ArticleJournal of virology1994
The bovine papillomavirus type 1 E5 transforming protein specifically binds and activates the beta-type receptor for the platelet-derived growth factor but not other related tyrosine kinase-containing receptors to induce cellular transformation.
Article in Journal of virology, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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Who cites it
33 citing papers in PubMed, 71 citations in OpenAlex.
- 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
- Hydrophobic Mismatch Drives the Interaction of E5 with the Transmembrane Segment of PDGF Receptor.Biophysical journal · 2015Article
- Viral miniproteins.Annual review of microbiology · 2014Review
- The E5 proteins.Virology · 2013Review
- 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
- Analysis of activated platelet-derived growth factor β receptor and Ras-MAP kinase pathway in equine sarcoid fibroblasts.BioMed research international · 2013Article
- Papillomavirus E5: the smallest oncoprotein with many functions.Molecular cancer · 2011Review
- 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
- Packing contacts can mediate highly specific interactions between artificial transmembrane proteins and the PDGFbeta receptor.Proceedings of the National Academy of Sciences of the United States of America · 2007Article
- Modulation of cell function by small transmembrane proteins modeled on the bovine papillomavirus E5 protein.Oncogene · 2005Review
- Endoplasmic reticulum-localized human papillomavirus type 16 E5 protein alters endosomal pH but not trans-Golgi pH.Journal of virology · 2005Article
- Productive interaction between transmembrane mutants of the bovine papillomavirus E5 protein and the platelet-derived growth factor beta receptor.Journal of virology · 2005Article
- Upregulation of swelling-activated Cl- channel sensitivity to cell volume by activation of EGF receptors in murine mammary cells.The Journal of physiology · 2003Article
- 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
- c-Src activation by the E5 oncoprotein enables transformation independently of PDGF receptor activation.Oncogene · 2002Article
- Review
- Golgi alkalinization by the papillomavirus E5 oncoprotein.The Journal of cell biology · 2000Article
Corrections and comments
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Authors and funding
8 authors at 1 institution in 1 country.
Funding
Abstract
The 44-amino-acid E5 protein of bovine papillomavirus type 1 is a highly hydrophobic protein which appears to transform cells through the activation of growth factor receptors. To investigate the specificity of E5-growth factor receptor interactions required for mitogenic signaling, we utilized a nontumorigenic, murine myeloid cell line (32D) which is strictly dependent on interleukin-3 (IL-3) for sustained proliferation in culture. This IL-3 dependence can be functionally substituted by the expression of a variety of surrogate growth factor receptors and the addition of the corresponding ligand. Several receptor cDNAs for the alpha- and beta-type platelet-derived growth factor receptors [alpha PDGFR and beta PDGFR], the epidermal growth factor receptor, and the colony-stimulating factor 1 receptor) were transfected into 32D cells constitutively expressing the E5 protein to test for IL-3-independent growth. Only beta PDGFR was capable of abrogating the IL-3 dependence of 32D cells. The proliferative signal induced by the coexpression of beta PDGFR and E5 was accompanied by stable complex formation between these proteins, constitutive tyrosine phosphorylation of the receptor, and tumorigenicity in nude mice. The lack of cooperative interaction between E5 and the epidermal growth factor receptor, the colony-stimulating factor 1 receptor, and the highly related alpha PDGFR was paralleled by the inability of E5 to bind to these receptors and failure to increase receptor tyrosine phosphorylation. Thus, these data indicate that the ability of E5 to induce sustained proliferation and transformation of 32D cells is a direct consequence of specific interaction between the E5 protein and the beta PDGFR signaling complex and the subsequent stimulation of receptor tyrosine phosphorylation.
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