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Related Experiment Videos

A mitotic function for Src?

S A Courtneidge1, S Fumagalli

  • 1Differentiation Programme, European Molecular Biology Laboratory, Postfach 16.2209, Meyerhofstrasse 1, 69012 Heidelberg, Germany.

Trends in Cell Biology
|October 1, 1994
PubMed
Summary
This summary is machine-generated.

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During cell division (mitosis), increased c-Src kinase activity correlates with elevated tyrosine phosphorylation of Sam68 protein. This suggests c-Src signaling may regulate RNA processing during the cell cycle.

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • c-Src protein tyrosine kinase activity elevates during mitosis.
  • Sam68, a protein interacting with Src, shows increased tyrosine phosphorylation during mitosis.
  • Sam68 shares homology with RNA-binding proteins and is related to p62, a RasGAP-associated protein.

Purpose of the Study:

  • To investigate the relationship between p62 and Sam68.
  • To clarify the roles of p62 and Sam68 in Src signaling pathways.
  • To explore the potential involvement of Src in regulating RNA processing during the cell cycle.

Main Methods:

  • Analysis of protein tyrosine phosphorylation.
  • Studies on protein-protein interactions (Src and Sam68).

Related Experiment Videos

  • Comparative analysis of Sam68 and p62 homology.

    • Main Results:

    • Src and Sam68 have been shown to interact.
    • Increased Src activity during mitosis coincides with increased Sam68 tyrosine phosphorylation.
    • Sam68 exhibits homology to RNA-binding proteins.

    Conclusions:

    • Src signaling pathways are potentially involved in regulating RNA processing.
    • The interaction between Src and Sam68 may play a role in cell cycle-dependent RNA metabolism.
    • Further research is needed to elucidate the precise roles of Sam68 and p62 in Src signaling.