2024
Native architecture of a human GBP1 defense complex for cell-autonomous immunity to infection
Zhu S, Bradfield C, Maminska A, Park E, Kim B, Kumar P, Huang S, Kim M, Zhang Y, Bewersdorf J, MacMicking J. Native architecture of a human GBP1 defense complex for cell-autonomous immunity to infection. Science 2024, 383: eabm9903. PMID: 38422126, DOI: 10.1126/science.abm9903.Peer-Reviewed Original ResearchConceptsGuanylate-binding proteinsCaspase-4Surface of Gram-negative bacteriaGuanosine triphosphate hydrolysisImmunity to infectionInnate immunity to infectionCryo-electron tomographyGram-negative bacteriaImmunity proteinSignaling platformsMembrane insertionHuman cellsNative structureCombat infectionsLipopolysaccharide releaseGasdermin DExtended conformationLiving organismsProteinDefense complexCellsNative architectureGBP1BacteriaInfection
2023
PLSCR1 is a cell-autonomous defence factor against SARS-CoV-2 infection
Xu D, Jiang W, Wu L, Gaudet R, Park E, Su M, Cheppali S, Cheemarla N, Kumar P, Uchil P, Grover J, Foxman E, Brown C, Stansfeld P, Bewersdorf J, Mothes W, Karatekin E, Wilen C, MacMicking J. PLSCR1 is a cell-autonomous defence factor against SARS-CoV-2 infection. Nature 2023, 619: 819-827. PMID: 37438530, PMCID: PMC10371867, DOI: 10.1038/s41586-023-06322-y.Peer-Reviewed Original ResearchConceptsC-terminal β-barrel domainSpike-mediated fusionCell-autonomous defenseLarge-scale exome sequencingΒ-barrel domainGenome-wide CRISPRSARS-CoV-2 infectionHost cell cytosolScramblase activityPhospholipid scramblaseLive SARS-CoV-2 infectionHuman lung epitheliumPLSCR1SARS-CoV-2 USASingle-molecule switchingSARS-CoV-2 variantsExome sequencingHuman populationRestriction factorsViral RNANew SARS-CoV-2 variantsSARS-CoV-2Robust activityLung epitheliumDefense factors
2021
Selenoprotein W ensures physiological bone remodeling by preventing hyperactivity of osteoclasts
Kim H, Lee K, Kim J, Kim M, Kim J, Lee H, Chung Y, Shin H, Kim T, Park E, Rho J, Lee S, Kim N, Lee S, Choi Y, Jeong D. Selenoprotein W ensures physiological bone remodeling by preventing hyperactivity of osteoclasts. Nature Communications 2021, 12: 2258. PMID: 33859201, PMCID: PMC8050258, DOI: 10.1038/s41467-021-22565-7.Peer-Reviewed Original ResearchConceptsSelenoprotein WCell-cell fusionRNA sequencing analysisProfile of receptor activationOsteoclast differentiationNuclear factor of activated T cells cytoplasmic 1Bone remodelingBone mass phenotypeOsteoclastogenesis in vitroNuclear translocation of NF-kBTranslocation of NF-kBPhysiological bone remodelingBlocks osteoporosisNuclear translocationNuclear factorOsteoclastogenic genesMechanism of actionMass phenotypeBone metabolismBone resorptionReceptor activationOsteoclast maturationCytoplasmic 1Osteoclast formationNF-kB
2020
Guanylate-binding proteins convert cytosolic bacteria into caspase-4 signaling platforms
Wandel MP, Kim BH, Park ES, Boyle KB, Nayak K, Lagrange B, Herod A, Henry T, Zilbauer M, Rohde J, MacMicking JD, Randow F. Guanylate-binding proteins convert cytosolic bacteria into caspase-4 signaling platforms. Nature Immunology 2020, 21: 880-891. PMID: 32541830, PMCID: PMC7381384, DOI: 10.1038/s41590-020-0697-2.Peer-Reviewed Original ResearchConceptsGuanylate-binding proteinsCaspase-4 activationCaspase-4Human caspase-4Pyroptotic cell deathGram-negative bacteriaCytosolic bacteriaReplicative nicheEvolutionary evidenceIntracellular bacteriaCell deathMultiple antagonistsNeighboring cellsCaspase-11BacteriaAntibacterial defenseBacterial challengeGasderminShigella flexneriProteinDependent pyroptosisActivationPathwayBacterial lipopolysaccharideGBP2
2019
TDAG51 is a crucial regulator of maternal care and depressive-like behavior after parturition
