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pp60c-src is a substrate for phosphorylation when cells are stimulated to enter cycle

FEBS Letters
|November 5, 1984
PubMed

Insights

The cellular oncogene pp60c-src (proto-oncogene c-Src) shows increased serine phosphorylation when quiescent cells are stimulated to proliferate. This suggests a role for pp60c-src in cell cycle control.

Area of Science:

  • Molecular Biology
  • Cell Biology
  • Oncogenes

Background:

  • The proto-oncogene c-Src (pp60c-src) is an endogenous cellular oncogene product.
  • pp60c-src possesses protein kinase activity and is itself a phosphoprotein.

Purpose of the Study:

  • To investigate the role of pp60c-src in cell proliferation control.
  • To study the phosphorylation of pp60c-src as a substrate during cell cycle entry.

Main Methods:

  • Partial purification of pp60c-src using DEAE ion-exchange chromatography.
  • Immune precipitation techniques were employed.
  • Analysis of pp60c-src phosphorylation in quiescent cells stimulated with serum, platelet-derived growth factor, or 12-O-tetradecanoyl-phorbol-13-acetate.

Main Results:

  • A 2-4 fold increase in serine phosphorylation of pp60c-src was consistently observed.
  • Phosphorylation levels increased upon stimulation of quiescent cells to enter the cell cycle.

Conclusions:

  • pp60c-src phosphorylation is enhanced when cells are stimulated to grow.
  • These findings support the hypothesis that pp60c-src plays a role in the regulation of cell proliferation.

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