1999
TNF recruits TRADD to the plasma membrane but not the trans-Golgi network, the principal subcellular location of TNF-R1.
Jones S, Ledgerwood E, Prins J, Galbraith J, Johnson D, Pober J, Bradley J. TNF recruits TRADD to the plasma membrane but not the trans-Golgi network, the principal subcellular location of TNF-R1. The Journal Of Immunology 1999, 162: 1042-8. PMID: 9916731, DOI: 10.4049/jimmunol.162.2.1042.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAntigens, CDAortaBrefeldin ACattleCell CompartmentationCell Line, TransformedCell MembraneEndothelium, VascularGolgi ApparatusHumansMicroscopy, ConfocalProteinsReceptors, Tumor Necrosis FactorReceptors, Tumor Necrosis Factor, Type ISubcellular FractionsTNF Receptor-Associated Factor 1TransfectionTumor Necrosis Factor-alphaU937 CellsConceptsTrans-Golgi networkPlasma membraneTNF-R1Golgi regionConfocal immunofluorescence microscopyHuman endothelial cell line ECV304Endothelial cell line ECV304Receptor-mediated endocytosisAdaptor proteinSubcellular localizationSubcellular locationCell fractionationBovine aortic endothelial cellsCoimmunoprecipitation studiesEndothelial cellsTRADDCell line U937Golgi apparatusSubcellular interactionsWestern blot analysisCell extractsMonocyte cell line U937Expression plasmidGolgiImmunofluorescence microscopy
1998
The N-terminal domains target TNF receptor-associated factor-2 to the nucleus and display transcriptional regulatory activity.
Min W, Bradley JR, Galbraith JJ, Jones SJ, Ledgerwood EC, Pober JS. The N-terminal domains target TNF receptor-associated factor-2 to the nucleus and display transcriptional regulatory activity. The Journal Of Immunology 1998, 161: 319-24. PMID: 9647239, DOI: 10.4049/jimmunol.161.1.319.Peer-Reviewed Original ResearchMeSH KeywordsBiological TransportCell NucleusCells, CulturedCytoplasmEndothelium, VascularFluorescent Antibody Technique, IndirectHumansPeptide FragmentsProtein BiosynthesisProtein Structure, TertiaryProteinsReceptors, Tumor Necrosis FactorTNF Receptor-Associated Factor 2Transcription, GeneticTransfectionUmbilical VeinsConceptsFinger domainAmino-terminal RING finger domainNuclear localizationTNF receptor-associated factor 2Cytoplasmic signal transductionReceptor-associated factor 2Zinc finger domainTranscriptional regulatory activityAmino-terminal halfC-Jun N-terminal kinase (JNK) activationRING finger domainProminent nuclear localizationConfocal immunofluorescence microscopyWestern blottingTRAF2 moleculeAdaptor proteinDeletion mutantsSignal transductionSubcellular localizationGene transcriptionKinase activationHuman endothelial cellsTRAF2 proteinCell extractsHuman endothelial cell line
1996
"Cytosolic" phospholipase A2 is in the nucleus of subconfluent endothelial cells but confined to the cytoplasm of confluent endothelial cells and redistributes to the nuclear envelope and cell junctions upon histamine stimulation.
Sierra-Honigmann MR, Bradley JR, Pober JS. "Cytosolic" phospholipase A2 is in the nucleus of subconfluent endothelial cells but confined to the cytoplasm of confluent endothelial cells and redistributes to the nuclear envelope and cell junctions upon histamine stimulation. Laboratory Investigation 1996, 74: 684-95. PMID: 8600319.Peer-Reviewed Original ResearchConceptsSubconfluent endothelial cellsConfluent endothelial cellsNuclear envelopeNuclear localizationConfocal immunofluorescence microscopyEndothelial cellsDose-dependent redistributionGrowth-arrested cellsSubcellular localizationCell density dependencePlasma membraneCell cycleCytoplasmic enzymeNuclear extractsCell junctionsPhospholipase A2 enzymeBovine endothelial cellsHeLa cellsImmunofluorescence microscopyCell lysatesCell nucleiIntercellular junctionsSubconfluent cellsPredominant MrAcid metabolism