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Related Experiment Videos

c-Src and mitosis.

D Shalloway1, S Bagrodia, I Chackalaparampil

  • 1Section of Biochemistry, Molecular and Cell Biology, Cornell University, Ithaca, NY 14853.

Ciba Foundation Symposium
|January 1, 1992
PubMed
Summary
This summary is machine-generated.

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The proto-oncoprotein pp60c-src kinase activity increases during mitosis, regulated by phosphorylation and dephosphorylation events. Further research is needed to fully understand cell cycle control of pp60c-src activity.

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • The proto-oncoprotein pp60c-src's transforming potential and function correlate with its protein tyrosine kinase activity.
  • Cell cycle regulation of pp60c-src activity is crucial for its physiological role.

Purpose of the Study:

  • To investigate the cell cycle-dependent regulation of pp60c-src protein tyrosine kinase activity.
  • To elucidate the mechanisms controlling pp60c-src activity during mitosis.

Main Methods:

  • Used mouse fibroblasts overexpressing chicken or mouse pp60c-src.
  • Analyzed pp60c-src phosphorylation at serine, threonine, and tyrosine residues.
  • Assayed in vitro tyrosine kinase activity.
  • Utilized kinase-defective mutants and site-directed mutagenesis.

Related Experiment Videos

  • Treated cells with okadaic acid, a serine/threonine phosphatase inhibitor.

    • Main Results:

    • pp60c-src is phosphorylated by p34cdc2 at specific serine/threonine residues during mitosis.
    • Mitotic pp60c-src exhibits increased tyrosine kinase activity (approx. twofold) and SH2 domain accessibility (approx. 15-fold).
    • Phosphorylation at Tyr527 negatively regulates kinase activity; kinase-defective mutants show reduced Tyr527 phosphorylation during mitosis.
    • Mutating mitosis-specific phosphorylation sites partially blocks but does not abolish mitotic regulation of kinase activity and Tyr527 dephosphorylation.
    • Okadaic acid treatment stimulates pp60c-src kinase activity and decreases Tyr527 phosphorylation, suggesting phosphatase involvement.

    Conclusions:

    • p34cdc2-mediated phosphorylation is a key event, but not the sole regulator of, cell cycle-dependent pp60c-src activity.
    • Additional regulatory events, potentially involving phosphatases, contribute to the precise control of pp60c-src activity during the cell cycle.
    • Further investigation into the interplay of kinases and phosphatases acting on Tyr527 is warranted.