Featured Publications
EGF‐stimulated tyrosine phosphorylation of p185neu: a potential model for receptor interactions.
Stern DF, Kamps MP. EGF‐stimulated tyrosine phosphorylation of p185neu: a potential model for receptor interactions. The EMBO Journal 1988, 7: 995-1001. PMID: 3261240, PMCID: PMC454426, DOI: 10.1002/j.1460-2075.1988.tb02906.x.Peer-Reviewed Original ResearchConceptsEGF-stimulated tyrosine phosphorylationTyrosine phosphorylationEGF receptorKinase activityReceptor-like proteinEGF receptor kinaseIntrinsic kinase activityRat-1 cellsTyrosine kinase activityEpidermal growth factor receptorReceptor kinaseGrowth factor receptorIncubation of cellsPhosphorylationEGFNeu/Factor receptorReceptor interactionSimilar kineticsGrowth factorP185ProteinP185neuReceptorsCellsp185, a product of the neu proto-oncogene, is a receptorlike protein associated with tyrosine kinase activity.
Stern DF, Heffernan PA, Weinberg RA. p185, a product of the neu proto-oncogene, is a receptorlike protein associated with tyrosine kinase activity. Molecular And Cellular Biology 1986, 6: 1729-1740. PMID: 2878363, PMCID: PMC367701, DOI: 10.1128/mcb.6.5.1729.Peer-Reviewed Original ResearchConceptsTyrosine kinase activityEGF receptorGrowth factor receptorProto-oncogeneKinase activityNeu proto-oncogeneC-erbB geneFactor receptorPresence of tunicamycinDistinct electrophoretic mobilitiesEpidermal growth factor receptorNormal culture conditionsMajor structural alterationsTyrosine phosphorylationGene productsNeu oncogeneNormal homologsOncogeneCell linesElectrophoretic mobilityCulture conditionsGrowth factorP185ProteinReceptors
2010
Interactions of ErbB4 and Kap1 Connect the Growth Factor and DNA Damage Response Pathways
Gilmore-Hebert M, Ramabhadran R, Stern DF. Interactions of ErbB4 and Kap1 Connect the Growth Factor and DNA Damage Response Pathways. Molecular Cancer Research 2010, 8: 1388-1398. PMID: 20858735, PMCID: PMC3901583, DOI: 10.1158/1541-7786.mcr-10-0042.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCell Line, TumorChlorocebus aethiopsCOS CellsDNA DamageDown-RegulationErbB ReceptorsGene Expression Regulation, EnzymologicGene Expression Regulation, NeoplasticHumansIntercellular Signaling Peptides and ProteinsProtein BindingReceptor, ErbB-4Repressor ProteinsSignal TransductionSilencer Elements, TranscriptionalSubstrate SpecificityTripartite Motif-Containing Protein 28ConceptsIntracellular domainKinase activityDNA damage response pathwayDamage response pathwayDNA damage responseErbB4 intracellular domainGrowth factor signalingHigh kinase activitySoluble intracellular domainExpression of genesReceptor tyrosine kinasesSuppression of MDM2Candidate interactorsDamage responseResponse pathwaysFactor signalingPlasma membraneMultiple isoformsErbB4 kinase activityTyrosine kinaseDNA damageRole of ErbB4Protein 1KAP1Conjoint regulation
2008
Regulation of the Rad53 protein kinase in signal amplification by oligomer assembly and disassembly
Jia-Lin Ma N, Stern DF. Regulation of the Rad53 protein kinase in signal amplification by oligomer assembly and disassembly. Cell Cycle 2008, 7: 808-817. PMID: 18239457, DOI: 10.4161/cc.7.6.5595.Peer-Reviewed Original ResearchConceptsRad53 activationDNA damageOligomer assemblyRad53 kinase activityRad53 protein kinaseAbsence of Mec1DNA damage responseSignal transduction processesMammalian Chk2Autophosphorylation activityGenetic requirementsCheckpoint responseChk2 activationDamage responseEffector kinaseProtein kinaseKinase activityRad53Forms oligomersTransduction processesSCD domainsInduced oligomerizationOligomer formationOligomerizationChk2
2005
Activation of the Checkpoint Kinase Rad53 by the Phosphatidyl Inositol Kinase-like Kinase Mec1*
Ma JL, Lee SJ, Duong JK, Stern DF. Activation of the Checkpoint Kinase Rad53 by the Phosphatidyl Inositol Kinase-like Kinase Mec1*. Journal Of Biological Chemistry 2005, 281: 3954-3963. PMID: 16365046, DOI: 10.1074/jbc.m507508200.Peer-Reviewed Original ResearchConceptsPhosphorylation-dependent mechanismDNA damageKinase activityDNA replication checkpoint pathwayRad53 kinase activityCheckpoint kinase Rad53Essential protein kinaseReplication checkpoint pathwayActivation of Rad53Protein kinase activityMammalian Chk2Rad53 phosphorylationRad53 activationRad53Protein kinaseDownstream responsesCheckpoint pathwayOrthologsAutophosphorylationKinasePhosphorylationIntermolecular mechanismActivationPIKKsComplexesRegulation of CHK2 by DNA-dependent Protein Kinase*