Yun H, Park E, Choi S, Shin B, Yu J, Yu J, Amarasekara D, Kim S, Lee N, Choi J, Choi Y, Rho J. TDAG51 is a crucial regulator of maternal care and depressive-like behavior after parturition. PLOS Genetics 2019, 15: e1008214. PMID: 31251738, PMCID: PMC6599150, DOI: 10.1371/journal.pgen.1008214.Peer-Reviewed Original ResearchConceptsDepressive-like behaviorPostpartum depressionDevelopment of postpartum depressionImpaired maternal behaviorRegulation of maternal careMonoamine neurotransmitter levelsCombination of physical changesNest-building testInfluence of genetic risk factorsTDAG51 deficiencyMaternity careGenetic risk factorsPup retrievalMental disordersPsychiatric illnessNeurotransmitter levelsMaternal behaviorPostpartumRisk factorsDepressionBuilding testsT-cell death-associated geneDeath-associated genesNursesCareInterferon-induced guanylate-binding proteins: Guardians of host defense in health and disease
Tretina K, Park ES, Maminska A, MacMicking JD. Interferon-induced guanylate-binding proteins: Guardians of host defense in health and disease. Journal Of Experimental Medicine 2019, 216: 482-500. PMID: 30755454, PMCID: PMC6400534, DOI: 10.1084/jem.20182031.Peer-Reviewed Original ResearchConceptsGuanylate-binding proteinsNumerous host cell typesHost cell typesImportant human diseasesCritical rheostatBasic biologyMicrobial pathogensHost defense activitiesHuman diseasesSimilar functionsCell typesHomeostatic settingsGTPasesInnate immunityDefense activitiesHost defenseInflammatory syndromeNeoplastic diseaseClinical approachTissue damageBacterial infectionsCentral orchestratorDiseaseIFNRheostat
2016
Porcine amino peptidase N domain VII has critical role in binding and entry of porcine epidemic diarrhea virus
Kamau A, Park J, Park E, Yu J, Rho J, Shin H. Porcine amino peptidase N domain VII has critical role in binding and entry of porcine epidemic diarrhea virus. Virus Research 2016, 227: 150-157. PMID: 27732876, PMCID: PMC7114530, DOI: 10.1016/j.virusres.2016.10.004.Peer-Reviewed Original ResearchConceptsPorcine aminopeptidase NPorcine epidemic diarrhea virusNIH3T3 cellsDomain VIIDiarrhea virusPorcine epidemic diarrhea virus infectionDeletion mutantsMutantsEnteric diseaseDomain IIIIntestinal cellsVero cellsAminopeptidase NTime course testIndirect plaquesTherapeutic developmentCellsBindingPorcineVirusInteraction of Tumor Necrosis Factor Receptor-associated Factor 6 (TRAF6) and Vav3 in the Receptor Activator of Nuclear Factor κB (RANK) Signaling Complex Enhances Osteoclastogenesis*
Yu J, Yun H, Shin B, Kim Y, Park E, Choi S, Yu J, Amarasekara D, Kim S, Inoue J, Walsh M, Choi Y, Takami M, Rho J. Interaction of Tumor Necrosis Factor Receptor-associated Factor 6 (TRAF6) and Vav3 in the Receptor Activator of Nuclear Factor κB (RANK) Signaling Complex Enhances Osteoclastogenesis*. Journal Of Biological Chemistry 2016, 291: 20643-20660. PMID: 27507811, PMCID: PMC5034056, DOI: 10.1074/jbc.m116.728303.Peer-Reviewed Original ResearchConceptsTNF receptor-associated factor 6Signaling complexIVVY motifCross-talkDbl homology domainCoiled-coil domainFactor 6RANK-mediated osteoclastogenesisTRAF6-binding siteFunctional cross-talkUbiquitin pathwayBinding partnersCytoplasmic tailTumor necrosis factor receptor-associated factor 6Activation of nuclear factor-kBInteraction partnersNuclear factor-kBProteomic approachVav3Signaling cascadesFunctional importanceMotifCooperative signalingMutantsInteraction of tumor necrosis factor receptor-associated factor 6Interferon-induced guanylate-binding proteins in inflammasome activation and host defense
Kim BH, Chee JD, Bradfield CJ, Park ES, Kumar P, MacMicking JD. Interferon-induced guanylate-binding proteins in inflammasome activation and host defense. Nature Immunology 2016, 17: 481-489. PMID: 27092805, PMCID: PMC4961213, DOI: 10.1038/ni.3440.Peer-Reviewed Original Research
