About
Titles
Research Scientist in Pharmacology
Appointments
Research
Research at a Glance
Yale Co-Authors
Frequent collaborators of Yuko Tsutsui's published research.
Publications Timeline
A big-picture view of Yuko Tsutsui's research output by year.
Mark A Lemmon, PhD, FRS
Steve Stayrook
Iris Van Alderwerelt Van Rosenburgh
Katerina Politi, PhD
Krishna C. Mudumbi, PhD
Michael Grant, MD
18Publications
355Citations
Publications
2024
Allosteric activation of the co-receptor BAK1 by the EFR receptor kinase initiates immune signaling
Mühlenbeck H, Tsutsui Y, Lemmon M, Bender K, Zipfel C. Allosteric activation of the co-receptor BAK1 by the EFR receptor kinase initiates immune signaling. ELife 2024, 12: rp92110. PMID: 39028038, PMCID: PMC11259431, DOI: 10.7554/elife.92110.Peer-Reviewed Original ResearchCitationsAltmetricMeSH Keywords and ConceptsConceptsKinase domainReceptor kinasePhosphorylation-dependent conformational changesActive conformationIntragenic suppressor mutationsCo-receptor BAK1Kinase-dead variantPlant receptor kinasesProtein kinase domainLeucine-rich repeatNon-catalytic functionsIntracellular kinase domainCo-receptorLRR-RKsSuppressor mutationsTrans-phosphorylationPseudokinase domainActivation loopActive kinaseAllosteric activationTransmembrane signalingBAK1Immune signalingRegulate signalingSignaling activityAllosteric activation of the co-receptor BAK1 by the EFR receptor kinase initiates immune signaling
Mühlenbeck H, Tsutsui Y, Lemmon M, Bender K, Zipfel C. Allosteric activation of the co-receptor BAK1 by the EFR receptor kinase initiates immune signaling. ELife 2024, 12 DOI: 10.7554/elife.92110.4.Peer-Reviewed Original ResearchAltmetricConceptsKinase domainReceptor kinasePhosphorylation-dependent conformational changesActive conformationIntragenic suppressor mutationsCo-receptor BAK1Kinase-dead variantPlant receptor kinasesProtein kinase domainLeucine-rich repeatNon-catalytic functionsIntracellular kinase domainCo-receptorLRR-RKsSuppressor mutationsTrans-phosphorylationPseudokinase domainActivation loopActive kinaseAllosteric activationTransmembrane signalingBAK1Immune signalingRegulate signalingSignaling activityDual function of LapB (YciM) in regulating Escherichia coli lipopolysaccharide synthesis
Shu S, Tsutsui Y, Nathawat R, Mi W. Dual function of LapB (YciM) in regulating Escherichia coli lipopolysaccharide synthesis. Proceedings Of The National Academy Of Sciences Of The United States Of America 2024, 121: e2321510121. PMID: 38635633, PMCID: PMC11046580, DOI: 10.1073/pnas.2321510121.Peer-Reviewed Original ResearchAltmetricMeSH Keywords and ConceptsConceptsLPS synthesisTetratricopeptide repeatCytoplasmic domainLevels of lipopolysaccharideCryo-EM structureGram-negative bacteriaLipopolysaccharide synthesisProtease FtsHRubredoxin domainLpxC activityTransmembrane helicesIn vivo analysisLpxCPseudomonas aeruginosaEnzymatic activityLapBFtsHAllosteric effectsYciMDual functionIn vitroTetratricopeptideAdaptorMotifDeacetylase
2022
Biochemical and structural basis for differential inhibitor sensitivity of EGFR with distinct exon 19 mutations
van Alderwerelt van Rosenburgh I, Lu D, Grant M, Stayrook S, Phadke M, Walther Z, Goldberg S, Politi K, Lemmon M, Ashtekar K, Tsutsui Y. Biochemical and structural basis for differential inhibitor sensitivity of EGFR with distinct exon 19 mutations. Nature Communications 2022, 13: 6791. PMID: 36357385, PMCID: PMC9649653, DOI: 10.1038/s41467-022-34398-z.Peer-Reviewed Original ResearchCitationsAltmetric
2021
Structural basis for ligand reception by anaplastic lymphoma kinase
Li T, Stayrook SE, Tsutsui Y, Zhang J, Wang Y, Li H, Proffitt A, Krimmer SG, Ahmed M, Belliveau O, Walker IX, Mudumbi KC, Suzuki Y, Lax I, Alvarado D, Lemmon MA, Schlessinger J, Klein DE. Structural basis for ligand reception by anaplastic lymphoma kinase. Nature 2021, 600: 148-152. PMID: 34819665, PMCID: PMC8639777, DOI: 10.1038/s41586-021-04141-7.Peer-Reviewed Original ResearchCitationsAltmetricMeSH Keywords and ConceptsStructural Insights into Pseudokinase Domains of Receptor Tyrosine Kinases
