2020
TBC1D5-Catalyzed Cycling of Rab7 Is Required for Retromer-Mediated Human Papillomavirus Trafficking during Virus Entry
Xie J, Heim EN, Crite M, DiMaio D. TBC1D5-Catalyzed Cycling of Rab7 Is Required for Retromer-Mediated Human Papillomavirus Trafficking during Virus Entry. Cell Reports 2020, 31: 107750. PMID: 32521275, PMCID: PMC7339955, DOI: 10.1016/j.celrep.2020.107750.Peer-Reviewed Original ResearchConceptsGTPase-activating proteinsRetrograde transport pathwayVirus entryRetromer activityHPV traffickingTrafficking complexMembrane recruitmentRetromer complexRab7-GTPCellular proteinsCellular compartmentsEndosome membraneRetromerRetrograde pathwayArtificial proteinsL2 capsid proteinsCapsid proteinRab7HPV entryTraffickingTBC1D5ProteinGTPTransport pathwaysPathway
2017
Single methyl groups can act as toggle switches to specify transmembrane Protein-protein interactions
He L, Steinocher H, Shelar A, Cohen EB, Heim EN, Kragelund BB, Grigoryan G, DiMaio D. Single methyl groups can act as toggle switches to specify transmembrane Protein-protein interactions. ELife 2017, 6: e27701. PMID: 28869036, PMCID: PMC5597333, DOI: 10.7554/elife.27701.Peer-Reviewed Original ResearchConceptsProtein-protein interactionsErythropoietin receptorTransmembrane proteinTransmembrane protein-protein interactionsTMD interactionsModel transmembrane proteinMouse erythropoietin receptorHuman erythropoietin receptorSingle methyl groupGrowth factor independenceSide chain methyl groupsCellular processesMouse cellsFactor independenceChain methyl groupsIntrinsic specificityToggle switchTraptamersMethyl groupProteinReceptor activitySpecific positionsReceptorsSpecificityOligomerizationTwo 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
2015
Direct Binding of Retromer to Human Papillomavirus Type 16 Minor Capsid Protein L2 Mediates Endosome Exit during Viral Infection
Popa A, Zhang W, Harrison MS, Goodner K, Kazakov T, Goodwin EC, Lipovsky A, Burd CG, DiMaio D. Direct Binding of Retromer to Human Papillomavirus Type 16 Minor Capsid Protein L2 Mediates Endosome Exit during Viral Infection. PLOS Pathogens 2015, 11: e1004699. PMID: 25693203, PMCID: PMC4334968, DOI: 10.1371/journal.ppat.1004699.Peer-Reviewed Original ResearchConceptsTrans-Golgi networkRetromer cargoTransmembrane proteinGolgi apparatusDirect bindingCoat protein complexCellular transmembrane proteinsVirus entryMinor capsid proteinCarboxy-terminal segmentProtein complexesL2 minor capsid proteinMinor capsid protein L2Early endosomesVesicular transportRetromerPlasma membraneEndosomal membranesBinding motifProtein L2Capsid proteinEndosomesL2 proteinViral componentsProtein
2001
Identification 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
Bovine 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
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 activationThe HPV16 E5 Protein: Expression, Detection, and Stable Complex Formation with Transmembrane Proteins in COS Cells
Hwang E, Nottoli T, Dimaio D. The HPV16 E5 Protein: Expression, Detection, and Stable Complex Formation with Transmembrane Proteins in COS Cells. Virology 1995, 211: 227-233. PMID: 7645215, DOI: 10.1006/viro.1995.1395.Peer-Reviewed Original ResearchConceptsE5 proteinHPV16 E5 proteinStable complex formationTransmembrane proteinGrowth factor receptorE5 genePlatelet-derived growth factor beta receptorViral proteinsVesicular stomatitis virus glycoproteinComplex formationFactor receptorCOS monkey cellsGrowth factor beta receptorStable growth transformationCultured cell systemsEpidermal growth factor receptorFactor 1 receptorTransforming proteinCoimmunoprecipitation analysisCOS cellsExpression vectorMonkey cellsBiochemical propertiesProteinE5 expressionLigand-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 autophosphorylation
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 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 transformation
