2022
Mitochondrial dysfunction induces ALK5-SMAD2-mediated hypovascularization and arteriovenous malformations in mouse retinas
Zhang H, Li B, Huang Q, López-Giráldez F, Tanaka Y, Lin Q, Mehta S, Wang G, Graham M, Liu X, Park I, Eichmann A, Min W, Zhou J. Mitochondrial dysfunction induces ALK5-SMAD2-mediated hypovascularization and arteriovenous malformations in mouse retinas. Nature Communications 2022, 13: 7637. PMID: 36496409, PMCID: PMC9741628, DOI: 10.1038/s41467-022-35262-w.Peer-Reviewed Original ResearchConceptsMitochondrial dysfunctionThioredoxin 2Single-cell RNA-seq analysisRNA-seq analysisMutant miceNuclear genesMitochondrial proteinsMitochondrial localizationHuman retinal diseasesTranscriptional factorsGene expressionMutant retinasMitochondrial activityExtracellular matrixNovel mechanismVascular maturationArteriovenous malformationsGenetic deficiencyVessel growthSmad2Mouse retinaVascular malformationsMechanistic studiesBasement membraneRetinal vascular malformations
2019
Nuclear localization of the tyrosine kinase BMX mediates VEGFR2 expression
Liu T, Li Y, Su H, Zhang H, Jones D, Zhou HJ, Ji W, Min W. Nuclear localization of the tyrosine kinase BMX mediates VEGFR2 expression. Journal Of Cellular And Molecular Medicine 2019, 24: 126-138. PMID: 31642192, PMCID: PMC6933376, DOI: 10.1111/jcmm.14663.Peer-Reviewed Original ResearchConceptsTyrosine kinase BMXVEGFR2 promoter activityPromoter activityNuclear localizationVEGFR2 promoterKinase-inactive formGene promoter activityEndothelial cellsNucleus of ECsVascular endothelial growth factor receptorSiRNA-mediated silencingAngiogenesis-related diseasesChromatin immunoprecipitationDirect transactivationSH3 domainTranscription factorsGrowth factor receptorVEGFR2 expressionNovel functionVEGFR2 transcriptionSp1Human endothelial cellsLuciferase assayEC migrationFactor receptor
2010
Functional Analyses of the Bone Marrow Kinase in the X Chromosome in Vascular Endothelial Growth Factor–Induced Lymphangiogenesis
Jones D, Xu Z, Zhang H, He Y, Kluger MS, Chen H, Min W. Functional Analyses of the Bone Marrow Kinase in the X Chromosome in Vascular Endothelial Growth Factor–Induced Lymphangiogenesis. Arteriosclerosis Thrombosis And Vascular Biology 2010, 30: 2553-2561. PMID: 20864667, PMCID: PMC3106279, DOI: 10.1161/atvbaha.110.214999.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCells, CulturedCorneaEndothelial CellsFemaleHumansLymphangiogenesisLymphatic VesselsMaleMiceMice, Inbred C57BLMice, KnockoutPhosphorylationProtein-Tyrosine KinasesRecombinant ProteinsRNA InterferenceSignal TransductionSkinTransfectionVascular Endothelial Growth Factor AVascular Endothelial Growth Factor CVascular Endothelial Growth Factor Receptor-2Vascular Endothelial Growth Factor Receptor-3ConceptsBone marrow kinaseX chromosomeLymphatic endothelial cell tube formationVascular endothelial growth factorVEGFR-3 receptorRole of BmxLymphatic endothelial cellsEndothelial cell tube formationVEGFR-2 activationCell tube formationLymphangiogenic signalingReceptor autophosphorylationFunctional analysisLymphangiogenic responseFirst insightPathological angiogenesisWild-type micePharmacological inhibitionTube formationBMXChromosomesKinaseVEGFR-3Critical roleSignaling
2009
JAK2 and SHP2 Reciprocally Regulate Tyrosine Phosphorylation and Stability of Proapoptotic Protein ASK1*
