Abstract
The 44-amino acid E5 transforming protein of bovine papillomavirus is the shortest protein known to induce tumorigenic transformation of fibroblasts. We showed previously that expression of the E5 protein activates the cellular beta receptor for platelet-derived growth factor (PDGF) and proposed that the activated receptor transmits the transforming signal to the cell. Here we use coimmunoprecipitation analysis to show that the E5 protein and the activated PDGF receptor exist in a stable complex in transformed mouse C127 cells. These results suggest a distinct mechanism of growth factor receptor activation and provide further evidence that the PDGF receptor is an important target of the E5 protein.
Publication types
-
Research Support, Non-U.S. Gov't
-
Research Support, U.S. Gov't, P.H.S.
MeSH terms
-
Animals
-
Bovine papillomavirus 1 / genetics
-
Bovine papillomavirus 1 / metabolism*
-
Cell Line, Transformed
-
Cell Transformation, Viral*
-
Electrophoresis, Polyacrylamide Gel
-
Mice
-
Molecular Weight
-
Oncogene Proteins, Viral / genetics
-
Oncogene Proteins, Viral / isolation & purification
-
Oncogene Proteins, Viral / metabolism*
-
Platelet-Derived Growth Factor / metabolism
-
Protein Binding
-
Receptors, Cell Surface / isolation & purification
-
Receptors, Cell Surface / metabolism*
-
Receptors, Platelet-Derived Growth Factor
Substances
-
Oncogene Proteins, Viral
-
Platelet-Derived Growth Factor
-
Receptors, Cell Surface
-
oncogene protein E5, Bovine papillomavirus type 1
-
Receptors, Platelet-Derived Growth Factor