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Tyrosine phosphorylation of three cellular proteins correlates with transformation of rat 1 cells by pp60src

A H Bouton1, S B Kanner, R R Vines

  • 1Department of Microbiology and Cancer Center, University of Virginia Health Sciences Center, Charlottesville 22908.

Molecular Carcinogenesis
|January 1, 1991
PubMed

Insights

Researchers identified three proteins whose tyrosine phosphorylation correlates with cellular transformation induced by the tyrosine kinase pp60c-src. One protein, p120, and ras-associated GTPase-activating protein (GAP) were identified, along with a novel 64-67 kDa protein interacting with GAP.

Area of Science:

  • Molecular Biology
  • Cellular Biology
  • Oncology

Background:

  • pp60c-src is a tyrosine kinase implicated in cellular transformation.
  • Understanding the downstream targets of pp60c-src is crucial for deciphering its role in cancer.

Purpose of the Study:

  • To identify proteins whose tyrosine phosphorylation is altered by pp60c-src overexpression.
  • To investigate the relationship between pp60c-src activity and cellular transformation.

Main Methods:

  • Analysis of phosphotyrosine-containing proteins in Rat 1 cells.
  • Overexpression of wild-type and variant pp60c-src tyrosine kinase.
  • Immunoprecipitation and Western blotting.

Main Results:

  • Three proteins showed correlated tyrosine phosphorylation with pp60src-induced transformation.
  • p120 and ras-associated GTPase-activating protein (GAP) were identified.
  • A novel 64-67 kDa protein, whose tyrosine phosphorylation increased with activated pp60src, was identified and shown to interact with GAP.

Conclusions:

  • pp60c-src regulates the tyrosine phosphorylation of specific cellular proteins, including p120, GAP, and a novel 64-67 kDa protein.
  • The interaction between the 64-67 kDa protein and GAP suggests a coordinated role in pp60src-mediated signaling pathways.
  • These findings contribute to understanding the molecular mechanisms of pp60src-induced cellular transformation.

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