2000
Structural basis of the recognition of the Dishevelled DEP domain in the Wnt signaling pathway
Wong H, Mao J, Nguyen J, Srinivas S, Zhang W, Liu B, Li L, Wu D, Zheng J. Structural basis of the recognition of the Dishevelled DEP domain in the Wnt signaling pathway. Nature Structural & Molecular Biology 2000, 7: 1178-1184. PMID: 11101902, PMCID: PMC4381838, DOI: 10.1038/82047.Peer-Reviewed Original Research3T3 CellsAdaptor Proteins, Signal TransducingAmino Acid SequenceAmino Acid SubstitutionAnimalsBinding SitesCell MembraneDishevelled ProteinsDNA-Binding ProteinsLymphoid Enhancer-Binding Factor 1Membrane ProteinsMiceModels, MolecularMolecular Sequence DataMutationNuclear Magnetic Resonance, BiomolecularPhosphoproteinsProtein BindingProtein FoldingProtein Structure, SecondaryProtein Structure, TertiaryProto-Oncogene ProteinsSequence AlignmentSignal TransductionStatic ElectricityStructure-Activity RelationshipSubstrate SpecificityTranscription FactorsTransfectionWnt ProteinsZebrafish ProteinsProtein Phosphatase 2Cα Dephosphorylates Axin and Activates LEF-1-dependent Transcription*
Wu D, Strovel E, Sussman D. Protein Phosphatase 2Cα Dephosphorylates Axin and Activates LEF-1-dependent Transcription*. Journal Of Biological Chemistry 2000, 275: 2399-2403. PMID: 10644691, DOI: 10.1074/jbc.275.4.2399.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Proteins, Signal TransducingAnimalsAxin ProteinCOS CellsDishevelled ProteinsDNA-Binding ProteinsEnzyme ActivationJNK Mitogen-Activated Protein KinasesLymphoid Enhancer-Binding Factor 1Mitogen-Activated Protein KinasesPhosphoprotein PhosphatasesPhosphoproteinsPhosphorylationPrecipitin TestsProtein BindingProtein Phosphatase 2Protein Phosphatase 2CProteinsRepressor ProteinsSaccharomyces cerevisiae ProteinsSignal TransductionTranscription FactorsTranscriptional ActivationConceptsLEF-1-dependent transcriptionWnt signal transductionSignal transductionExpression of PP2CProtein phosphatase 2CalphaProtein phosphatase 2CαTwo-hybrid systemDishevelled gene familyReporter gene assayGene familyPositive regulatorCytoplasmic proteinsPP2CNegative regulatorAxinWnt-1Gene assayTranscriptionTransductionRegulatorSynergistic responseProteinExpressionDephosphorylationRepression
1999
Suppression of Glycogen Synthase Kinase Activity Is Not Sufficient for Leukemia Enhancer Factor-1 Activation*
Yuan H, Mao J, Li L, Wu D. Suppression of Glycogen Synthase Kinase Activity Is Not Sufficient for Leukemia Enhancer Factor-1 Activation*. Journal Of Biological Chemistry 1999, 274: 30419-30423. PMID: 10521419, DOI: 10.1074/jbc.274.43.30419.Peer-Reviewed Original ResearchMeSH Keywords3T3 CellsAdaptor Proteins, Signal TransducingAnimalsAxin ProteinBeta CateninCalcium-Calmodulin-Dependent Protein KinasesCarrier ProteinsCytoskeletal ProteinsDNA-Binding ProteinsEnzyme ActivationGenes, ReporterGlycogen Synthase Kinase 3Glycogen Synthase KinasesLuciferasesLymphoid Enhancer-Binding Factor 1MiceNeoplasm ProteinsPhosphorylationProtein Serine-Threonine KinasesProteinsProtein-Tyrosine KinasesProto-Oncogene ProteinsProto-Oncogene Proteins c-aktRecombinant ProteinsRepressor ProteinsSignal TransductionTrans-ActivatorsTranscription FactorsTranscription, GeneticTransfectionWnt ProteinsWnt1 ProteinZebrafish ProteinsConceptsGlycogen synthase kinase-3LEF-1-dependent transcriptionKinase activityWnt proteinsWnt-1Glycogen synthase kinase activitySynthase kinase activityProtein kinase AktSynthase kinase-3Enhancer factor-1Kinase AktAxinKinase 3MAktPeptide substratesReduced associationAktPhe residueTyr-216Factor 1TranscriptionFRATProteinActivationAdditional mechanismAxin and Frat1 interact with Dvl and GSK, bridging Dvl to GSK in Wnt‐mediated regulation of LEF‐1