2015
Tumor Necrosis Factor (TNF) Receptor-associated Factor (TRAF)-interacting Protein (TRIP) Negatively Regulates the TRAF2 Ubiquitin-dependent Pathway by Suppressing the TRAF2-Sphingosine 1-Phosphate (S1P) Interaction*
Park E, Choi S, Shin B, Yu J, Yu J, Hwang J, Yun H, Chung Y, Choi J, Choi Y, Rho J. Tumor Necrosis Factor (TNF) Receptor-associated Factor (TRAF)-interacting Protein (TRIP) Negatively Regulates the TRAF2 Ubiquitin-dependent Pathway by Suppressing the TRAF2-Sphingosine 1-Phosphate (S1P) Interaction*. Journal Of Biological Chemistry 2015, 290: 9660-9673. PMID: 25716317, PMCID: PMC4392267, DOI: 10.1074/jbc.m114.609685.Peer-Reviewed Original ResearchMeSH KeywordsBinding SitesCytokinesGene ExpressionHEK293 CellsHeLa CellsHumansImmunoblottingLysineLysophospholipidsNF-kappa BProtein BindingReverse Transcriptase Polymerase Chain ReactionRNA InterferenceSignal TransductionSphingosineTNF Receptor-Associated Factor 2Tumor Necrosis Factor Receptor-Associated Peptides and ProteinsTumor Necrosis Factor-alphaUbiquitinUbiquitinationConceptsTRAF-interacting proteinTNFR-associated factor 2TNF-induced inflammatory responseE3 ubiquitin (Ub) ligase activityTNF receptor signaling complexE3 Ub ligasesUbiquitin-dependent pathwayCellular binding partnersMitogen-activated protein kinase activationNF-kB activationNegative regulator of proinflammatory cytokine productionProtein kinase activityDownstream signaling cascadesCell proliferationTNF receptorsUb ligasesTNFR signaling pathwayDown-regulation of proinflammatory cytokine productionLigase activityRING domainTumor necrosis factorProinflammatory cytokine productionAdaptor moleculeCellular processesRegulation of proinflammatory cytokine production
2012
D-chiro-inositol Negatively Regulates the Formation of Multinucleated Osteoclasts by Down-Regulating NFATc1
Yu J, Choi S, Park E, Shin B, Yu J, Lee S, Takami M, Kang J, Meong H, Rho J. D-chiro-inositol Negatively Regulates the Formation of Multinucleated Osteoclasts by Down-Regulating NFATc1. Journal Of Clinical Immunology 2012, 32: 1360-1371. PMID: 22711011, DOI: 10.1007/s10875-012-9722-z.Peer-Reviewed Original ResearchConceptsTartrate-resistant acid phosphataseEffect of D-chiro-inositolOC differentiationD-chiro-inositolExpression of OC marker genesNuclear factor of activated T cells c1Inflammatory bone lossCell-cell fusionAccelerated bone destructionDose-dependent mannerExpression of NFATc1Formation of multinucleated osteoclastsBone-related diseasesMultinucleated giant cellsSecondary osteoporosisCell fusion assayOsteoclastogenic genesBone destructionBone lossDiabetes mellitusOC precursorsGiant cellsOC formationMultinucleated osteoclastsNFATc1
2009
Protein arginine methyltransferase 1 regulates herpes simplex virus replication through ICP27 RGG-box methylation
Yu J, Shin B, Park E, Yang S, Choi S, Kang M, Rho J. Protein arginine methyltransferase 1 regulates herpes simplex virus replication through ICP27 RGG-box methylation. Biochemical And Biophysical Research Communications 2009, 391: 322-328. PMID: 19913501, DOI: 10.1016/j.bbrc.2009.11.057.Peer-Reviewed Original ResearchConceptsProtein arginine methyltransferase 1ICP27 RGG boxProtein arginine methylationArginine methylationRGG boxHerpes simplex virus type 1Arginine residuesRNA-binding activityArginine substitution mutantsArginine methyltransferase 1Gene expression in vivoRNA metabolismMethylation sitesSubcellular localizationSubstitution mutantsCellular processesCellular regulationExpression in vivoHerpes simplex virus replicationArginine mutationPRMT inhibitorsICP27Methyltransferase 1Cytokine signalingCellular mediators