Sheetz J, Mathea S, Karvonen H, Malhotra K, Chatterjee D, Niininen W, Perttila R, Preuss F, Suresh K, Stayrook S, Tsutsui Y, Radhakrishnan R, Ungureanu D, Knapp S, Lemmon M. Structural Insights into Pseudokinase Domains of Receptor Tyrosine Kinases. The FASEB Journal 2021, 35 DOI: 10.1096/fasebj.2021.35.s1.02446.Peer-Reviewed Original ResearchConceptsReceptor tyrosine kinasesPseudokinase domainTyrosine kinaseTyrosine kinase-mediated signalingKey cellular processesKinase-mediated signalingExtracellular cuesViable drug targetTransduce signalsCellular processesEmbryonic developmentPseudokinasesTissue homeostasisFuture dissectionReceptor dimerizationStructural insightsKinase activityCancer hallmarksSignaling mechanismDrug targetsPutative routesKinaseOncogenic driversSmall moleculesPhosphotransfer
2017
Imatinib Binding to Human c-Src is Coupled to Inter-Domain Allostery and Suggest a Novel Kinase Inhibition Strategy
Tsutsui Y, Deredge D, Wintrode P, Hays F. Imatinib Binding to Human c-Src is Coupled to Inter-Domain Allostery and Suggest a Novel Kinase Inhibition Strategy. Biophysical Journal 2017, 112: 63a. DOI: 10.1016/j.bpj.2016.11.381.Peer-Reviewed Original Research
2016
Imatinib binding to human c-Src is coupled to inter-domain allostery and suggests a novel kinase inhibition strategy
Tsutsui Y, Deredge D, Wintrode P, Hays F. Imatinib binding to human c-Src is coupled to inter-domain allostery and suggests a novel kinase inhibition strategy. Scientific Reports 2016, 6: 30832. PMID: 27480221, PMCID: PMC4969603, DOI: 10.1038/srep30832.Peer-Reviewed Original ResearchCitationsMeSH Keywords and ConceptsConceptsHuman c-SrcC-SrcNon-receptor tyrosine kinase inhibitorsFunctional regulatory sitesC-Src SH3SH2 domainKinase domainHydrogen-deuterium exchangeKinase activationConformational dynamicsRegulatory sitesAllosteric siteMutation sitesKinase inhibitorsPatient tissuesInhibition strategiesAnti-neoplastic drugsPeptide ligandsDevelopment of TKICurrent study identifiesImatinib-resistant mutationsTyrosine kinase inhibitorsImatinib analogsMass spectrometryAllostery
2015
Conformation-Dependent Human p52Shc Phosphorylation by Human c‑Src
Tsutsui Y, Johnson J, Demeler B, Kinter M, Hays F. Conformation-Dependent Human p52Shc Phosphorylation by Human c‑Src. Biochemistry 2015, 54: 3469-3482. PMID: 25961473, DOI: 10.1021/acs.biochem.5b00122.Peer-Reviewed Original ResearchCitationsAltmetricMeSH Keywords and ConceptsMeSH KeywordsCell MembraneCSK Tyrosine-Protein KinaseExtracellular Signal-Regulated MAP KinasesGRB2 Adaptor ProteinHumansMAP Kinase Signaling SystemPhosphatidylinositol PhosphatesPhosphorylationProtein StabilityProto-Oncogene Proteins p21(ras)Shc Signaling Adaptor ProteinsSrc Homology 2 Domain-Containing, Transforming Protein 1Src-Family KinasesConceptsHuman c-SrcMembrane-mimetic environmentsC-SrcPhosphorylation sitesAdaptor proteinGrb2 adaptor proteinPhosphorylation-dependent interactionPhosphorylation levelsRas/MAPKAmount of phosphorylationActive c-SrcCascade activationProtein phosphorylationMass spectrometry analysisComplex assemblyPhosphorylation statePhosphorylation statusP52ShcTyrosine residuesPhosphatidylinositol 4Tyrosine kinaseBiophysical characterizationInitial binding interactionGrb2Functional linkage
2014
Overproduction and biophysical characterization of human HSP70 proteins
Boswell-Casteel R, Johnson J, Duggan K, Tsutsui Y, Hays F. Overproduction and biophysical characterization of human HSP70 proteins. Protein Expression And Purification 2014, 106: 57-65. PMID: 25266791, PMCID: PMC4248018, DOI: 10.1016/j.pep.2014.09.013.Peer-Reviewed Original ResearchCitationsMeSH Keywords and ConceptsConceptsHuman HSP70 proteinHeat shock proteinsResponse pathwaysHSP70 proteinBiophysical characterizationFacilitate protein foldingVital cellular functionsInitial biophysical characterizationProtein-protein interactionsFuture biochemical studiesHeterologous overexpressionHSP functionCellular functionsProtein functionProtein foldingHSP70 familyFunctional characterizationConformational rearrangementsShock proteinsChemical stressorsHuman Hsp70HSP proteinsDownstream investigationsBiochemical studiesEscherichia coli