2023
Allosteric inhibition of the T cell receptor by a designed membrane ligand
Ye Y, Morita S, Chang J, Buckley P, Wilhelm K, DiMaio D, Groves J, Barrera F. Allosteric inhibition of the T cell receptor by a designed membrane ligand. ELife 2023, 12: e82861. PMID: 37796108, PMCID: PMC10554751, DOI: 10.7554/elife.82861.Peer-Reviewed Original ResearchConceptsT cell receptorTCR activationCD3ζ subunitsTM ligandsComplex molecular machinesReceptor tyrosine kinase EphA2Cell receptorTM domainTransmembrane domainNative nanodiscsTCR subunitsAllosteric changesTM bundleCytoplasmic sideTM regionMolecular mechanismsExtracellular domainAllosteric inhibitionLck phosphorylationMolecular machinesMembrane receptorsAberrant activationSubunitsMembrane ligandsDecades of investigation
1999
Bovine papillomavirus E2 protein activates a complex growth-inhibitory program in p53-negative HT-3 cervical carcinoma cells that includes repression of cyclin A and cdc25A phosphatase genes and accumulation of hypophosphorylated retinoblastoma protein.
Naeger L, Goodwin E, Hwang E, DeFilippis R, Zhang H, DiMaio D. Bovine papillomavirus E2 protein activates a complex growth-inhibitory program in p53-negative HT-3 cervical carcinoma cells that includes repression of cyclin A and cdc25A phosphatase genes and accumulation of hypophosphorylated retinoblastoma protein. Molecular Cancer Research 1999, 10: 413-22. PMID: 10392903.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCarrier ProteinsCattleCdc25 PhosphatasesCDC2-CDC28 KinasesCell Cycle ProteinsCell DivisionCyclin ACyclin-Dependent Kinase 2Cyclin-Dependent Kinase Inhibitor p21Cyclin-Dependent KinasesCyclinsDNA-Binding ProteinsE2F Transcription FactorsE2F1 Transcription FactorEnzyme InhibitorsFemaleGene Expression RegulationGrowth InhibitorsHeLa CellsHumansPhosphoprotein PhosphatasesPhosphorylationProtein Serine-Threonine KinasesProtein Tyrosine PhosphatasesRepressor ProteinsRetinoblastoma ProteinRetinoblastoma-Binding Protein 1Transcription Factor DP1Transcription FactorsTumor Cells, CulturedTumor Suppressor Protein p53Uterine Cervical NeoplasmsViral ProteinsConceptsCervical carcinoma cell linesHT-3 cellsCarcinoma cell linesE2 proteinE6/E7 genesCell linesGrowth inhibitionCervical carcinoma cellsCyclin ACyclin-dependent kinase 2 activityExpression of CDC25AKinase 2 activityE7 genesCell cycle componentsCarcinoma cellsCDC25B expressionE2 expressionProtein levels
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 substitutionsOncogenic 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 ResearchConceptsBa/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
Virocrine 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
1996
Activation of the endogenous p53 growth inhibitory pathway in HeLa cervical carcinoma cells by expression of the bovine papillomavirus E2 gene.
Hwang E, Naeger L, DiMaio D. Activation of the endogenous p53 growth inhibitory pathway in HeLa cervical carcinoma cells by expression of the bovine papillomavirus E2 gene. Oncogene 1996, 12: 795-803. PMID: 8632901.Peer-Reviewed Original ResearchMeSH KeywordsBovine papillomavirus 1CDC2-CDC28 KinasesCell DivisionCyclin-Dependent Kinase 2Cyclin-Dependent Kinase Inhibitor p21Cyclin-Dependent KinasesCyclinsDNA ReplicationDNA-Binding ProteinsEnzyme InhibitorsFemaleGene Expression Regulation, NeoplasticGene Expression Regulation, ViralGenes, ViralHeLa CellsHumansModels, BiologicalPhosphorylationProtein Serine-Threonine KinasesTumor Suppressor Protein p53Uterine Cervical NeoplasmsViral ProteinsConceptsTumor suppressor proteinGrowth inhibitory pathwaySuppressor proteinHeLa cellsP21/waf1Kinase activityE2 geneBPV E2 proteinP53 tumor suppressor proteinCdk2/cyclin E kinase activityCyclin-dependent kinase inhibitorGrowth regulatory pathwaysHeLa cervical carcinoma cellsP53-responsive genesCell cycle regulatory proteinsCDK kinase activityCyclin E kinase activityCycle regulatory proteinsDependent kinase inhibitorG1 cell cycle regulatory proteinsB-MybTranscription factorsRegulatory proteinsRegulatory pathwaysP105Rb
1995
Ligand-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
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