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
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 substitutions
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