2024
The CUL5 E3 ligase complex negatively regulates central signaling pathways in CD8+ T cells
Liao X, Li W, Zhou H, Rajendran B, Li A, Ren J, Luan Y, Calderwood D, Turk B, Tang W, Liu Y, Wu D. The CUL5 E3 ligase complex negatively regulates central signaling pathways in CD8+ T cells. Nature Communications 2024, 15: 603. PMID: 38242867, PMCID: PMC10798966, DOI: 10.1038/s41467-024-44885-0.Peer-Reviewed Original ResearchConceptsCD8+ T cellsT cellsCancer immunotherapyMouse CD8+ T cellsAnti-tumor immunityTumor growth inhibition abilityAnti-tumor effectsInhibition of neddylationCD8Effector functionsTCR stimulationIL2 signalingCentral signaling pathwaysCore signaling pathwaysEffector activityNegative regulatory mechanismsTranslational implicationsImmunotherapyGrowth inhibition abilityCytokine signalingTCRProteomic alterationsSignaling pathwayCancerCRISPR-based screens
2010
[High glucose increases periostin expression and the related signal pathway in adult rat cardiac fibroblasts].
Zou P, Wu L, Wu D, Fan D, Cui X, Zhou Y, Wang C, Li L. [High glucose increases periostin expression and the related signal pathway in adult rat cardiac fibroblasts]. Acta Physiol Sinica 2010, 62: 247-54. PMID: 20571742.Peer-Reviewed Original Research
2007
Quantitative Phosphoproteome Profiling of Wnt3a-mediated Signaling Network Indicating the Involvement of Ribonucleoside-diphosphate Reductase M2 Subunit Phosphorylation at Residue Serine 20 in Canonical Wnt Signal Transduction*
Tang L, Deng N, Wang L, Dai J, Wang Z, Jiang X, Li S, Li L, Sheng Q, Wu D, Li L, Zeng R. Quantitative Phosphoproteome Profiling of Wnt3a-mediated Signaling Network Indicating the Involvement of Ribonucleoside-diphosphate Reductase M2 Subunit Phosphorylation at Residue Serine 20 in Canonical Wnt Signal Transduction*. Molecular & Cellular Proteomics 2007, 6: 1952-1967. PMID: 17693683, DOI: 10.1074/mcp.m700120-mcp200.Peer-Reviewed Original ResearchConceptsCanonical WntDifferential phosphoproteinsWnt3a stimulationMultiple post-translational modificationsCanonical Wnt signal transductionWnt signal transductionUnique phosphorylation sitesPost-translational modificationsInteraction network analysisStable isotopic formsCanonical Wnt signalingReporter gene assayInhibitor of WntPhosphorylation networksNovel phosphoproteinsExtracellular stimuliPhosphoproteome profilingPhosphorylation sitesSignaling networksPhosphorylation regulationProtein phosphorylationSignal transductionPhosphorylation changesRNA interferenceDownstream effectors
2005
Using biosensors to detect the release of serotonin from taste buds during taste stimulation.
Huang Y, Maruyama Y, Lu K, Pereira E, Plonsky I, Baur J, Wu D, Roper S. Using biosensors to detect the release of serotonin from taste buds during taste stimulation. Archives Italiennes De Biologie 2005, 143: 87-96. PMID: 16106989, PMCID: PMC3712826.Peer-Reviewed Original Research
2002
Regulation of Gli1 Transcriptional Activity in the Nucleus by Dyrk1*
Mao J, Maye P, Kogerman P, Tejedor F, Toftgard R, Xie W, Wu G, Wu D. Regulation of Gli1 Transcriptional Activity in the Nucleus by Dyrk1*. Journal Of Biological Chemistry 2002, 277: 35156-35161. PMID: 12138125, DOI: 10.1074/jbc.m206743200.Peer-Reviewed Original ResearchMeSH Keywords3T3 CellsAnimalsCell DifferentiationCell NucleusCOS CellsGene Expression RegulationHedgehog ProteinsMiceOncogene ProteinsPhosphorylationPrecipitin TestsProtein Serine-Threonine KinasesProtein TransportProtein-Tyrosine KinasesSignal TransductionTrans-ActivatorsTranscription FactorsTranscription, GeneticZinc Finger Protein GLI1ConceptsTranscriptional activityGene transcriptionDual-specificity protein kinaseNuclear export mutantGLI1 transcriptional activityMouse C3H10T1/2 cellsReporter gene assayCellular rolesExport mutantsTranscriptional regulationProtein kinaseKinase activityC3H10T1/2 cellsLEF-1Kinase 1DYRK1Sonic hedgehogC-JunGene assayCell nucleiShhTranscriptionRegulationGli1Pathway