Li J, Stern DF. Regulation of CHK2 by DNA-dependent Protein Kinase*. Journal Of Biological Chemistry 2005, 280: 12041-12050. PMID: 15668230, DOI: 10.1074/jbc.m412445200.Peer-Reviewed Original ResearchMeSH KeywordsAndrostadienesAntigens, NuclearAtaxia Telangiectasia Mutated ProteinsCell Cycle ProteinsCells, CulturedCheckpoint Kinase 2DNADNA DamageDNA-Activated Protein KinaseDNA-Binding ProteinsEnzyme ActivationHumansKu AutoantigenNuclear ProteinsPhosphorylationProtein Serine-Threonine KinasesTumor Suppressor ProteinsWortmanninConceptsActivation of Chk2DNA-PKChk2 phosphorylationDNA damageDNA-Dependent Protein Kinase Catalytic SubunitProtein Kinase Catalytic SubunitDNA-dependent protein kinaseFunctional DNA-PKRegulation of Chk2Kinase catalytic subunitRegulation of DNAChk2 kinase activityATM-deficient cellsDiverse cellular responsesKinase inhibitor wortmanninATM-defective cellsChk2 activationExposure of cellsCatalytic subunitProtein kinaseKinase activityChk2Inhibitor wortmanninRabbit reticulocytesCellular responses
2003
Rad53 Phosphorylation Site Clusters Are Important for Rad53 Regulation and Signaling
Lee SJ, Schwartz MF, Duong JK, Stern DF. Rad53 Phosphorylation Site Clusters Are Important for Rad53 Regulation and Signaling. Molecular And Cellular Biology 2003, 23: 6300-6314. PMID: 12917350, PMCID: PMC180918, DOI: 10.1128/mcb.23.17.6300-6314.2003.Peer-Reviewed Original ResearchMeSH KeywordsAlanineAmino Acid SubstitutionBinding SitesCell Cycle ProteinsCheckpoint Kinase 2DNA DamageFungal ProteinsIntracellular Signaling Peptides and ProteinsMAP Kinase Kinase 1Mitogen-Activated Protein Kinase KinasesMutationPhosphorylationProtein KinasesProtein Serine-Threonine KinasesProtein Structure, TertiarySaccharomyces cerevisiae ProteinsSaccharomycetalesSchizosaccharomyces pombe ProteinsSignal TransductionConceptsDNA damage-induced interactionsPhosphorylation of Rad53Rad53 kinase activityTel1-dependent mannerEssential protein kinaseDNA damageConsensus phosphorylation sitesRad53 activationRad53 phosphorylationFHA domainPhosphorylation sitesCheckpoint functionUpstream kinaseYeast Rad53Protein kinaseRad53Kinase activityAlanine substitutionsReplication blockadeBasal interactionSubstitution mutationsImpaired interactionDun1Mec1Site clusters
2002
Chk2 Activation and Phosphorylation-Dependent Oligomerization
Xu X, Tsvetkov LM, Stern DF. Chk2 Activation and Phosphorylation-Dependent Oligomerization. Molecular And Cellular Biology 2002, 22: 4419-4432. PMID: 12024051, PMCID: PMC133858, DOI: 10.1128/mcb.22.12.4419-4432.2002.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAtaxia Telangiectasia Mutated ProteinsBinding SitesCell Cycle ProteinsCell-Free SystemCells, CulturedCheckpoint Kinase 2DNA DamageDNA-Binding ProteinsEnzyme ActivationFibroblastsGenes, Tumor SuppressorHumansMutationPhosphorylationProtein KinasesProtein Serine-Threonine KinasesProtein Structure, TertiaryRabbitsRadiation, IonizingRecombinant ProteinsSignal TransductionTumor Suppressor ProteinsConceptsSQ/TQ cluster domainsChk2 activationDNA damageDNA damage checkpoint pathwaySerine/threonine kinaseAutophosphorylation of Chk2Phosphorylation-dependent oligomerizationDamage checkpoint pathwayKinase catalytic domainForkhead-associated (FHA) domainWortmannin-sensitive kinaseChk2 kinase activityLimited DNA damageAmino acid substitutionsCell-free systemEukaryotic proteinsFHA domainActive Chk2Threonine kinaseCheckpoint functionCatalytic domainOligomeric complexesCheckpoint pathwayKinase activityChk2
1997
Mutations in SPK1/RAD53 that specifically abolish checkpoint but not growth-related functions
