2009
AIP1 Functions as Arf6-GAP to Negatively Regulate TLR4 Signaling2
Wan T, Liu T, Zhang H, Tang S, Min W. AIP1 Functions as Arf6-GAP to Negatively Regulate TLR4 Signaling2. Journal Of Biological Chemistry 2009, 285: 3750-3757. PMID: 19948740, PMCID: PMC2823516, DOI: 10.1074/jbc.m109.069385.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Proteins, Signal TransducingADP-Ribosylation Factor 6ADP-Ribosylation FactorsAmino Acid SequenceAnimalsCarrier ProteinsCattleCell LineCells, CulturedChlorocebus aethiopsCOS CellsGTPase-Activating ProteinsGuanylate KinasesHumansImmunoblottingLipopolysaccharidesMembrane GlycoproteinsMiceMice, KnockoutMitogen-Activated Protein KinasesMolecular Sequence DataMyeloid Differentiation Factor 88NF-kappa BPhosphatidylinositol 4,5-DiphosphateProtein BindingReceptors, Interleukin-1Sequence Homology, Amino AcidToll-Like Receptor 4TransfectionConceptsGTPase-activating proteinsArf6 GAPAIP1 functionsNovel GTPase-activating proteinInhibition of ARF6Pleckstrin homologyGAP domainAdaptor proteinSmall GTPaseDisrupts formationPlasma membraneAIP1MAPK pathwayLipid precursorsToll-like receptor 4Arf6NF-kappaBComplex componentsToll-like receptorsProteinRich sitesGTPaseHomologyComplexesCells increases
2008
AIP1 functions as an endogenous inhibitor of VEGFR2-mediated signaling and inflammatory angiogenesis in mice
Zhang H, He Y, Dai S, Xu Z, Luo Y, Wan T, Luo D, Jones D, Tang S, Chen H, Sessa WC, Min W. AIP1 functions as an endogenous inhibitor of VEGFR2-mediated signaling and inflammatory angiogenesis in mice. Journal Of Clinical Investigation 2008, 118: 3904-3916. PMID: 19033661, PMCID: PMC2575835, DOI: 10.1172/jci36168.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCattleCell MovementCorneal NeovascularizationDisease Models, AnimalEndothelial CellsHumansInflammationMiceMice, KnockoutNeovascularization, PathologicOrgan SpecificityPhosphatidylinositol 3-KinasesRas GTPase-Activating ProteinsSignal TransductionVascular Endothelial Growth Factor AVascular Endothelial Growth Factor Receptor-2ConceptsASK1-interacting protein-1Inflammatory angiogenesisKO miceEndogenous inhibitorInhibition of VEGFR2PI3K p85Retina neovascularizationAdaptive angiogenesisVEGF-VEGFR2 signalingRetinal angiogenesisEC migrationMiceVascular ECsVEGF responseAngiogenesisProtein 1EC apoptosisVEGFR2Late phaseVEGFMechanistic dataVascular developmentAIP1 functionsK-complexesInhibitorsAIP1 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 knockdownAIP1 Is Critical in Transducing IRE1-mediated Endoplasmic Reticulum Stress Response*
Luo D, He Y, Zhang H, Yu L, Chen H, Xu Z, Tang S, Urano F, Min W. AIP1 Is Critical in Transducing IRE1-mediated Endoplasmic Reticulum Stress Response*. Journal Of Biological Chemistry 2008, 283: 11905-11912. PMID: 18281285, PMCID: PMC2335342, DOI: 10.1074/jbc.m710557200.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsApoptosisCattleDimerizationDNA-Binding ProteinsEndoplasmic ReticulumEndothelial CellsEnzyme ActivationHumansJNK Mitogen-Activated Protein KinasesMAP Kinase Kinase Kinase 5Membrane ProteinsMiceMice, KnockoutProtein BindingProtein Serine-Threonine KinasesProtein Structure, TertiaryRas GTPase-Activating ProteinsRegulatory Factor X Transcription FactorsSignal TransductionTranscription FactorsX-Box Binding Protein 1ConceptsASK1-interacting protein-1SENP1 mediates TNF-induced desumoylation and cytoplasmic translocation of HIPK1 to enhance ASK1-dependent apoptosis
Li X, Luo Y, Yu L, Lin Y, Luo D, Zhang H, He Y, Kim YO, Kim Y, Tang S, Min W. SENP1 mediates TNF-induced desumoylation and cytoplasmic translocation of HIPK1 to enhance ASK1-dependent apoptosis. Cell Death & Differentiation 2008, 15: 739-750. PMID: 18219322, DOI: 10.1038/sj.cdd.4402303.Peer-Reviewed Original ResearchMeSH KeywordsAcetylcysteineAnimalsAntioxidantsApoptosisCarrier ProteinsCattleCells, CulturedCysteine EndopeptidasesCytoplasmEndopeptidasesEndothelial CellsFibroblastsHumansMAP Kinase Kinase Kinase 5MiceMice, KnockoutMutationProtein KinasesProtein Processing, Post-TranslationalProtein Serine-Threonine KinasesProtein TransportReactive Oxygen SpeciesRecombinant ProteinsRNA InterferenceRNA, Small InterferingSignal TransductionSmall Ubiquitin-Related Modifier ProteinsThioredoxinsTime FactorsTransfectionTumor Necrosis Factor-alphaConceptsASK1-dependent apoptosisASK1-JNK activationCytoplasmic translocationMouse embryonic fibroblast cellsNuclear translocationSUMO-specific proteasesWild-type formEmbryonic fibroblast cellsNuclear importAntioxidant protein thioredoxinHIPK1Mutant formsEndothelial cellsDeSUMOylationProtein thioredoxinSubsequent cytoplasmic translocationSENP1TranslocationCritical functionsThioredoxinFibroblast cellsApoptosisCellsActivationSUMO
