2017
Two transmembrane dimers of the bovine papillomavirus E5 oncoprotein clamp the PDGF β receptor in an active dimeric conformation
Karabadzhak AG, Petti LM, Barrera FN, Edwards APB, Moya-Rodríguez A, Polikanov YS, Freites JA, Tobias DJ, Engelman DM, DiMaio D. 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 2017, 114: e7262-e7271. PMID: 28808001, PMCID: PMC5584431, DOI: 10.1073/pnas.1705622114.Peer-Reviewed Original ResearchConceptsTransmembrane domainE5 proteinE5 dimerPlatelet-derived growth factor β receptorGrowth factor β receptorActive dimeric conformationPDGF β-receptorTransmembrane dimerProtein bindsMembrane environmentReceptor dimerizationDimeric conformationAtom molecular dynamics simulationsBiochemical experimentsMouse cellsMolecular mechanismsActive dimerΒ receptorBovine papillomavirusProteinSpecific interactionsMembrane modelingReceptor activationDimerizationComplexes
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 receptorsRole 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 activation
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