Fay DS, Sun Z, Stern D. Mutations in SPK1/RAD53 that specifically abolish checkpoint but not growth-related functions. Current Genetics 1997, 31: 97-105. PMID: 9021124, DOI: 10.1007/s002940050181.Peer-Reviewed Original ResearchMeSH KeywordsAllelesCell Cycle ProteinsCheckpoint Kinase 2Cloning, MolecularElectrophoresis, Polyacrylamide GelGene Expression Regulation, EnzymologicGene Expression Regulation, FungalMutagenesisPlasmidsProtein KinasesProtein Serine-Threonine KinasesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSequence DeletionTransformation, GeneticConceptsCheckpoint functionKinase domainKinase activityEssential protein kinaseWild-type levelsGrowth-related functionsCheckpoint arrestProtein kinaseDeletional analysisN-terminusSPK1Cell cycleMutant allelesGrowth activityMutationsRad53Normal rateSaccharomycesMultiple stagesKinaseDomainCheckpointActivityAllelesRegulation
1996
Spk1/Rad53 is regulated by Mec1-dependent protein phosphorylation in DNA replication and damage checkpoint pathways.
Sun Z, Fay DS, Marini F, Foiani M, Stern DF. Spk1/Rad53 is regulated by Mec1-dependent protein phosphorylation in DNA replication and damage checkpoint pathways. Genes & Development 1996, 10: 395-406. PMID: 8600024, DOI: 10.1101/gad.10.4.395.Peer-Reviewed Original ResearchMeSH KeywordsAlkaline PhosphataseCell CycleCell Cycle ProteinsCell DivisionCheckpoint Kinase 2DNA DamageDNA ReplicationDNA, FungalFungal ProteinsGene Expression Regulation, FungalGenes, FungalHydroxyureaImmunoblottingIntracellular Signaling Peptides and ProteinsMethyl MethanesulfonateMutagenesisPhosphorylationPrecipitin TestsProtein KinasesProtein Serine-Threonine KinasesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSignal TransductionTemperatureConceptsProtein kinaseCheckpoint pathwayEssential protein kinaseDamage checkpoint pathwayDamage-induced phosphorylationKinase-defective formG1/S boundarySignal transduction pathwaysRegulation of phosphorylationTreatment of cellsCheckpoint functionCdc mutantsDNA replicationProtein phosphorylationUpstream kinaseCheckpoint arrestRegulated phosphorylationTransduction pathwaysKinase activityCell cyclePhosphorylationS boundaryDamage DNACycle arrestKinase
1995
ScSpk1 Spk1 (S. cerevisiae)
Zheng P, Fay D, Stern D. ScSpk1 Spk1 (S. cerevisiae). 1995, 126-127. DOI: 10.1016/b978-012324719-3/50028-5.Peer-Reviewed Original ResearchKinase domainProtein kinaseMluI cell cycle boxS-phase-specific genesS phase-specific expressionPhase-specific genesPhase-specific expressionTyr kinase activitySer/ThrSpecific protein kinasesProtein tyrosine kinasesTranscriptional regulationMutant cellsNuclear proteinsNuclear localizationKinase activitySPK1DNA damageKinaseDNA synthesisProteinRepair synthesisGenesLatter activityImportant role
1993
SPK1 is an essential S-phase-specific gene of Saccharomyces cerevisiae that encodes a nuclear serine/threonine/tyrosine kinase.
Zheng P, Fay DS, Burton J, Xiao H, Pinkham JL, Stern DF. SPK1 is an essential S-phase-specific gene of Saccharomyces cerevisiae that encodes a nuclear serine/threonine/tyrosine kinase. Molecular And Cellular Biology 1993, 13: 5829-5842. PMID: 8355715, PMCID: PMC360328, DOI: 10.1128/mcb.13.9.5829.Peer-Reviewed Original ResearchMeSH KeywordsBase SequenceCell Cycle ProteinsCheckpoint Kinase 2Chromosome MappingDNA RepairFungal ProteinsGene ExpressionGene Expression Regulation, FungalGenes, FungalMolecular Sequence DataMutagenesis, InsertionalNuclear ProteinsOligodeoxyribonucleotidesPromoter Regions, GeneticProtein KinasesProtein Serine-Threonine KinasesRestriction MappingRNA, MessengerS PhaseSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSequence AlignmentSubstrate SpecificityConceptsSerine/threonine/tyrosine kinasesS-phase-specific transcriptionCell cycle-dependent transcriptionS-phase-specific genesDual-specificity protein kinaseImmune complex kinase assayTyr kinase activityTyrosine protein kinaseDNA synthesisExcision repair genesBudded cellsCEN plasmidGenomic libraryPositive regulatorProtein-SerKinase assaysProtein kinaseNuclear localizationNucleotide sequenceBox elementKinase activityGenetic techniquesSPK1Tyrosine kinaseUpstream region
1992
A subdomain in the transmembrane domain is necessary for p185neu* activation.
