ArticleJournal of virology1995
Mutational analysis of the interaction between the bovine papillomavirus E5 transforming protein and the endogenous beta receptor for platelet-derived growth factor in mouse C127 cells.
Article in Journal of virology, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed, 56 citations in OpenAlex.
- New approach for genomic characterisation of equine sarcoid-derived BPV-1/-2 using nanopore-based sequencing.Virology journal · 2022Article
- Membrane receptor activation mechanisms and transmembrane peptide tools to elucidate them.The Journal of biological chemistry · 2020Review
- Comparing side chain packing in soluble proteins, protein-protein interfaces, and transmembrane proteins.Proteins · 2018Article
- Two transmembrane dimers of the bovine papillomavirus E5 oncoprotein clamp the PDGF β receptor in an active dimeric conformation.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Compensatory mutants of the bovine papillomavirus E5 protein and the platelet-derived growth factor β receptor reveal a complex direct transmembrane interaction.Journal of virology · 2013Article
- The E5 proteins.Virology · 2013Review
- A single amino acid substitution converts a transmembrane protein activator of the platelet-derived growth factor β receptor into an inhibitor.The Journal of biological chemistry · 2013Article
- Construction and maintenance of randomized retroviral expression libraries for transmembrane protein engineering.Protein engineering, design & selection : PEDS · 2011Article
- Structural role of the conserved cysteines in the dimerization of the viral transmembrane oncoprotein E5.Biophysical journal · 2010Article
- Construction and genetic selection of small transmembrane proteins that activate the human erythropoietin receptor.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- Artificial transmembrane oncoproteins smaller than the bovine papillomavirus E5 protein redefine sequence requirements for activation of the platelet-derived growth factor beta receptor.Journal of virology · 2009Article
- The bovine papillomavirus E5 protein and the PDGF beta receptor: it takes two to tango.Virology · 2009Review
- In vitro dimerization of the bovine papillomavirus E5 protein transmembrane domain.Biochemistry · 2008Article
- Modulation of cell function by small transmembrane proteins modeled on the bovine papillomavirus E5 protein.Oncogene · 2005Review
- Productive interaction between transmembrane mutants of the bovine papillomavirus E5 protein and the platelet-derived growth factor beta receptor.Journal of virology · 2005Article
- Article
- Multiple transmembrane amino acid requirements suggest a highly specific interaction between the bovine papillomavirus E5 oncoprotein and the platelet-derived growth factor beta receptor.Journal of virology · 2002Article
- Review
- Identification of the transmembrane dimer interface of the bovine papillomavirus E5 protein.Oncogene · 2001Article
- The bovine papillomavirus E5 protein requires a juxtamembrane negative charge for activation of the platelet-derived growth factor beta receptor and transformation of C127 cells.Journal of virology · 1999Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
The bovine papillomavirus E5 protein is a 44-amino-acid membrane-associated protein that forms a stable complex with the endogenous platelet-derived growth factor (PDGF) beta receptor in rodent and bovine fibroblasts, resulting in sustained receptor activation and cell transformation. We report here that high-level expression of the E5 protein caused a reduction in the level of the mature form of the PDGF beta receptor in acutely and stably transformed mouse C127 cells. To explore in more detail the interaction of the E5 protein and the PDGF beta receptor, we tested the abilities of various E5 point mutants to bind the PDGF receptor, to induce PDGF receptor down-regulation and tyrosine phosphorylation, and to transform cells. A transformation-competent mutant, like the wild-type E5 protein, bound the receptor and induced receptor tyrosine phosphorylation and down-regulation. Transformation-defective E5 proteins either failed to interact with the endogenous PDGF beta receptor in mouse fibroblasts or underwent an aberrant interaction with the receptor. Mutation of glutamine at position 17, aspartic acid at position 33, or both carboxyl-terminal cysteine residues required for E5 homodimerization interfered with stable complex formation with the PDGF receptor, tyrosine phosphorylation and down-regulation of the receptor, and cell transformation. Point mutations at several other carboxyl-terminal positions generated transformation-defective E5 proteins that formed a complex with the PDGF receptor and induced receptor tyrosine phosphorylation but did not induce PDGF receptor down-regulation. Either PDGF receptor activation is not sufficient for transformation of C127 cells or the receptors that are tyrosine phosphorylated in response to these mutant E5 proteins are not fully activated and therefore are not able to deliver a mitogenic signal.
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