ArticleJournal of virology1996
E5 oncoprotein transmembrane mutants dissociate fibroblast transforming activity from 16-kilodalton protein binding and platelet-derived growth factor receptor binding and phosphorylation.
Article in Journal of virology, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 46 citations in OpenAlex.
- The E5 proteins.Virology · 2013Review
- 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
- ErbB4 (JM-b/CYT-1)-induced expression and phosphorylation of c-Jun is abrogated by human papillomavirus type 16 E5 protein.Oncogene · 2007Article
- Bovine papillomavirus E7 transformation function correlates with cellular p600 protein binding.Proceedings of the National Academy of Sciences of the United States of America · 2005Article
- Productive interaction between transmembrane mutants of the bovine papillomavirus E5 protein and the platelet-derived growth factor beta receptor.Journal of virology · 2005Article
- c-Src activation by the E5 oncoprotein enables transformation independently of PDGF receptor activation.Oncogene · 2002Article
- Review
- Identification of the transmembrane dimer interface of the bovine papillomavirus E5 protein.Oncogene · 2001Article
- Cooperative transformation and coexpression of bovine papillomavirus type 1 E5 and E7 proteins.Journal of virology · 2001Article
- Golgi alkalinization by the papillomavirus E5 oncoprotein.The Journal of cell biology · 2000Article
- 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
- Bovine papillomavirus E5 protein induces oligomerization and trans-phosphorylation of the platelet-derived growth factor beta receptor.Proceedings of the National Academy of Sciences of the United States of America · 1998Article
- Role of glutamine 17 of the bovine papillomavirus E5 protein in platelet-derived growth factor beta receptor activation and cell transformation.Journal of virology · 1998Article
- Identification of amino acids in the transmembrane and juxtamembrane domains of the platelet-derived growth factor receptor required for productive interaction with the bovine papillomavirus E5 protein.Journal of virology · 1997Article
- The vacuolar H+-ATPase: a universal proton pump of eukaryotes.The Biochemical journal · 1997Review
- Multiplicity of uses of monoclonal antibodies that define papillomavirus linear immunodominant epitopes.Immunologic research · 1997Review
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
The E5 oncoprotein of bovine papillomavirus type 1 is a 44-amino-acid, hydrophobic polypeptide which localizes predominantly in Golgi membranes and appears to transform cells through the activation of tyrosine kinase growth factor receptors. In fibroblasts, E5 interacts with both the 16-kilodalton vacuolar ATPase subunit and the platelet-derived growth factor receptor (PDGF-R) via its hydrophobic transmembrane domain and induces autophosphorylation of the receptor. To further analyze the correlation between E5 biological activity and its ability to bind these cellular proteins, a series of nine E5 transmembrane mutants was evaluated. In 32D mouse hematopoietic cells, there was an incomplete correlation between the abilities of the E5 mutant proteins to associate the PDGF-R and to transform cells. However, all transforming E5 mutant proteins induced PDGF-R tyrosine phosphorylation. In NIH 3T3 and C127 mouse fibroblasts, both transforming and nontransforming E5 mutant proteins were defective for PDGF-R binding. In addition, while most of the transforming E5 proteins induced PDGF-R phosphorylation, one hypertransforming mutant (serine 17) neither bound nor induced receptor autophosphorylation. These findings support the hypothesis that the transformation of fibroblasts by E5 transmembrane mutants can involve alternative cellular targets or potentially independent activities of the E5 protein. In addition, these results underscore the critical role of the transmembrane domain in mediating E5 biological activities.
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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.