Cao H, Bangalore L, Bormann BJ, Stern DF. A subdomain in the transmembrane domain is necessary for p185neu* activation. The EMBO Journal 1992, 11: 923-932. PMID: 1347745, PMCID: PMC556533, DOI: 10.1002/j.1460-2075.1992.tb05131.x.Peer-Reviewed Original ResearchMeSH Keywords3T3 CellsAmino Acid SequenceAnimalsBase SequenceBlotting, WesternCell MembraneElectrophoresis, Polyacrylamide GelErbB ReceptorsGliomaGlutamatesGlutamic AcidMiceMolecular Sequence DataMutagenesis, Site-DirectedNeuroblastomaPrecipitin TestsProtein-Tyrosine KinasesProto-Oncogene ProteinsRatsReceptor, ErbB-2Signal TransductionValineConceptsTransmembrane domainTyrosine kinase activityKinase activityElevated tyrosine kinase activitySite-directed mutagenesisSpecific amino acidsEpidermal growth factor receptorGlutamic acidGrowth factor receptorEGF receptorPrimary structureAmino acidsFactor receptorProteinSpecific interactionsActivationDomainMutagenesisReceptorsMolecular weightAcidNeu proteinP185neuHigh propensityRole
1991
TPA inhibits the tyrosine kinase activity of the neu protein in vivo and in vitro.
Cao H, Decker S, Stern DF. TPA inhibits the tyrosine kinase activity of the neu protein in vivo and in vitro. Oncogene 1991, 6: 705-11. PMID: 1675782.Peer-Reviewed Original ResearchConceptsImmune complex kinase assayReceptor-like proteinTyrosine kinase activityProtein kinase CThreonine phosphorylationThreonine residuesTransmembrane domainKinase assaysTyrosine phosphorylationKinase activityAntiphosphotyrosine antibodyIncubation of cellsKinase CPhosphorylationPoint mutationsProteinNeu/Neu proteinLabeling experimentsSerineP185PhosphotyrosineTPAOncogenicMutations
1986
p185, a Product of the neu Proto-Oncogene, Is a Receptorlike Protein Associated with Tyrosine Kinase Activity
Stern D, Heffernan P, Weinberg R. p185, a Product of the neu Proto-Oncogene, Is a Receptorlike Protein Associated with Tyrosine Kinase Activity. Molecular And Cellular Biology 1986, 6: 1729-1740. DOI: 10.1128/mcb.6.5.1729-1740.1986.Peer-Reviewed Original ResearchTyrosine kinase activityEGF receptorGrowth factor receptorProto-oncogeneKinase activityNeu proto-oncogeneC-erbB geneFactor receptorPresence of tunicamycinDistinct electrophoretic mobilitiesEpidermal growth factor receptorNormal culture conditionsMajor structural alterationsTyrosine phosphorylationGene productsNeu oncogeneNormal homologsOncogeneCell linesElectrophoretic mobilityCulture conditionsGrowth factorP185ProteinReceptorsp185, a Product of the neu Proto-Oncogene, Is a Receptorlike Protein Associated with Tyrosine Kinase Activity
Stern D, Heffernan P, Weinberg R. p185, a Product of the neu Proto-Oncogene, Is a Receptorlike Protein Associated with Tyrosine Kinase Activity. Molecular And Cellular Biology 1986, 6: 1729-1740. DOI: 10.1128/mcb.6.5.1729-1740.1986.Peer-Reviewed Original ResearchEpidermal growth factorTyrosine kinase activityEpidermal growth factor receptorNeu proto-oncogeneAssociated with tyrosine kinase activityProto-oncogeneKinase activityNeu oncogenePresence of tunicamycinTyrosine phosphorylationNormal culture conditionsGene productsC-erbB geneMutated versionGrowth factorTransformed counterpartsGrowth factor receptorCell linesStimulated degradationElectrophoretic mobilityC-erbBCulture conditionsOncogeneGenesP185