1998
Bovine papillomavirus E5 protein induces oligomerization and trans-phosphorylation of the platelet-derived growth factor β receptor
Lai C, Henningson C, DiMaio D. Bovine papillomavirus E5 protein induces oligomerization and trans-phosphorylation of the platelet-derived growth factor β receptor. Proceedings Of The National Academy Of Sciences Of The United States Of America 1998, 95: 15241-15246. PMID: 9860953, PMCID: PMC28027, DOI: 10.1073/pnas.95.26.15241.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SubstitutionAnimalsBovine papillomavirus 1CattleCell LineCell Line, TransformedCross-Linking ReagentsDimerizationHumansKineticsMacromolecular SubstancesMiceOncogene Proteins, ViralPhosphorylationProtein-Tyrosine KinasesReceptor, Platelet-Derived Growth Factor betaReceptors, Platelet-Derived Growth FactorRecombinant ProteinsSequence DeletionTransfectionConceptsBovine papillomavirus E5 proteinE5 proteinPDGF beta receptorCellular platelet-derived growth factor (PDGF) beta receptorKinase-negative mutant receptorPlatelet-derived growth factor beta receptorPlatelet-derived growth factor β receptorChemical cross-linking experimentsGrowth factor β receptorConstitutive tyrosine phosphorylationGrowth factor beta receptorLigand-independent fashionCross-linking experimentsReceptor tyrosine kinasesStable complexesExtracts of cellsPDGF beta-receptor activationIntramolecular autophosphorylationBeta receptorsCoimmunoprecipitation experimentsTransmembrane proteinReceptor activationTyrosine phosphorylationReceptor dimerizationMutant receptors
1995
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
Nilson L, Gottlieb R, Polack G, DiMaio D. 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. Journal Of Virology 1995, 69: 5869-5874. PMID: 7543592, PMCID: PMC189463, DOI: 10.1128/jvi.69.9.5869-5874.1995.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBinding SitesBovine papillomavirus 1Cell LineDNA Mutational AnalysisDown-RegulationFrameshift MutationKineticsMiceMolecular Sequence DataMutagenesisMutagenesis, Site-DirectedOncogene Proteins, ViralPhosphotyrosinePoint MutationProtein-Tyrosine KinasesReceptor, Platelet-Derived Growth Factor betaReceptors, Platelet-Derived Growth FactorRecombinant ProteinsTyrosineConceptsMouse C127 cellsE5 proteinReceptor tyrosine phosphorylationTyrosine phosphorylationPDGF beta receptorC127 cellsPDGF receptorWild-type E5 proteinBovine papillomavirus E5 proteinCarboxyl-terminal cysteine residueCell transformationPlatelet-derived growth factor beta receptorMembrane-associated proteinsSustained receptor activationPDGF receptor activationMutation of glutamineTransformation-competent mutantsGrowth factor beta receptorBovine papillomavirus E5Carboxyl-terminal positionBeta receptorsHigh-level expressionPlatelet-derived growth factorStable complex formationReceptor activationLigand-Independent Activation of the Platelet-Derived Growth Factor β Receptor: Requirements for Bovine Papillomavirus E5-Induced Mitogenic Signaling
Drummond-Barbosa D, Vaillancourt R, Kazlauskas A, DiMaio D. Ligand-Independent Activation of the Platelet-Derived Growth Factor β Receptor: Requirements for Bovine Papillomavirus E5-Induced Mitogenic Signaling. Molecular And Cellular Biology 1995, 15: 2570-2581. PMID: 7739538, PMCID: PMC230487, DOI: 10.1128/mcb.15.5.2570.Peer-Reviewed Original ResearchConceptsE5 proteinPDGF beta receptorTyrosine phosphorylationMitogenic signalsMitogenic signalingReceptor mutantsSH2 domain-containing proteinsPlatelet-derived growth factor beta receptorPDGF beta receptor tyrosine kinaseDomain-containing proteinsPhosphorylation of substratesInterleukin-3Tyrosine phosphorylation sitesGrowth factor β receptorBa/F3 cellsReceptor tyrosine phosphorylationGrowth factor beta receptorLigand-independent activationReceptor tyrosine kinasesTyrosine kinase activityBovine papillomavirus E5Beta receptorsComplex formationPhosphorylation sitesReceptor autophosphorylationAn intact PDGF signaling pathway is required for efficient growth transformation of mouse C127 cells by the bovine papillomavirus E5 protein.
Riese D, DiMaio D. An intact PDGF signaling pathway is required for efficient growth transformation of mouse C127 cells by the bovine papillomavirus E5 protein. Oncogene 1995, 10: 1431-9. PMID: 7731695.Peer-Reviewed Original ResearchConceptsBPV E5 proteinPDGF beta receptorE5 proteinE5 geneC127 cellsBovine papillomavirus E5 proteinPDGF beta-receptor genePlatelet-derived growth factor beta receptorGrowth transformationBovine papillomavirus type 1 E5 proteinC127 cell linesMembrane-associated proteinsMouse C127 cellsHeterologous cell typesV-sis oncogeneDNA synthesisGrowth factor beta receptorStable growth transformationBeta receptor geneCell linesBeta receptorsBPV E5Reduced DNA synthesisMouse C127Genetic support
1992
Localization of bovine papillomavirus type 1 E5 protein to transformed basal keratinocytes and permissive differentiated cells in fibropapilloma tissue.
Burnett S, Jareborg N, DiMaio D. Localization of bovine papillomavirus type 1 E5 protein to transformed basal keratinocytes and permissive differentiated cells in fibropapilloma tissue. Proceedings Of The National Academy Of Sciences Of The United States Of America 1992, 89: 5665-5669. PMID: 1319069, PMCID: PMC49353, DOI: 10.1073/pnas.89.12.5665.Peer-Reviewed Original Research
1989
Genetic evidence that acute morphologic transformation, induction of cellular DNA synthesis, and focus formation are mediated by a single activity of the bovine papillomavirus E5 protein.
Settleman J, Fazeli A, Malicki J, Horwitz B, DiMaio D. Genetic evidence that acute morphologic transformation, induction of cellular DNA synthesis, and focus formation are mediated by a single activity of the bovine papillomavirus E5 protein. Molecular And Cellular Biology 1989, 9: 5563-5572. PMID: 2555701, PMCID: PMC363726, DOI: 10.1128/mcb.9.12.5563.Peer-Reviewed Original ResearchConceptsE5 proteinE5 geneCellular DNA synthesisC127 cellsBovine papillomavirus E5 proteinMouse C127 cellsDNA synthesisMorphologic transformationCultured rodent cellsDefective phenotypeMissense mutantsUnstable proteinDefective mutantsGenetic evidenceMutational analysisE5 activityRodent cellsCell cycleViral genesBiochemical activitySerum starvationCell transformationGenesContact inhibitionVirus multiplicity