ArticleMolecular and cellular biology1995
Ligand-independent activation of the platelet-derived growth factor beta receptor: requirements for bovine papillomavirus E5-induced mitogenic signaling.
Article in Molecular and cellular biology, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
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Who cites it
38 citing papers in PubMed, 84 citations in OpenAlex.
- Ligand-independent activation of platelet-derived growth factor receptor β promotes vitreous-induced contraction of retinal pigment epithelial cells.BMC ophthalmology · 2023Article
- 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
- 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
- Pericyte-fibroblast transition promotes tumor growth and metastasis.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- The PDGF-BB-SOX7 axis-modulated IL-33 in pericytes and stromal cells promotes metastasis through tumour-associated macrophages.Nature communications · 2016Article
- Biologically active LIL proteins built with minimal chemical diversity.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- De novo selection of oncogenes.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- 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
- 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
- Papillomavirus E5: the smallest oncoprotein with many functions.Molecular cancer · 2011Review
- The canine papillomavirus e5 protein signals from the endoplasmic reticulum.Journal of virology · 2009Article
- 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
- Expression of platelet derived growth factor family members and the potential role of imatinib mesylate for cervical cancer.Cancer cell international · 2006Article
- Roles of tyrosine 589 and 591 in STAT5 activation and transformation mediated by FLT3-ITD.Blood · 2006Article
- Article
- Modulation of cell function by small transmembrane proteins modeled on the bovine papillomavirus E5 protein.Oncogene · 2005Review
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
The E5 protein of bovine papillomavirus type 1 binds to and activates the endogenous platelet-derived growth factor (PDGF) beta receptor in fibroblasts, resulting in cell transformation. We have developed a functional assay to test the ability of PDGF beta receptor mutants to mediate a mitogenic signal initiated by the E5 protein. Lymphoid Ba/F3 cells are strictly dependent on interleukin-3 for growth, but coexpression of the wild-type PDGF beta receptor and the E5 or v-sis-encoded protein generated a mitogenic signal which allowed Ba/F3-derived cells to proliferate in the absence of interleukin-3. In these cells, the E5 protein bound to and caused increased tyrosine phosphorylation of both the mature and the precursor forms of the wild-type PDGF beta receptor. The tyrosine kinase activity of the receptor was necessary for E5-induced receptor tyrosine phosphorylation and mitogenic activity but not for complex formation with the E5 protein. In contrast, the PDGF-binding domain of the receptor was not required for complex formation with the E5 protein, E5-induced tyrosine phosphorylation or mitogenic activity, demonstrating that E5-mediated receptor activation is ligand independent. Analysis of receptor mutants lacking various combinations of tyrosine phosphorylation sites revealed that the E5 and v-sis-encoded proteins display similar requirements for signaling and suggested that the wild-type PDGF beta receptor can generate multiple independent mitogenic signals. Importantly, these mutants dissociated two activities of the PDGF beta receptor tyrosine kinase, both of which are required for sustained mitogenic signaling: (i) receptor autophosphorylation and creation of binding sites for SH2 domain-containing proteins and (ii) phosphorylation of substrates other than the receptor itself.
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