1999
The Bovine Papillomavirus E5 Protein Requires a Juxtamembrane Negative Charge for Activation of the Platelet-Derived Growth Factor β Receptor and Transformation of C127 Cells
Klein O, Kegler-Ebo D, Su J, Smith S, DiMaio D. The Bovine Papillomavirus E5 Protein Requires a Juxtamembrane Negative Charge for Activation of the Platelet-Derived Growth Factor β Receptor and Transformation of C127 Cells. Journal Of Virology 1999, 73: 3264-3272. PMID: 10074180, PMCID: PMC104090, DOI: 10.1128/jvi.73.4.3264-3272.1999.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBinding SitesCattleCell Transformation, ViralCOS CellsMiceMolecular Sequence DataMutationOncogene Proteins, ViralReceptor, Platelet-Derived Growth Factor betaReceptors, Platelet-Derived Growth FactorStatic ElectricityConceptsPlatelet-derived growth factor beta receptorPDGF beta receptorGrowth factor beta receptorE5 proteinBovine papillomavirus E5 proteinCell transformationHomodimeric transmembrane proteinSustained receptor activationC127 mouse fibroblastsExtracellular juxtamembrane regionBeta receptorsE5 dimerE5 mutantsDouble mutantJuxtamembrane regionTransmembrane proteinC-terminusC127 cellsAcidic residuesE5 geneMutantsPosition 33Mouse fibroblastsProteinSalt bridge
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 receptorsA single amino acid substitution in a WW‐like domain of diverse members of the PDGF receptor subfamily of tyrosine kinases causes constitutive receptor activation
Irusta P, DiMaio D. A single amino acid substitution in a WW‐like domain of diverse members of the PDGF receptor subfamily of tyrosine kinases causes constitutive receptor activation. The EMBO Journal 1998, 17: 6912-6923. PMID: 9843497, PMCID: PMC1171039, DOI: 10.1093/emboj/17.23.6912.Peer-Reviewed Original ResearchMeSH KeywordsAlanineAmino Acid SequenceAmino Acid SubstitutionAnimalsBinding SitesCell Line, TransformedCloning, MolecularDimerizationEnzyme ActivationHumansInterleukin-3LigandsMiceMolecular Sequence DataMutagenesis, Site-DirectedPeptidesPhosphorylationPolymerase Chain ReactionReceptor Protein-Tyrosine KinasesReceptor, Platelet-Derived Growth Factor betaReceptors, Platelet-Derived Growth FactorSequence Homology, Amino AcidStructure-Activity RelationshipTyrosineValineConceptsTyrosine kinase activityKinase activityTyrosine kinasePlatelet-derived growth factor beta receptorCytoplasmic juxtamembrane domainPDGF receptorSignal transduction proteinsWW-like domainTransmembrane receptor tyrosine kinaseProtein-protein interactionsBa/F3 cellsGST fusion proteinSingle amino acid substitutionConstitutive receptor activationGrowth factor beta receptorAbsence of ligandReceptor tyrosine kinasesAmino acid substitutionsSequence PPXYTransduction proteinsWW domainsCellular functionsJuxtamembrane regionTyrosine phosphorylationAlanine substitutionsStructural models of the bovine papillomavirus E5 protein
Surti T, Klein O, Aschheim K, DiMaio D, Smith S. Structural models of the bovine papillomavirus E5 protein. Proteins Structure Function And Bioinformatics 1998, 33: 601-612. PMID: 9849943, DOI: 10.1002/(sici)1097-0134(19981201)33:4<601::aid-prot12>3.0.co;2-i.Peer-Reviewed Original ResearchConceptsBovine papillomavirus E5 proteinE5 dimerE5 proteinType II integral membrane proteinIntegral membrane proteinsPrevious mutagenesis studiesLigand-independent activationDisulfide-linked homodimerPDGF beta receptorMembrane proteinsTransmembrane orientationMutagenesis studiesMembrane bilayerCell transformationGenetic resultsProteinGln17Receptor moleculesMolecular scaffoldsComplex formationAsp33Computational searchDimerizationDimer structureDimersRole of Glutamine 17 of the Bovine Papillomavirus E5 Protein in Platelet-Derived Growth Factor β Receptor Activation and Cell Transformation
