2021
ATPIF1 maintains normal mitochondrial structure which is impaired by CCM3 deficiency in endothelial cells
Wang K, Chen H, Zhou Z, Zhang H, Zhou HJ, Min W. ATPIF1 maintains normal mitochondrial structure which is impaired by CCM3 deficiency in endothelial cells. Cell & Bioscience 2021, 11: 11. PMID: 33422124, PMCID: PMC7796565, DOI: 10.1186/s13578-020-00514-z.Peer-Reviewed Original ResearchActivation of mitophagyHuman umbilical vein endothelial cellsNormal mitochondrial structureMorphology of mitochondriaRNA-seq screeningMitochondrial membrane potentialCRISPR-Cas9 SystemCerebral cavernous malformationsEndothelial cellsExpression of KLF4Destruction of mitochondriaUmbilical vein endothelial cellsMitochondrial structureSignaling pathwaysVein endothelial cellsMitochondriaATPIF1MitophagyEndothelial progenitor cellsProgenitor cellsCell proliferationMembrane potentialKLF4PathwayProtein
2019
A Unique SUMO-Interacting Motif of Trx2 Is Critical for Its Mitochondrial Presequence Processing and Anti-oxidant Activity
Chen C, Wang K, Zhang H, Zhou HJ, Chen Y, Min W. A Unique SUMO-Interacting Motif of Trx2 Is Critical for Its Mitochondrial Presequence Processing and Anti-oxidant Activity. Frontiers In Physiology 2019, 10: 1089. PMID: 31555141, PMCID: PMC6727865, DOI: 10.3389/fphys.2019.01089.Peer-Reviewed Original ResearchSUMO-interacting motifMitochondrial processing peptidaseReactive oxygen speciesMitochondrial intermediate peptidaseStress-induced cellular senescenceOxidative stress-induced cellular senescenceMitochondrial redox proteinsMitochondrial thioredoxin 2Excess reactive oxygen speciesMitochondrial processingPresequence processingProcessing peptidaseTrx2 proteinMitochondrial targetingMassive reactive oxygen speciesAntisenescence activityCellular senescenceThioredoxin 2Chemical inhibitionMature formRedox proteinsUnprocessed formProteinTrx2Catalytic site
2010
Crystal Structure of CCM3, a Cerebral Cavernous Malformation Protein Critical for Vascular Integrity*
Li X, Zhang R, Zhang H, He Y, Ji W, Min W, Boggon TJ. Crystal Structure of CCM3, a Cerebral Cavernous Malformation Protein Critical for Vascular Integrity*. Journal Of Biological Chemistry 2010, 285: 24099-24107. PMID: 20489202, PMCID: PMC2911348, DOI: 10.1074/jbc.m110.128470.Peer-Reviewed Original ResearchMeSH KeywordsApoptosis Regulatory ProteinsBinding, CompetitiveBrainCrystallography, X-RayDimerizationHemangioma, Cavernous, Central Nervous SystemHumansKineticsMembrane ProteinsMolecular ConformationMutationPaxillinProtein ConformationProtein FoldingProtein Structure, SecondaryProtein Structure, TertiaryProto-Oncogene ProteinsConceptsN-terminal dimerization domainPaxillin LD motifsCerebral cavernous malformationsAlpha-helical proteinsLD motifsCCM complexHomology domainFocal adhesionsDimerization domainMolecular basisHydrophobic pocketHuman populationCCM3 mutationsMutationsCCM3Crystal structureVascular integrityCCM2DomainPaxillinProteinMotifCCM1InteractionCellsSENP1-mediated GATA1 deSUMOylation is critical for definitive erythropoiesis
Yu L, Ji W, Zhang H, Renda MJ, He Y, Lin S, Cheng EC, Chen H, Krause DS, Min W. SENP1-mediated GATA1 deSUMOylation is critical for definitive erythropoiesis. Journal Of Experimental Medicine 2010, 207: 1183-1195. PMID: 20457756, PMCID: PMC2882842, DOI: 10.1084/jem.20092215.Peer-Reviewed Original ResearchConceptsSmall ubiquitin-like modifier (SUMO) modificationImportant regulatory mechanismEmbryonic day 13.5Down-regulation correlatesFetal liverCre-loxP systemEmbryonic lethalityProtein functionDefinitive erythropoiesisGene promoterDNA bindingRegulatory mechanismsGene expressionGATA1SENP1Fetal liver cellsProtein analysisDay 13.5Global deletionProteinSubsequent erythropoiesisKnockout miceErythropoiesisLiver cellsDeSUMOylation
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