2001
Gα16 Couples Chemoattractant Receptors to NF-κB Activation
Yang M, Sang H, Rahman A, Wu D, Malik A, Ye R. Gα16 Couples Chemoattractant Receptors to NF-κB Activation. The Journal Of Immunology 2001, 166: 6885-6892. PMID: 11359849, DOI: 10.4049/jimmunol.166.11.6885.Peer-Reviewed Original ResearchMeSH KeywordsActive Transport, Cell NucleusAmino Acid SubstitutionCell NucleusEnzyme ActivationGenes, ReporterGlutamineGTP-Binding Protein alpha Subunits, Gq-G11HeLa CellsHeterotrimeric GTP-Binding ProteinsHumansIsoenzymesLeucineLuciferasesNF-kappa BPhospholipase C betaReceptors, ChemokineReceptors, Formyl PeptideReceptors, ImmunologicReceptors, PeptideSignal TransductionTrans-ActivatorsTransfectionType C PhospholipasesConceptsNF-kappaB activationFormyl peptide receptorChemoattractant receptorsPeptide receptorCXC chemokine receptor 2NF-kappaB.Chemokine receptor 2Regulatory protein alpha subunitNF-κB activationLuciferase activityProtein kinase CKappaB-luciferase activityPhosphorylation of IkappaBalphaPhospholipase C-beta activityC3a receptorReceptor 2Seven-membrane-spanning receptorsAgonist stimulationConventional PKC isoformsPharmacological inhibitorsLuciferase reporterReceptorsHemopoietic cellsProtein alpha subunitsCell model systemLow-Density Lipoprotein Receptor-Related Protein-5 Binds to Axin and Regulates the Canonical Wnt Signaling Pathway
Mao J, Wang J, Liu B, Pan W, Farr G, Flynn C, Yuan H, Takada S, Kimelman D, Li L, Wu D. Low-Density Lipoprotein Receptor-Related Protein-5 Binds to Axin and Regulates the Canonical Wnt Signaling Pathway. Molecular Cell 2001, 7: 801-809. PMID: 11336703, DOI: 10.1016/s1097-2765(01)00224-6.Peer-Reviewed Original Research3T3 CellsAmino Acid SequenceAnimalsAxin ProteinCalcium-Calmodulin-Dependent Protein KinasesCOS CellsGene ExpressionGlycogen Synthase Kinase 3LDL-Receptor Related ProteinsLow Density Lipoprotein Receptor-Related Protein-5MammalsMiceMolecular Sequence DataMutagenesisProtein BindingProtein Structure, TertiaryProteinsProto-Oncogene ProteinsReceptors, LDLRepressor ProteinsSignal TransductionWnt ProteinsZebrafish ProteinsCalcium Responses to Thyrotropin-Releasing Hormone, Gonadotropin-Releasing Hormone and Somatostatin in Phospholipase Cβ3 Knockout Mice
Romoser V, Graves T, Wu D, Jiang H, Hinkle P. Calcium Responses to Thyrotropin-Releasing Hormone, Gonadotropin-Releasing Hormone and Somatostatin in Phospholipase Cβ3 Knockout Mice. Endocrinology 2001, 15: 125-135. PMID: 11145744, DOI: 10.1210/mend.15.1.0588.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAortaBlotting, WesternCalciumCells, CulturedFemaleFluorescent Antibody TechniqueGonadotropin-Releasing HormoneIsoenzymesMaleMiceMice, KnockoutMicroscopy, FluorescenceMuscle, Smooth, VascularPituitary GlandSignal TransductionSomatostatinThyrotropin-Releasing HormoneType C PhospholipasesConceptsWild-type miceKnockout micePituitary cellsSmooth muscle cellsCalcium responseIntracellular calciumMuscle cellsAortic smooth muscle cellsThyrotropin-Releasing HormoneCalcium-mobilizing actionGonadotropin-Releasing HormoneInhibited influxMicroM TRHExtracellular calciumSomatostatinPituitary tissueKnockout animalsMiceHormoneSignal pathwayPLCbeta1Phospholipase CbetaPLCbeta3CalciumGalphaq/11
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 ProteinsRoles of phospholipid signaling in chemoattractant-induced responses
Wu D, Huang C, Jiang H. Roles of phospholipid signaling in chemoattractant-induced responses. Journal Of Cell Science 2000, 113: 2935-2940. PMID: 10934033, DOI: 10.1242/jcs.113.17.2935.Peer-Reviewed Original ResearchRoles of PLC-β2 and -β3 and PI3Kγ in Chemoattractant-Mediated Signal Transduction
