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Related Experiment Videos

A target for Src in mitosis

S Fumagalli1, N F Totty, J J Hsuan

  • 1European Molecular Biology Laboratory, Heidelberg, Germany.

Nature
|April 28, 1994
PubMed
Summary
This summary is machine-generated.

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The study identified a 68 kDa protein (p68) whose tyrosine phosphorylation is significantly enhanced during mitosis in Src-transformed cells. This protein interacts with c-Src, suggesting a role in cell cycle regulation and cancer progression.

Area of Science:

  • Cell Biology
  • Molecular Oncology
  • Protein Phosphorylation

Background:

  • c-Src protein activity increases during specific cell cycle phases (G1, G2/M).
  • Src substrates during these phases are poorly understood.
  • Src-transformed cells exhibit widespread protein tyrosine phosphorylation.

Purpose of the Study:

  • To compare phosphotyrosine content in growing vs. mitotically arrested Src-transformed cells.
  • To identify Src substrates regulated during mitosis.
  • To investigate the role of p68 in Src-mediated signaling.

Main Methods:

  • Comparative analysis of phosphotyrosine content.
  • Co-immunoprecipitation to assess protein association.
  • In vitro binding assays using SH3 domains.

Related Experiment Videos

  • Protein purification and microsequencing.

    • Main Results:

    • A ~68 kDa protein (p68) showed greatly enhanced phosphorylation during mitosis.
    • p68 was physically associated with activated c-Src.
    • p68 bound to the c-Src SH3 domain in vitro.
    • Tyrosine-phosphorylated p68 was also found in mitotic extracts of normal cells.
    • p68 was identified as related to GAP-associated protein p62.

    Conclusions:

    • Mitotic phosphorylation of p68 is enhanced by c-Src.
    • p68 is a novel substrate or binding partner of c-Src.
    • The phosphorylation of p68 is not solely a consequence of transformation.
    • p68 may play a role in regulating cell division or mitosis.