The E5 oncoprotein of bovine papillomavirus binds to a 16 kd cellular protein.
AUTOR(ES)
Goldstein, D J
RESUMO
The E5 oncoprotein of bovine papillomavirus type 1 is the smallest known viral transforming protein. It is a 44 amino acid polypeptide asymmetrically oriented in Golgi and plasma membranes which appears to modify (either directly or indirectly) the internalization and phosphorylation of at least two growth factor receptors: EGF and CSF-1. To identify cellular proteins associated with E5, we have constructed two E5 fusion proteins, each of which contains a well-characterized epitope at the E5 amino terminus. These E5-epitope fusion proteins are biologically active, localize normally to cellular membranes and form dimers. Both monoclonal and polyclonal antibodies against the inserted epitopes specifically co-precipitate E5 and an associated 16 kd cellular protein. A transformation-defective E5 mutant containing a substitution within the hydrophobic portion of E5 is defective in its ability to bind the 16 kd protein. These findings suggest a role for E5/16 kd binding in the process of cellular transformation.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=551639Documentos Relacionados
- Cellular transformation by a transmembrane peptide: structural requirements for the bovine papillomavirus E5 oncoprotein.
- Genetic and biochemical definition of the bovine papillomavirus E5 transforming protein.
- Activation of the platelet-derived growth factor receptor by the bovine papillomavirus E5 transforming protein.
- Platelet-derived growth factor receptor can mediate tumorigenic transformation by the bovine papillomavirus E5 protein.
- The E5 oncoprotein of human papillomavirus type 16 inhibits the acidification of endosomes in human keratinocytes.