Klein O, Polack G, Surti T, Kegler-Ebo D, Smith S, DiMaio D. Role of Glutamine 17 of the Bovine Papillomavirus E5 Protein in Platelet-Derived Growth Factor β Receptor Activation and Cell Transformation. Journal Of Virology 1998, 72: 8921-8932. PMID: 9765437, PMCID: PMC110309, DOI: 10.1128/jvi.72.11.8921-8932.1998.Peer-Reviewed Original ResearchConceptsBovine papillomavirus E5 proteinPDGF beta receptorE5 proteinTransform cellsCellular platelet-derived growth factor (PDGF) beta receptorAmino acidsBa/F3 hematopoietic cellsPosition 17Cell transformationPlatelet-derived growth factor beta receptorHomodimeric transmembrane proteinReceptor tyrosine phosphorylationGrowth factor beta receptorReceptor tyrosine kinasesPDGF receptor tyrosine kinaseReceptor activationPossible amino acidsBeta receptorsStable complexesComplex formationMutant proteinsTransmembrane domainTransmembrane proteinGrowth factor-beta (TGF-beta) receptor activationTyrosine phosphorylationVIROCRINE TRANSFORMATION: The Intersection Between Viral Transforming Proteins and Cellular Signal Transduction Pathways
DiMaio D, Lai C, Klein O. VIROCRINE TRANSFORMATION: The Intersection Between Viral Transforming Proteins and Cellular Signal Transduction Pathways. Annual Review Of Microbiology 1998, 52: 397-421. PMID: 9891803, DOI: 10.1146/annurev.micro.52.1.397.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAntigens, Polyomavirus TransformingBovine papillomavirus 1CattleCell Transformation, ViralHerpesvirus 4, HumanMiceOncogene ProteinsReceptor Protein-Tyrosine KinasesReceptor, Platelet-Derived Growth Factor betaReceptors, ErythropoietinReceptors, Platelet-Derived Growth FactorReceptors, Tumor Necrosis FactorSignal TransductionViral Envelope ProteinsViral Matrix ProteinsViral ProteinsConceptsCellular signal transduction pathwaysSignal transduction pathwaysTransduction pathwaysPlatelet-derived growth factor beta receptorPolyoma virus middle T antigenCellular signal transductionViral transforming proteinsCellular signaling pathwaysViral transformationMiddle T antigenGrowth factor beta receptorReceptor tyrosine kinasesTransforming proteinSignal transductionE5 proteinTumor necrosis factor receptorErythropoietin receptorTyrosine kinaseSignaling pathwaysCell transformationDiverse virusesNecrosis factor receptorViral oncoproteinsSpleen focusT antigenOncogenic activation of the PDGF β receptor by the transmembrane domain of p185neu*
Petti L, Irusta P, DiMaio D. Oncogenic activation of the PDGF β receptor by the transmembrane domain of p185neu*. Oncogene 1998, 16: 843-851. PMID: 9484775, DOI: 10.1038/sj.onc.1201590.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsCell Transformation, NeoplasticCells, CulturedMiceMolecular Sequence DataOncogenesPhosphorylationPhosphotyrosineReceptor, ErbB-2Receptors, Platelet-Derived Growth FactorRecombinant Fusion ProteinsStructure-Activity RelationshipConceptsBa/F3 cellsTransmembrane domainBa/F3 hematopoietic cellsF3 cellsWild-type PDGF receptorNovel tyrosine phosphorylated proteinsIL-3-independent growthTyrosine phosphorylated proteinsDistinct signaling pathwaysWild-type PDGFLevels of phosphotyrosineWild-type receptorIL-3Β receptorPDGF β-receptorPhosphorylated proteinsTyrosine autophosphorylationOncogenic formsKinase activityMouse C127Receptor homodimerizationOncogenic activationSignaling pathwaysChimeric receptorsFoci formation
1997
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
