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Four different classes of retroviruses induce phosphorylation of tyrosines present in similar cellular proteins

J A Cooper1, T Hunter

  • 1Salk Institute, San Diego, California 92138.

Molecular and Cellular Biology
|May 1, 1981
PubMed

Insights

Four unrelated classes of transforming retroviruses induce tyrosine phosphorylation in the same cellular proteins. These phosphoproteins may be substrates for viral tyrosine-specific protein kinases, suggesting a common mechanism in viral transformation.

Area of Science:

  • Oncology
  • Virology
  • Molecular Biology

Background:

  • Viral transformation of cells can involve alterations in protein phosphorylation.
  • Specific retroviruses encode tyrosine-specific protein kinases that mediate cellular changes.

Purpose of the Study:

  • To investigate the phosphoprotein changes induced by different classes of transforming retroviruses.
  • To determine if these viruses target common cellular proteins for tyrosine phosphorylation.

Main Methods:

  • Analysis of phosphoprotein profiles in chicken embryo cells and mouse 3T3 cells transformed by various retroviruses.
  • Identification of phosphoproteins containing phosphotyrosine.

Main Results:

  • Chicken embryo cells transformed by PRC II, Fujinami sarcoma virus, Y73, or Rous sarcoma virus showed increased levels of specific phosphoproteins.
  • These phosphoproteins contained phosphotyrosine and were potential substrates for viral tyrosine kinases.
  • A homologous protein was phosphorylated at the same site in mouse 3T3 cells transformed by Rous sarcoma virus or Abelson murine leukemia virus.
  • A second phosphotyrosine-containing protein was identified in Rous sarcoma virus and Abelson murine leukemia virus-transformed cells.

Conclusions:

  • Representatives of four unrelated classes of transforming retroviruses induce tyrosine phosphorylation in the same set of cellular proteins.
  • This suggests a conserved mechanism of cellular protein modification across diverse viral transforming agents.

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