2001
Mechanisms of cell transformation by papillomavirus E5 proteins
DiMaio D, Mattoon D. Mechanisms of cell transformation by papillomavirus E5 proteins. Oncogene 2001, 20: 7866-7873. PMID: 11753669, DOI: 10.1038/sj.onc.1204915.Peer-Reviewed Original ResearchConceptsE5 proteinBovine papillomavirus E5 proteinCellular signal transduction pathwaysSignal transduction pathwaysLigand-independent fashionGrowth factor receptor activityReceptor tyrosine kinasesTransforming proteinTransduction pathwaysGrowth factor receptorVacuolar ATPaseReceptor dimerizationTyrosine kinaseCell transformationProteinViral transformationBovine papillomavirusFactor receptorUnique mechanismStable complexesNew insightsReceptor activityPathwayReceptorsKinaseIdentification of the transmembrane dimer interface of the bovine papillomavirus E5 protein
Mattoon D, Gupta K, Doyon J, Loll P, DiMaio D. Identification of the transmembrane dimer interface of the bovine papillomavirus E5 protein. Oncogene 2001, 20: 3824-3834. PMID: 11439346, DOI: 10.1038/sj.onc.1204523.Peer-Reviewed Original ResearchConceptsBovine papillomavirus E5 proteinE5 proteinDimer interfacePlatelet-derived growth factor β receptorEssential glutamine residueHeterologous dimerization domainGrowth factor β receptorNon-productive interactionsReceptor tyrosine phosphorylationFocus formation assayPDGF β-receptorDimerization domainHomodimeric proteinTyrosine phosphorylationGenetic methodsGlutamine residuesActive chimerasΒ receptorActive orientationFormation assaysProtein helicesProteinPosition 17ReceptorsPhosphorylation
2000
The platelet-derived growth factor ß receptor as a target of the bovine papillomavirus E5 protein
DiMaio D, Lai C, Mattoon D. The platelet-derived growth factor ß receptor as a target of the bovine papillomavirus E5 protein. Cytokine & Growth Factor Reviews 2000, 11: 283-293. PMID: 10959076, DOI: 10.1016/s1359-6101(00)00012-5.Peer-Reviewed Original ResearchConceptsE5 proteinBovine papillomavirus E5 proteinSH2 domain-containing proteinsCellular signal transduction pathwaysDomain-containing proteinsSignal transduction complexSignal transduction pathwaysLigand-independent fashionGrowth factor receptor activitySpecific transmembraneTransduction complexCytoplasmic domainTransmembrane proteinTransduction pathwaysReceptor dimerizationTyrosine residuesAmino acidsProteinViral transformationDirect interactionBovine papillomavirusUnique mechanismStable complexesComplex formationNew insightsBovine Papillomavirus E5 Protein Induces the Formation of Signal Transduction Complexes Containing Dimeric Activated Platelet-derived Growth Factor β Receptor and Associated Signaling Proteins*
Lai C, Henningson C, DiMaio D. Bovine Papillomavirus E5 Protein Induces the Formation of Signal Transduction Complexes Containing Dimeric Activated Platelet-derived Growth Factor β Receptor and Associated Signaling Proteins*. Journal Of Biological Chemistry 2000, 275: 9832-9840. PMID: 10734138, DOI: 10.1074/jbc.275.13.9832.Peer-Reviewed Original ResearchConceptsBovine papillomavirus E5 proteinE5 proteinPDGF beta receptorBeta receptor complexCellular platelet-derived growth factor (PDGF) beta receptorReceptor complexPlatelet-derived growth factor beta receptorPlatelet-derived growth factor β receptorRas-GTPase activating proteinAssembly of multiproteinSignal transduction complexGrowth factor β receptorGrowth factor beta receptorCell growth transformationTransduction complexBeta receptorsP85 subunitSignaling proteinsPhospholipase CgammaActivating proteinReceptor dimersConstitutive activationInactive receptorProteinReceptor molecules
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 ResearchConceptsPlatelet-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 proteinC127 cellsC-terminusAcidic 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 receptorsStructural 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 phosphorylation
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 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 activationAn 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
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. DOI: 10.1128/mcb.13.7.4137-4145.1993.Peer-Reviewed Original ResearchE5 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 β-receptorTransforming proteinNMuMG cellsCellular proteinsGrowth factor receptorTyrosine phosphorylationEpithelial cell lineFibroblast transformationPlatelet-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 ResearchConceptsE5 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 transformationPlatelet-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. DOI: 10.1128/mcb.13.7.4137-4145.1993.Peer-Reviewed Original ResearchBovine papillomavirus type 1E5 proteinPlatelet-derived growth factor receptorPlatelet-derived growth factorBovine papillomavirus E5 proteinMurine mammary epithelial cell lineTumorigenic transformationIncreased tyrosine phosphorylationMammary epithelial cell lineWell-characterized roleSustained proliferative signalingMouse mammary glandPlatelet-derived growth factor receptor genesNMuMG cellsTransforming proteinTyrosine phosphorylationCellular proteinsE5 geneGrowth factor receptor pathwayEpidermal growth factor receptor pathwayEpithelial cell lineProliferative signalsB receptorSusceptible to transformationReceptor pathway
1991
Activation 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 ResearchConceptsPlatelet-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
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. DOI: 10.1128/mcb.9.12.5563-5572.1989.Peer-Reviewed Original ResearchE5 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 starvationFoci formationCell transformationGenesContact inhibitionGenetic 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 multiplicityGenetic 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. DOI: 10.1128/mcb.9.12.5563-5572.1989.Peer-Reviewed Original ResearchInduction of cellular DNA synthesisE5 proteinCellular DNA synthesisBovine papillomavirusC127 cellsBovine papillomavirus E5 proteinDNA synthesisStable cell transformantsMouse C127 cellsMutants expressed normal levelsVirus multiplicity of infectionMissense mutantsDefective phenotypesGenetic evidenceE5 geneE5 activitySerum starvationFocus-forming assayMultiplicity of infectionCell cycleMutation analysisViral genesBiochemical activityMorphological transformationContact inhibitionTransforming activity of a 16-amino-acid segment of the bovine papillomavirus E5 protein linked to random sequences of hydrophobic amino acids
Horwitz B, Weinstat D, DiMaio D. Transforming activity of a 16-amino-acid segment of the bovine papillomavirus E5 protein linked to random sequences of hydrophobic amino acids. Journal Of Virology 1989, 63: 4515-4519. PMID: 2552136, PMCID: PMC251082, DOI: 10.1128/jvi.63.11.4515-4519.1989.Peer-Reviewed Original ResearchConceptsE5 proteinAmino acidsWild-type E5 proteinBovine papillomavirus E5 proteinAmino acid sequence requirementsHydrophobic amino acid sequenceCarboxyl-terminal amino acidsMouse C127 cellsAmino acid sequenceBovine papillomavirus type 1Carboxyl-terminal portionWild-type onesHydrophobic amino acidsPapillomavirus type 1Hydrophobic sequenceDifferent amino acidsAcid sequenceC127 cellsSequence requirementsE5 geneCell transformationFoci formationSubstitution mutationsCell membraneProtein