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Related Experiment Videos

Protein phosphorylation and growth control.

T Hunter, C B Alexander, J A Cooper

    Ciba Foundation Symposium
    |January 1, 1985
    PubMed
    Summary
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    Tyrosine phosphorylation of the protein p42 is a conserved response to various mitogens, including growth factors like EGF and PDGF. This rapid, transient phosphorylation suggests p42 plays a key role in early cellular responses to mitogenic signals.

    Area of Science:

    • Cellular Biology
    • Molecular Biology
    • Biochemistry

    Background:

    • Many growth factor receptors and viral proteins activate protein-tyrosine kinases.
    • These kinases phosphorylate target proteins on tyrosine residues.
    • Several substrates for protein-tyrosine kinases have been identified.

    Purpose of the Study:

    • To investigate the role of protein p42 phosphorylation in cellular responses to mitogens.
    • To determine the signaling pathways involved in p42 tyrosine phosphorylation.
    • To assess the conservation and generality of p42 phosphorylation as a cellular response.

    Main Methods:

    • Treatment of quiescent fibroblasts with various mitogens, including EGF, PDGF, IGF I, insulin, TPA, and thrombin.
    • Analysis of protein phosphorylation patterns using biochemical assays.

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  • Quantification of p42 phosphorylation stoichiometry.

    • Main Results:

    • EGF and PDGF treatment rapidly and transiently induced tyrosine phosphorylation of p42 in quiescent fibroblasts.
    • p42 phosphorylation was also observed in response to IGF I, insulin, TPA, and thrombin.
    • p42 is a highly conserved, rare, soluble cytoplasmic protein, with over 50% phosphorylation at saturating mitogen levels.

    Conclusions:

    • Tyrosine phosphorylation of p42 is a highly conserved and general response to mitogenic stimuli.
    • This phosphorylation event is likely crucial for early cellular responses to mitogens.
    • The signaling pathways may involve both direct protein-tyrosine kinase activation and indirect mechanisms.