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 ResearchThe central hydrophobic domain of the bovine papillomavirus E5 transforming protein can be functionally replaced by many hydrophobic amino acid sequences containing a glutamine
Kulke R, Horwitz B, Zibello T, DiMaio D. The central hydrophobic domain of the bovine papillomavirus E5 transforming protein can be functionally replaced by many hydrophobic amino acid sequences containing a glutamine. Journal Of Virology 1992, 66: 505-511. PMID: 1727496, PMCID: PMC238311, DOI: 10.1128/jvi.66.1.505-511.1992.Peer-Reviewed Original ResearchConceptsHydrophobic amino acidsAmino acidsE5 proteinRandom hydrophobic sequencesHydrophobic domainRodent fibroblast cell linesCentral hydrophobic domainHydrophobic amino acid sequenceCarboxyl-terminal amino acidsMouse C127 cellsAmino acid sequenceClasses of mutantsAbsence of glutamineBovine papillomavirus E5Mutant proteinsTransforming proteinDefective mutantsHydrophobic sequenceFibroblast cell lineProtein stabilityAcid sequenceC127 cellsHomodimer formationEfficient transformationProteinA glutamine residue in the membrane-associating domain of the bovine papillomavirus type 1 E5 oncoprotein mediates its binding to a transmembrane component of the vacuolar H(+)-ATPase
Goldstein D, Kulke R, Dimaio D, Schlegel R. A glutamine residue in the membrane-associating domain of the bovine papillomavirus type 1 E5 oncoprotein mediates its binding to a transmembrane component of the vacuolar H(+)-ATPase. Journal Of Virology 1992, 66: 405-413. PMID: 1370089, PMCID: PMC238300, DOI: 10.1128/jvi.66.1.405-413.1992.Peer-Reviewed Original ResearchConceptsK proteinGrowth factor receptorE5 oncoproteinGlutamine residuesRandom hydrophobic sequencesSpecific amino acid residuesMembrane-associated domainMajor transforming proteinK protein componentCarboxyl-terminal domainEndoplasmic reticulum membraneFactor receptorBovine papillomavirus type 1Colony-stimulating factor 1 receptorTransformation-defective mutantsAmino acid residuesPotential binding sitesPlatelet-derived growth factor receptorAmino acid substitutionsPapillomavirus type 1Hydrophilic amino acidsE5 dimerE5 mutantsFactor 1 receptorProtein complexes
1991
Tumorigenic transformation of murine keratinocytes by the E5 genes of bovine papillomavirus type 1 and human papillomavirus type 16
Leptak C, Cajal S, Kulke R, Horwitz B, Riese D, Dotto G, DiMaio D. Tumorigenic transformation of murine keratinocytes by the E5 genes of bovine papillomavirus type 1 and human papillomavirus type 16. Journal Of Virology 1991, 65: 7078-7083. PMID: 1658398, PMCID: PMC250837, DOI: 10.1128/jvi.65.12.7078-7083.1991.Peer-Reviewed Original ResearchConceptsBovine papillomavirus type 1E5 genePapillomavirus type 1Human Papillomavirus Type 16 E5 GeneTumorigenic transformationHost epithelial cellsExpression vectorRecombinant virusesRetroviral expression vectorMurine keratinocytesBiological propertiesTumorigenic cellsMurine epidermal keratinocytesGenesMurine fibroblastsFrameshift mutationCultured linesHuman papillomavirus type 16Cell linesEpithelial cellsPapillomavirus type 16Epidermal keratinocytesRetrovirusesCellsKeratinocytesActivation 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
1990
Bovine papillomavirus E2 repressor mutant displays a high-copy-number phenotype and enhanced transforming activity
Riese D, Settleman J, Neary K, DiMaio D. Bovine papillomavirus E2 repressor mutant displays a high-copy-number phenotype and enhanced transforming activity. Journal Of Virology 1990, 64: 944-949. PMID: 2153255, PMCID: PMC249196, DOI: 10.1128/jvi.64.2.944-949.1990.Peer-Reviewed Original ResearchConceptsRepressor proteinWild-type copy numberBovine papillomavirus type 1 genomeCopy numberViral genomeTranscriptional repressor proteinTransient expression experimentsMouse C127 cellsMutant viral DNAViral DNAType 1 genomeNumber phenotypeRepressor activityLow copy numberMethionine codonInitiation codonExpression experimentsC127 cellsGenomeCV1 cellsRepressor mutantsFoci formationColony formationCodonProtein
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