Li L, Yuan H, Weaver C, Mao J, Farr G, Sussman D, Jonkers J, Kimelman D, Wu D. Axin and Frat1 interact with Dvl and GSK, bridging Dvl to GSK in Wnt‐mediated regulation of LEF‐1. The EMBO Journal 1999, 18: 4233-4240. PMID: 10428961, PMCID: PMC1171499, DOI: 10.1093/emboj/18.15.4233.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Proteins, Signal TransducingAnimalsAxin ProteinCalcium-Calmodulin-Dependent Protein KinasesDishevelled ProteinsDNA-Binding ProteinsGlycogen Synthase Kinase 3Glycogen Synthase KinasesLymphoid Enhancer-Binding Factor 1PhosphoproteinsProtein BindingProtein ConformationProteinsProto-Oncogene ProteinsRepressor ProteinsSignal TransductionTranscription FactorsWnt ProteinsWnt1 ProteinXenopusXenopus ProteinsZebrafish ProteinsDishevelled Proteins Lead to Two Signaling Pathways REGULATION OF LEF-1 AND c-Jun N-TERMINAL KINASE IN MAMMALIAN CELLS*
Li L, Yuan H, Xie W, Mao J, Caruso A, McMahon A, Sussman D, Wu D. Dishevelled Proteins Lead to Two Signaling Pathways REGULATION OF LEF-1 AND c-Jun N-TERMINAL KINASE IN MAMMALIAN CELLS*. Journal Of Biological Chemistry 1999, 274: 129-134. PMID: 9867820, DOI: 10.1074/jbc.274.1.129.Peer-Reviewed Original ResearchMeSH Keywords3T3 CellsAdaptor Proteins, Signal TransducingAnimalsBeta CateninCalcium-Calmodulin-Dependent Protein KinasesCell Cycle ProteinsCOS CellsCytoskeletal ProteinsDishevelled ProteinsDNA-Binding ProteinsEnzyme ActivationJNK Mitogen-Activated Protein KinasesLymphoid Enhancer-Binding Factor 1MiceMitogen-Activated Protein KinasesPhosphoproteinsSignal TransductionTrans-ActivatorsTranscription FactorsTranscription, GeneticUp-RegulationConceptsJNK activationMammalian cellsT-cell factorSmall G proteinsC-Jun N-terminal kinaseDominant negative mutantBeta-catenin levelsDifferent signaling pathwaysCOS-7 cellsN-terminal kinaseC-Jun NDishevelled proteinsDvl proteinsDEP domainDependent transcriptionNegative mutantPathway regulationKinase activityLEF-1Transcription activitySignaling pathwaysG proteinsNovel pathwayCell factorProtein
1998
Guanine nucleotide exchange factor GEF115 specifically mediates activation of Rho and serum response factor by the G protein α subunit Gα13
Mao J, Yuan H, Xie W, Wu D. Guanine nucleotide exchange factor GEF115 specifically mediates activation of Rho and serum response factor by the G protein α subunit Gα13. Proceedings Of The National Academy Of Sciences Of The United States Of America 1998, 95: 12973-12976. PMID: 9789025, PMCID: PMC23675, DOI: 10.1073/pnas.95.22.12973.Peer-Reviewed Original ResearchMeSH Keywords3T3 CellsAmino Acid SequenceAnimalsCOS CellsDNA-Binding ProteinsGene Expression RegulationGTPase-Activating ProteinsGTP-Binding ProteinsGuanine Nucleotide Exchange FactorsKineticsLuciferasesMiceMolecular Sequence DataNuclear ProteinsProteinsRecombinant Fusion ProteinsRhoA GTP-Binding ProteinSequence AlignmentSequence Homology, Amino AcidSerum Response FactorSignal TransductionTranscription FactorsTranscription, GeneticTransfectionConceptsSerum response factorActivation of RhoSRF activationHeterotrimeric G protein alpha subunitsG protein signaling (RGS) domainG protein alpha subunitsTerminal partRho-specific guanineProtein alpha subunitsResponse factorDomain deletion mutantSignal transduction pathwaysNIH 3T3 cellsDbl homologyRGS activitySequence motifsTransduction pathwaysGalpha13Signaling domainsGalpha12Alpha subunitMutantsSynergistic activationGalphaqTransfection systemTec/Bmx non‐receptor tyrosine kinases are involved in regulation of Rho and serum response factor by Gα12/13
