protein kinase activity.

    Conclusions:

    • Highly active, modified forms of pp60v-src exist in transformed cells.
    • These active forms are transient and likely regulated by dephosphorylation.
    • Amino-terminal tyrosine phosphorylation enhances pp60v-src activity, with phosphotyrosyl protein phosphatase involvement in regulation.