Li Z, Jiang H, Xie W, Zhang Z, Smrcka A, Wu D. Roles of PLC-β2 and -β3 and PI3Kγ in Chemoattractant-Mediated Signal Transduction. Science 2000, 287: 1046-1049. PMID: 10669417, DOI: 10.1126/science.287.5455.1046.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsB-LymphocytesChemokine CCL4Chemotactic FactorsChemotaxis, LeukocyteImmunoglobulin lambda-ChainsIsoenzymesMacrophage Inflammatory ProteinsMiceNeutrophil InfiltrationNeutrophilsN-Formylmethionine Leucyl-PhenylalaninePeritonitisPhosphatidylinositol 3-KinasesPhosphatidylinositol PhosphatesPhospholipase C betaPhosphorylationSignal TransductionSkin UlcerSuperoxidesType C PhospholipasesClimbing fiber synapse elimination during postnatal cerebellar development requires signal transduction involving Gαq and phospholipase Cβ4
Hashimoto K, Watanabe M, Kurihara H, Offermanns S, Jiang H, Wu Y, Jun K, Shin H, Inoue Y, Wu D, Simon M, Kano M. Climbing fiber synapse elimination during postnatal cerebellar development requires signal transduction involving Gαq and phospholipase Cβ4. Progress In Brain Research 2000, 124: 31-48. PMID: 10943115, DOI: 10.1016/s0079-6123(00)24006-5.Peer-Reviewed Original ResearchAge FactorsAnimalsAtaxiaCell SizeCerebellumExcitatory Postsynaptic PotentialsGene Expression Regulation, DevelopmentalGene Expression Regulation, EnzymologicGTP-Binding Protein alpha Subunits, Gq-G11GTP-Binding ProteinsIsoenzymesMiceMice, Neurologic MutantsMicroscopy, ElectronNerve FibersOrgan Culture TechniquesPhospholipase C betaPurkinje CellsRNA, MessengerSignal TransductionSynapsesType C PhospholipasesProtein 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 Rho
1997
α-Latrotoxin Stimulates Exocytosis by the Interaction with a Neuronal G-Protein-Coupled Receptor
Krasnoperov V, Bittner M, Beavis R, Kuang Y, Salnikow K, Chepurny O, Little A, Plotnikov A, Wu D, Holz R, Petrenko A. α-Latrotoxin Stimulates Exocytosis by the Interaction with a Neuronal G-Protein-Coupled Receptor. Neuron 1997, 18: 925-937. PMID: 9208860, DOI: 10.1016/s0896-6273(00)80332-3.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBrain ChemistryCalciumCattleChromaffin GranulesCloning, MolecularCOS CellsDimerizationExocytosisGTP-Binding ProteinsMembrane ProteinsMolecular Sequence DataProtein PrecursorsQa-SNARE ProteinsRatsReceptors, Cell SurfaceReceptors, PeptideRecombinant ProteinsSensory Receptor CellsSequence AlignmentSequence Homology, Amino AcidSignal TransductionSpider VenomsTissue DistributionConceptsG protein-coupled receptorsAlpha-latrotoxin receptorNeuronal G protein-coupled receptorNovel orphan G-protein-coupled receptorI alphaCalcium-independent receptorSecretin receptor familyOrphan G protein-coupled receptorRegulation of neurosecretionEndogenous proteolytic cleavageMolecular cloningPrecursor polypeptideSerpentine receptorsCIRLFusion complexExtracellular bindingAlpha-LatrotoxinFunctional expressionReceptor familyProteolytic cleavagePresynaptic receptorsAffinity columnNeurotransmitter releaseStable complexesPresynaptic neurotoxins
1996
Pertussis Toxin-sensitive Activation of Phospholipase C by the C5a and fMet-Leu-Phe Receptors*
Jiang H, Kuang Y, Wu Y, Smrcka A, Simon M, Wu D. Pertussis Toxin-sensitive Activation of Phospholipase C by the C5a and fMet-Leu-Phe Receptors*. Journal Of Biological Chemistry 1996, 271: 13430-13434. PMID: 8662841, DOI: 10.1074/jbc.271.23.13430.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsAntigens, CDCell LineEnzyme ActivationGTP-Binding ProteinsMolecular Sequence DataPertussis ToxinReceptor, Anaphylatoxin C5aReceptors, ComplementReceptors, Formyl PeptideReceptors, ImmunologicReceptors, PeptideSignal TransductionTransfectionType C PhospholipasesVirulence Factors, BordetellaConceptsPLC-beta3PTX-sensitive G proteinsG proteinsFMet-LeuGbetagamma subunitsCOS-7 cellsPhospholipase CPLC-beta2Receptor-mediated PLC activationPTX-sensitive mannerFMLP-mediated activationPertussis toxinPhe receptorCell activationGi proteinsChemoattractant receptorsReceptorsPLC activationC5aBeta2Gq classActivationBeta3Betagamma subunitsSignal transduction pathways