ArticleProceedings of the National Academy of Sciences of the United States of America1998
Bovine papillomavirus E5 protein induces oligomerization and trans-phosphorylation of the platelet-derived growth factor beta receptor.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
What it found
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Who cites it
35 citing papers in PubMed, 63 citations in OpenAlex.
- Equine Sarcoid: From BPV-Driven Oncogenesis to Host-Sustained Tumor Persistence.Pathogens (Basel, Switzerland) · 2026Review
- Activation of the PDGF β Receptor by a Persistent Artificial Signal Peptide.Journal of molecular biology · 2021Article
- Biologically Active Ultra-Simple Proteins Reveal Principles of Transmembrane Domain Interactions.Journal of molecular biology · 2019Article
- Synthetic cytokine receptors transmit biological signals using artificial ligands.Nature communications · 2018Article
- Single methyl groups can act as toggle switches to specify transmembrane Protein-protein interactions.eLife · 2017Article
- 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
- PDGFs and their receptors.Gene · 2017Review
- Pericyte-fibroblast transition promotes tumor growth and metastasis.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Hepatic sinusoids in liver injury, inflammation, and fibrosis: new pathophysiological insights.Journal of gastroenterology · 2016Review
- Biologically active LIL proteins built with minimal chemical diversity.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Hydrophobic Mismatch Drives the Interaction of E5 with the Transmembrane Segment of PDGF Receptor.Biophysical journal · 2015Article
- YIP1 family member 4 (YIPF4) is a novel cellular binding partner of the papillomavirus E5 proteins.Scientific reports · 2015Article
- Viral miniproteins.Annual review of microbiology · 2014Review
- 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
- Analysis of activated platelet-derived growth factor β receptor and Ras-MAP kinase pathway in equine sarcoid fibroblasts.BioMed research international · 2013Article
- Construction and maintenance of randomized retroviral expression libraries for transmembrane protein engineering.Protein engineering, design & selection : PEDS · 2011Article
- Neuropilin-1 promotes cirrhosis of the rodent and human liver by enhancing PDGF/TGF-beta signaling in hepatic stellate cells.The Journal of clinical investigation · 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
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
The bovine papillomavirus E5 protein is a 44-aa transmembrane protein that forms a stable complex with the cellular platelet-derived growth factor (PDGF) beta receptor and induces constitutive tyrosine phosphorylation and activation of the receptor, resulting in cell transformation. The E5 protein does not resemble PDGF, but rather activates the receptor in a ligand-independent fashion, thus providing a unique system to examine activation of receptor tyrosine kinases. Here, we used a variety of approaches to explore the mechanism of receptor activation by the E5 protein. Chemical cross-linking experiments revealed that the E5 protein activated only a small fraction of the endogenous PDGF beta receptor in transformed fibroblasts and suggested that this fraction was constitutively dimerized. Coimmunoprecipitation experiments using extracts of cells engineered to coexpress full-length and truncated PDGF beta receptors confirmed that the E5 protein induced oligomerization of the receptor. Furthermore, in cells expressing the E5 protein, a kinase-active receptor was able to trans-phosphorylate a kinase-negative mutant receptor but was unable to catalyze intramolecular autophosphorylation. These results indicated that the E5 protein induced PDGF beta receptor activation by forming a stable complex with the receptor, resulting in receptor dimerization and trans-phosphorylation.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.