2007
RIP1-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
2006
Differential Functions of Tumor Necrosis Factor Receptor 1 and 2 Signaling in Ischemia-Mediated Arteriogenesis and Angiogenesis
Luo D, Luo Y, He Y, Zhang H, Zhang R, Li X, Dobrucki WL, Sinusas AJ, Sessa WC, Min W. Differential Functions of Tumor Necrosis Factor Receptor 1 and 2 Signaling in Ischemia-Mediated Arteriogenesis and Angiogenesis. American Journal Of Pathology 2006, 169: 1886-1898. PMID: 17071609, PMCID: PMC1780200, DOI: 10.2353/ajpath.2006.060603.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsArteriesBlood VesselsCattleCell MovementCell ProliferationCell SurvivalEndothelial CellsEndothelium, VascularHindlimbHumansIschemiaMiceMice, Inbred C57BLMice, KnockoutMolecular Sequence DataNeovascularization, PathologicOrganogenesisPerfusionProtein-Tyrosine KinasesReceptors, Tumor Necrosis Factor, Type IReceptors, Tumor Necrosis Factor, Type IISignal TransductionTNF Receptor-Associated Factor 2ConceptsTNFR2 KO miceTumor necrosis factorTNFR1-KOEndothelial cellsFemoral artery ligation modelIschemia-mediated arteriogenesisIschemic reserve capacityTNFR1 knockout miceInfiltration of macrophagesTumor necrosis factor receptor 1Wild-type miceArtery ligation modelNecrosis factor receptor 1Dependent reporter gene expressionNuclear factor-kappaBEC survivalFactor receptor 1Vascular endothelial cellsActivation of TNFR1Murine endothelial cellsTNFR2-KOClinical recoveryActivation of TNFR2Limb perfusionVascular proliferationSOCS1 Inhibits Tumor Necrosis Factor-induced Activation of ASK1-JNK Inflammatory Signaling by Mediating ASK1 Degradation*
He Y, Zhang W, Zhang R, Zhang H, Min W. SOCS1 Inhibits Tumor Necrosis Factor-induced Activation of ASK1-JNK Inflammatory Signaling by Mediating ASK1 Degradation*. Journal Of Biological Chemistry 2006, 281: 5559-5566. PMID: 16407264, DOI: 10.1074/jbc.m512338200.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCattleCells, CulturedEndothelial CellsEnzyme ActivationInflammationIntracellular Signaling Peptides and ProteinsJNK Mitogen-Activated Protein KinasesMAP Kinase Kinase Kinase 5MiceMice, KnockoutRecombinant Fusion ProteinsRepressor ProteinsSignal TransductionSrc Homology DomainsSuppressor of Cytokine Signaling 1 ProteinSuppressor of Cytokine Signaling 3 ProteinSuppressor of Cytokine Signaling ProteinsTumor Necrosis Factor-alphaConceptsASK1 degradationDissociation of ASK1Member of suppressorTumor necrosis factor-induced activationEndothelial cellsActivation of JNKPhosphotyrosine bindingUndergoes ubiquitinationSH2 domainProteasomal inhibitorsASK1 activationNegative regulatorApoptotic responseASK1Cytokine signalingSOCS1 functionsASK1 expressionSOCS1Tumor necrosis factorSignalingSOCS1-deficient mice
2004
AIP1/DAB2IP, a Novel Member of the Ras-GAP Family, Transduces TRAF2-induced ASK1-JNK Activation*
Zhang H, Zhang R, Luo Y, D'Alessio A, Pober JS, Min W. AIP1/DAB2IP, a Novel Member of the Ras-GAP Family, Transduces TRAF2-induced ASK1-JNK Activation*. Journal Of Biological Chemistry 2004, 279: 44955-44965. PMID: 15310755, DOI: 10.1074/jbc.m407617200.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Proteins, Signal TransducingAnimalsCarrier ProteinsCattleCell LineCell MembraneCytoplasmGene DeletionGenes, ReporterGuanylate KinasesHumansImmunoblottingImmunoprecipitationJNK Mitogen-Activated Protein KinasesMAP Kinase Kinase 4MAP Kinase Kinase Kinase 5Microscopy, ConfocalMicroscopy, FluorescenceMitogen-Activated Protein Kinase KinasesModels, BiologicalMutationNF-kappa BProlineProtein Structure, TertiaryProtein TransportProteinsRas GTPase-Activating ProteinsSignal TransductionTNF Receptor-Associated Factor 2Transfection