Petti L, Reddy V, Smith S, DiMaio D. 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 1997, 71: 7318-7327. PMID: 9311809, PMCID: PMC192076, DOI: 10.1128/jvi.71.10.7318-7327.1997.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBovine papillomavirus 1CattleCell LineCell MembraneErbB ReceptorsHumansInterleukin-3KineticsLeucineLysineMiceMolecular Sequence DataMutagenesis, Site-DirectedOncogene Proteins v-sisOncogene Proteins, ViralPoint MutationPolymerase Chain ReactionProtein Structure, SecondaryRatsReceptor, ErbB-2Receptor, Platelet-Derived Growth Factor betaReceptors, Platelet-Derived Growth FactorReceptors, VirusRecombinant Fusion ProteinsRetroviridae Proteins, OncogenicSequence AlignmentThreonineTransfectionConceptsBovine papillomavirus E5 proteinE5 proteinTransmembrane domainPDGF beta receptorAmino acidsCellular platelet-derived growth factor (PDGF) beta receptorReceptor mutantsJuxtamembrane domainPlatelet-derived growth factor beta receptorPutative transmembrane domainsMurine Ba/F3 cellsCarboxyl-terminal domainBa/F3 cellsV-sisReceptor tyrosine phosphorylationExtracellular juxtamembrane domainGrowth factor beta receptorSpecific amino acidsProductive interactionReceptor activationPlatelet-derived growth factor receptorAcidic amino acidsComplex formationThreonine residuesBeta receptorsVirocrine transformation
Drummond-Barbosa D, DiMaio D. Virocrine transformation. Biochimica Et Biophysica Acta 1997, 1332: m1-m17. PMID: 9061007, DOI: 10.1016/s0304-419x(96)00034-0.Peer-Reviewed Original ResearchAntigens, Viral, TumorCell Transformation, ViralGrowth SubstancesOncogene Proteins, ViralPhosphorylationReceptor Protein-Tyrosine KinasesReceptor, IGF Type 1Receptor, Platelet-Derived Growth Factor betaReceptors, ErythropoietinReceptors, Growth FactorReceptors, Platelet-Derived Growth FactorReceptors, Tumor Necrosis FactorSignal TransductionTerminology as TopicViral Envelope ProteinsViral Matrix ProteinsViral ProteinsVirus Replication
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 ResearchMeSH KeywordsAnimalsBinding SitesBovine papillomavirus 1Cell DivisionCell LineHumansLigandsMiceMitogensMutationOncogene Proteins, ViralPhosphorylationProtein-Tyrosine KinasesReceptors, Platelet-Derived Growth FactorSignal TransductionConceptsE5 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 ResearchMeSH KeywordsAnimalsBovine papillomavirus 1Cell Transformation, ViralCells, CulturedIn Vitro TechniquesMiceOncogene Proteins, ViralPlatelet-Derived Growth FactorProtein-Tyrosine KinasesReceptors, Platelet-Derived Growth FactorSignal TransductionTransfectionConceptsBPV 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
1994
Specific interaction between the bovine papillomavirus E5 transforming protein and the beta receptor for platelet-derived growth factor in stably transformed and acutely transfected cells
Petti L, DiMaio D. Specific interaction between the bovine papillomavirus E5 transforming protein and the beta receptor for platelet-derived growth factor in stably transformed and acutely transfected cells. Journal Of Virology 1994, 68: 3582-3592. PMID: 8189497, PMCID: PMC236862, DOI: 10.1128/jvi.68.6.3582-3592.1994.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBinding SitesBovine papillomavirus 1CattleCell Line, TransformedErbB ReceptorsHumansMiceOncogene Proteins, ViralReceptors, Platelet-Derived Growth FactorTransfectionConceptsPDGF beta receptorE5 proteinPlatelet-derived growth factorEGF receptorEpidermal growth factorGrowth factor receptorCOS cellsTumorigenic transformationBovine fibroblastsPDGF receptorHeterologous cell systemFactor receptorNIH 3T3 cellsGrowth factorBovine papillomavirus E5Beta receptorsMembrane proteinsTransient overexpressionRodent fibroblastsCell typesProteinBovine papillomavirusPotential targetSpecific interactionsEpithelial cells
1993
Platelet-derived growth factor receptor can mediate tumorigenic transformation by the bovine papillomavirus E5 protein.