Yu L, Min W, He Y, Qin L, Zhang H, Bennett AM, Chen H. JAK2 and SHP2 Reciprocally Regulate Tyrosine Phosphorylation and Stability of Proapoptotic Protein ASK1*. Journal Of Biological Chemistry 2009, 284: 13481-13488. PMID: 19287004, PMCID: PMC2679448, DOI: 10.1074/jbc.m809740200.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsApoptosisCell LineEndothelial CellsEnzyme StabilityHumansInterferon-gammaJanus Kinase 2MAP Kinase Kinase Kinase 5MiceMice, KnockoutMultienzyme ComplexesMutationPhosphorylationProtein Tyrosine Phosphatase, Non-Receptor Type 11Signal TransductionSuppressor of Cytokine Signaling 1 ProteinSuppressor of Cytokine Signaling ProteinsTumor Necrosis Factor-alphaConceptsTyrosine phosphorylationSubstrate-trapping mutantProtein tyrosine phosphatase 2Phosphatase-inactive mutantProteasomal inhibitor MG132ASK1-JNK signalingEndothelial cellsJAK2-specific inhibitorIFN-gamma-induced tyrosine phosphorylationASK1 degradationASK1 dephosphorylationInactive mutantMouse endothelial cellsASK1 phosphorylationPhosphatase 2Inhibitor MG132SHP2Wild typeASK1DephosphorylationMutantsPhosphorylationEnhanced associationJAK2EC apoptosis
2008
AIP1 Recruits Phosphatase PP2A to ASK1 in Tumor Necrosis Factor–Induced ASK1-JNK Activation
Min W, Lin Y, Tang S, Yu L, Zhang H, Wan T, Luhn T, Fu H, Chen H. AIP1 Recruits Phosphatase PP2A to ASK1 in Tumor Necrosis Factor–Induced ASK1-JNK Activation. Circulation Research 2008, 102: 840-848. PMID: 18292600, DOI: 10.1161/circresaha.107.168153.Peer-Reviewed Original ResearchConceptsASK1-JNK signalingASK1 dephosphorylationAssociation of PP2APP2A catalytic subunitCatalytic inactive formPP2A inhibitor okadaicASK1-JNK activationC-Jun N-terminal kinaseActivation of JNKEndothelial cellsN-terminal kinasePhosphatase PP2ACritical rolePotential phosphataseProtein phosphataseGAP domainInhibitor okadaicProtein familyCatalytic subunitC2 domainPP2AAIP1Novel memberApoptotic signalingRNA knockdown
2007
Structural and Functional Characterization of the Human Protein Kinase ASK1
Bunkoczi G, Salah E, Filippakopoulos P, Fedorov O, Müller S, Sobott F, Parker SA, Zhang H, Min W, Turk BE, Knapp S. Structural and Functional Characterization of the Human Protein Kinase ASK1. Structure 2007, 15: 1215-1226. PMID: 17937911, PMCID: PMC2100151, DOI: 10.1016/j.str.2007.08.011.Peer-Reviewed Original ResearchConceptsApoptosis signal-regulating kinase 1Autophosphorylation sitesSignal-regulated kinases 1ASK1 kinase activityVitro autophosphorylation sitesAnalytical ultracentrifugationHigh-resolution structuresATP-mimetic inhibitorSite-directed mutantsReporter gene assayPhosphorylation motifsPhosphorylation sitesCatalytic domainFunctional characterizationKinase activityRegulatory mechanismsKinase 1Tight dimerMimetic inhibitorsGene assayEssential roleSelective inhibitorTail fashionCrystallographic analysisMass spectrometryRIP1-mediated AIP1 Phosphorylation at a 14-3-3-binding Site Is Critical for Tumor Necrosis Factor-induced ASK1-JNK/p38 Activation*
Zhang R, Zhang H, Lin Y, Li J, Pober JS, Min W. RIP1-mediated AIP1 Phosphorylation at a 14-3-3-binding Site Is Critical for Tumor Necrosis Factor-induced ASK1-JNK/p38 Activation*. Journal Of Biological Chemistry 2007, 282: 14788-14796. PMID: 17389591, DOI: 10.1074/jbc.m701148200.Peer-Reviewed Original ResearchMeSH Keywords14-3-3 ProteinsAdaptor Proteins, Signal TransducingAmino Acid SubstitutionAnimalsApoptosisCarrier ProteinsCattleCells, CulturedEndothelial CellsEnzyme ActivationGuanylate KinasesHumansMAP Kinase Kinase 4MAP Kinase Kinase Kinase 5MAP Kinase Signaling SystemMultiprotein ComplexesMutation, MissenseP38 Mitogen-Activated Protein KinasesPhosphorylationProtein BindingProtein Processing, Post-TranslationalProteinsReceptor-Interacting Protein Serine-Threonine KinasesTNF Receptor-Associated Factor 2Tumor Necrosis Factor-alphaConceptsJNK/p38 activationP38 activationTRAF2-ASK1ASK1-JNK activationPhospho-specific antibodiesTNF treatmentEndothelial cellsComplex formationGAP domainProtein familyTerminal domainAIP1Novel memberApoptotic signalingTNF signalingRNA knockdownRIP1PhosphorylationProtein 1ASK1-interacting protein-1EC apoptosisTRAF2ASK1Similar kineticsTumor necrosis factor