Mao J, Xie W, Yuan H, Simon M, Mano H, Wu D. Tec/Bmx non‐receptor tyrosine kinases are involved in regulation of Rho and serum response factor by Gα12/13. The EMBO Journal 1998, 17: 5638-5646. PMID: 9755164, PMCID: PMC1170892, DOI: 10.1093/emboj/17.19.5638.Peer-Reviewed Original ResearchConceptsNon-receptor tyrosine kinase familySerum response factorExpression of Galpha12SRF activationRho-independent pathwayThrombin effectTyrosine kinase familyActivation of SRFNon-receptor tyrosine kinaseG12/13 proteinsRho-dependent pathwayInvolvement of RhoTec kinasesActive alpha subunitG12 familyActivationTransient transfection systemTyrosine kinaseAlpha subunitCellsNIH 3T3 cellsKinase-deficient mutantKinaseRegulation of RhoSpecific Involvement of G Proteins in Regulation of Serum Response Factor-mediated Gene Transcription by Different Receptors*
Mao J, Yuan H, Xie W, Simon M, Wu D. Specific Involvement of G Proteins in Regulation of Serum Response Factor-mediated Gene Transcription by Different Receptors*. Journal Of Biological Chemistry 1998, 273: 27118-27123. PMID: 9765229, DOI: 10.1074/jbc.273.42.27118.Peer-Reviewed Original ResearchMeSH Keywords15-Hydroxy-11 alpha,9 alpha-(epoxymethano)prosta-5,13-dienoic Acid3T3 CellsAnimalsDNA-Binding ProteinsDrug SynergismEndothelinsGene Expression RegulationGTPase-Activating ProteinsGTP-Binding ProteinsLysophospholipidsMiceNuclear ProteinsProteinsReceptors, Cell SurfaceSerum Response FactorThrombinTranscription, GeneticConceptsThromboxane A2Lysophosphatidic acidType 1 muscarinic receptorG proteinsAlpha1-adrenergic receptorsInterleukin-8 receptorEndogenous G proteinsG protein-coupled receptorsProtein-coupled receptorsEndothelin receptorsMuscarinic receptorsDopamine receptorsSRF activationSerum response factorType 1Gene transcriptionReceptorsDifferent receptorsG protein subunitsSpecific involvementGalphaq/11Gq classCell linesNIH3T3 cellsThrombin
1996
Selective G Protein Coupling by C-C Chemokine Receptors (∗)
Kuang Y, Wu Y, Jiang H, Wu D. Selective G Protein Coupling by C-C Chemokine Receptors (∗). Journal Of Biological Chemistry 1996, 271: 3975-3978. PMID: 8626727, DOI: 10.1074/jbc.271.8.3975.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAvian ProteinsCell LineChemokine CCL2Chlorocebus aethiopsCloning, MolecularDNA PrimersDNA-Binding ProteinsGTP-Binding ProteinsHumansKineticsMonocytesPertussis ToxinPolymerase Chain ReactionReceptors, CCR2Receptors, ChemokineReceptors, CytokineRecombinant ProteinsTransfectionType C PhospholipasesVirulence Factors, BordetellaZinc FingersConceptsC chemokine receptor 1C chemokine receptorChemokine receptorsBroad spectrum anti-inflammatory drugsPertussis toxin-sensitive mannerChemokine receptor 1MCP-1 receptorAnti-inflammatory drugsG protein coupling specificityToxin-sensitive mannerGq classG protein couplingAccumulation of inositolPhospholipase CC chemokinesT cellsInflammatory reactionCotransfected COS-7 cellsGi proteinsReceptor 1Major mediatorC-terminal intracellular domainG beta gammaProtein couplingReceptors