Transformation by polyoma virus middle T antigen.

Research output: Contribution to journalArticle

10 Citations (Scopus)

Abstract

The transforming protein of polyoma virus, middle T antigen, is a membrane-associated phosphoprotein. Middle T forms a complex with, and is phosphorylated by, a cellular tyrosine kinase pp60c-src. Mutant analysis suggests that formation of this complex is critical to transformation by polyoma. Middle T binding causes pp60c-src to autophosphorylate at novel sites in its amino terminus, and increases the specific activity of the enzyme. However, at least one non-transforming mutant of middle T, dl1015, can also activate pp60c-src in these ways. This suggests that properties of middle T other than the ability to activate pp60c-src are also necessary for transformation. These properties may include the ability to associate with a phosphatidylinositol kinase, and/or with a protein of 61 kDa. The mechanism by which middle T activates pp60c-src may involve its ability to alter the phosphorylation state of the enzyme, and thus interfere with the regulation of pp60c-src activity in vivo. Polyoma virus transformed cells might then be a good model system for investigating the control of pp60c-src activity as well as defining substrates of the enzyme.

Original languageEnglish (US)
Pages (from-to)173-182
Number of pages10
JournalCancer Surveys
Volume5
Issue number2
StatePublished - 1986
Externally publishedYes

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Polyomavirus
Viral Tumor Antigens
Enzymes
src-Family Kinases
Phosphoproteins
Phosphatidylinositols
Proteins
Phosphotransferases
Phosphorylation
Membranes

ASJC Scopus subject areas

  • Cancer Research
  • Oncology

Cite this

Transformation by polyoma virus middle T antigen. / Courtneidge, Sara.

In: Cancer Surveys, Vol. 5, No. 2, 1986, p. 173-182.

Research output: Contribution to journalArticle

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abstract = "The transforming protein of polyoma virus, middle T antigen, is a membrane-associated phosphoprotein. Middle T forms a complex with, and is phosphorylated by, a cellular tyrosine kinase pp60c-src. Mutant analysis suggests that formation of this complex is critical to transformation by polyoma. Middle T binding causes pp60c-src to autophosphorylate at novel sites in its amino terminus, and increases the specific activity of the enzyme. However, at least one non-transforming mutant of middle T, dl1015, can also activate pp60c-src in these ways. This suggests that properties of middle T other than the ability to activate pp60c-src are also necessary for transformation. These properties may include the ability to associate with a phosphatidylinositol kinase, and/or with a protein of 61 kDa. The mechanism by which middle T activates pp60c-src may involve its ability to alter the phosphorylation state of the enzyme, and thus interfere with the regulation of pp60c-src activity in vivo. Polyoma virus transformed cells might then be a good model system for investigating the control of pp60c-src activity as well as defining substrates of the enzyme.",
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