Nilson L, DiMaio D. Platelet-derived growth factor receptor can mediate tumorigenic transformation by the bovine papillomavirus E5 protein. Molecular And Cellular Biology 1993, 13: 4137-4145. PMID: 8321218, PMCID: PMC359963, DOI: 10.1128/mcb.13.7.4137.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCell LineCell Transformation, NeoplasticCell Transformation, ViralFemaleMiceMice, Inbred BALB CMice, NudeOncogene Proteins, ViralPrecipitin TestsReceptors, Platelet-Derived Growth FactorConceptsE5 proteinPDGF receptorPlatelet-derived growth factorBovine papillomavirus E5 proteinTumorigenic transformationMouse mammary gland cellsMurine mammary epithelial cell lineBovine papillomavirus type 1 E5 proteinPDGF receptor genesBPV E5 proteinMammary epithelial cell lineSustained proliferative signalEpidermal growth factor receptor (EGFR) pathwayPlatelet-derived growth factor receptorMammary gland cellsStable complexesGrowth factor receptor pathwayPDGF beta receptorTransforming proteinNMuMG cellsCellular proteinsGrowth factor receptorTyrosine phosphorylationEpithelial cell lineFibroblast transformation
1992
Stable association between the bovine papillomavirus E5 transforming protein and activated platelet-derived growth factor receptor in transformed mouse cells.
Petti L, DiMaio D. Stable association between the bovine papillomavirus E5 transforming protein and activated platelet-derived growth factor receptor in transformed mouse cells. Proceedings Of The National Academy Of Sciences Of The United States Of America 1992, 89: 6736-6740. PMID: 1323117, PMCID: PMC49578, DOI: 10.1073/pnas.89.15.6736.Peer-Reviewed Original ResearchConceptsE5 proteinPlatelet-derived growth factorGrowth factor receptor activationPDGF receptorMouse C127 cellsBovine papillomavirus E5Platelet-derived growth factor receptorShorter proteinTransforming proteinCoimmunoprecipitation analysisGrowth factor receptorReceptor transmitsStable associationC127 cellsTumorigenic transformationMouse cellsProteinBovine papillomavirusFactor receptorDistinct mechanismsStable complexesGrowth factorReceptor activationImportant targetBeta receptors
1991
Biological properties of the deer papillomavirus E5 gene in mouse C127 cells: growth transformation, induction of DNA synthesis, and activation of the platelet-derived growth factor receptor
Kulke R, DiMaio D. Biological properties of the deer papillomavirus E5 gene in mouse C127 cells: growth transformation, induction of DNA synthesis, and activation of the platelet-derived growth factor receptor. Journal Of Virology 1991, 65: 4943-4949. PMID: 1651413, PMCID: PMC248956, DOI: 10.1128/jvi.65.9.4943-4949.1991.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBlotting, NorthernCell Transformation, ViralCloning, MolecularDeerDNAGene ExpressionGenes, ViralIn Vitro TechniquesMiceMolecular Sequence DataOncogene Proteins, ViralPapillomaviridaePlatelet-Derived Growth FactorReceptors, Cell SurfaceReceptors, Platelet-Derived Growth FactorRNA, ViralViral Structural ProteinsConceptsMouse C127 cellsE5 proteinC127 cellsE5 genePlatelet-derived growth factor beta receptorPDGF receptorBovine papillomavirus type 1 E5 proteinConstitutive tyrosine phosphorylationDNA synthesisGrowth factor beta receptorBovine papillomavirus type 1Platelet-derived growth factor receptorTransformation of fibroblastsPapillomavirus type 1Sequence similarityGrowth factor receptorTyrosine phosphorylationBiological activityShort regionFoci formationProteinFactor receptorReceptor formsB chainGrowth transformationActivation of the platelet‐derived growth factor receptor by the bovine papillomavirus E5 transforming protein.
Petti L, Nilson L, DiMaio D. Activation of the platelet‐derived growth factor receptor by the bovine papillomavirus E5 transforming protein. The EMBO Journal 1991, 10: 845-855. PMID: 1849073, PMCID: PMC452725, DOI: 10.1002/j.1460-2075.1991.tb08017.x.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBovine papillomavirus 1Cell LineCell Transformation, NeoplasticDNA ReplicationKineticsOncogenesPhosphorylationPlatelet-Derived Growth FactorProtein KinasesReceptors, Cell SurfaceReceptors, Platelet-Derived Growth FactorConceptsPlatelet-derived growth factorE5 proteinBovine papillomavirus E5 proteinImportant cellular intermediatesPDGF receptorRodent fibroblast cell linesV-sis geneMembrane-associated proteinsStable growth transformationBovine papillomavirus E5Platelet-derived growth factor receptorSequence similarityCellular proteinsFibroblast cell lineGrowth factor receptorC127 cellsTumorigenic transformationE5 geneGrowth regulationCellular intermediatesFR3T3 cellsMature formShort regionGenetic studiesBeta-type receptors