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
2000
E2F-Rb Complexes Assemble and Inhibit cdc25A Transcription in Cervical Carcinoma Cells following Repression of Human Papillomavirus Oncogene Expression
Wu L, Goodwin E, Naeger L, Vigo E, Galaktionov K, Helin K, DiMaio D. E2F-Rb Complexes Assemble and Inhibit cdc25A Transcription in Cervical Carcinoma Cells following Repression of Human Papillomavirus Oncogene Expression. Molecular And Cellular Biology 2000, 20: 7059-7067. PMID: 10982822, PMCID: PMC86242, DOI: 10.1128/mcb.20.19.7059-7067.2000.Peer-Reviewed Original ResearchMeSH KeywordsBinding SitesBovine papillomavirus 1Carcinoma, Squamous CellCarrier ProteinsCdc25 PhosphatasesCell CycleCell Cycle ProteinsCell Transformation, NeoplasticCell Transformation, ViralConsensus SequenceCysteine EndopeptidasesDNA, NeoplasmDNA-Binding ProteinsE2F Transcription FactorsE2F4 Transcription FactorFemaleGene Expression Regulation, NeoplasticGene Expression Regulation, ViralGenes, RetinoblastomaHumansMacromolecular SubstancesMultienzyme ComplexesNeoplasm ProteinsPapillomaviridaePapillomavirus InfectionsPhosphoproteinsPromoter Regions, GeneticProteasome Endopeptidase ComplexProtein BindingProteinsRecombinant Fusion ProteinsRetinoblastoma ProteinRetinoblastoma-Binding Protein 1Retinoblastoma-Like Protein p130Transcription Factor DP1Transcription FactorsTransfectionTumor Cells, CulturedTumor Virus InfectionsUterine Cervical NeoplasmsViral ProteinsConceptsCdc25A promoterE6/E7 repressionCervical carcinoma cellsE2F siteBovine papillomavirus E2 proteinE2 proteinE7 repressionWild-type E2 proteinE2F-responsive promotersRb tumor suppressor pathwayPapillomavirus E2 proteinCarcinoma cellsE2F-Rb complexesCell cycle genesHuman papillomavirus oncogene expressionHuman papillomavirus (HPV) E6/E7 oncogenesTumor suppressor pathwayMechanism of repressionHPV E6/E7 expressionCell cycle progressionCdc25A transcriptionDramatic growth arrestE2F complexesConsensus E2FProtein complexes
1999
The bovine papillomavirus E5 protein requires a juxtamembrane negative charge for activation of the platelet-derived growth factor beta 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 beta receptor and transformation of C127 cells. Journal Of Virology 1999, 73: 3264-72. 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
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
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 substitutionsTransactivation-competent bovine papillomavirus E2 protein is specifically required for efficient repression of human papillomavirus oncogene expression and for acute growth inhibition of cervical carcinoma cell lines.
Goodwin E, Naeger L, Breiding D, Androphy E, DiMaio D. Transactivation-competent bovine papillomavirus E2 protein is specifically required for efficient repression of human papillomavirus oncogene expression and for acute growth inhibition of cervical carcinoma cell lines. Journal Of Virology 1998, 72: 3925-34. PMID: 9557678, PMCID: PMC109618, DOI: 10.1128/jvi.72.5.3925-3934.1998.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBinding SitesBovine papillomavirus 1CattleCell DivisionCell NucleusCOS CellsDNADNA-Binding ProteinsFemaleGene Expression Regulation, ViralHeLa CellsHumansMutagenesisOncogene Proteins, ViralOncogenesPapillomaviridaeRepressor ProteinsRNA, MessengerRNA, ViralTrans-ActivatorsTranscriptional ActivationTumor Cells, CulturedUterine Cervical NeoplasmsViral ProteinsConceptsPapillomavirus E2 proteinGrowth arrestHT-3 cellsEfficient repressionTransactivation domainE2 proteinHeLa cellsG1/S-phase growth arrestE2 mutantsBovine papillomavirus type 1 E2 proteinBovine papillomavirus E2 proteinHerpes simplex virus VP16Reporter plasmidAcute growth inhibitionE2 transactivation domainGrowth inhibitionCervical carcinoma cell linesBPV1 E2 proteinCarcinoma cell linesHuman papillomavirus oncogene expressionViral DNA replicationPhase growth arrestSequence-specific transactivatorCell linesWild-type p53 gene
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: 5869-74. 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 autophosphorylation
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 ResearchConceptsPDGF 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
1982
Regulatory mutants of simian virus 40 Effect of mutations at a T antigen binding site on DNA replication and expression of viral genes
DiMaio D, Nathans D. Regulatory mutants of simian virus 40 Effect of mutations at a T antigen binding site on DNA replication and expression of viral genes. Journal Of Molecular Biology 1982, 156: 531-548. PMID: 6288959, DOI: 10.1016/0022-2836(82)90265-0.Peer-Reviewed Original ResearchConceptsViral DNA replicationDNA replicationEarly gene transcriptionT antigenGene transcriptionGene expressionCold-sensitive defectSecond-site mutationsSegment of DNAT antigen functionLate protein synthesisSimian virus 40 mutantsSV40 early proteinsLarge T antigenT-antigen geneEarly gene expressionBase pair substitutionsRegulatory mutantsRegulatory segmentRegulatory regionsDefined deletionsViral regulatory regionViral genesMutantsDNA show
1981
Binding of an SV40 T antigen-related protein to the DNA of SV40 regulatory mutants
McKay R, DiMaio D. Binding of an SV40 T antigen-related protein to the DNA of SV40 regulatory mutants. Nature 1981, 289: 810-813. PMID: 6258090, DOI: 10.1038/289810a0.Peer-Reviewed Original Research