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 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
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