Caveolin-1 Associates with TRAF2 to Form a Complex That Is Recruited to Tumor Necrosis Factor Receptors*
Feng X, Gaeta M, Madge L, Yang J, Bradley J, Pober J. Caveolin-1 Associates with TRAF2 to Form a Complex That Is Recruited to Tumor Necrosis Factor Receptors*. Journal Of Biological Chemistry 2000, 276: 8341-8349. PMID: 11112773, DOI: 10.1074/jbc.m007116200.Peer-Reviewed Original ResearchConceptsCaveolin-1Confocal fluorescence microscopyIntracellular regionNecrosis factor receptor-associated factor 2TNF receptor 2Receptor-associated factor 2TNF receptor 1Promoter-reporter geneCaveolin-1 associatesFluorescence microscopyProtein caveolin-1Caveolin-1 proteinHuman embryonic kidney 293 cellsIntracellular adapter proteinEmbryonic kidney 293 cellsAbsence of ligandRegions of enrichmentKidney 293 cellsEndogenous TRAF2HEK-293 cellsAdapter proteinCultured human umbilical vein endothelial cellsHuman umbilical vein endothelial cellsPlasma membraneUmbilical vein endothelial cellsThe Death Domain of Tumor Necrosis Factor Receptor 1 Is Necessary but Not Sufficient for Golgi Retention of the Receptor and Mediates Receptor Desensitization
Gaeta M, Johnson D, Kluger M, Pober J. The Death Domain of Tumor Necrosis Factor Receptor 1 Is Necessary but Not Sufficient for Golgi Retention of the Receptor and Mediates Receptor Desensitization. Laboratory Investigation 2000, 80: 1185-1194. PMID: 10950109, DOI: 10.1038/labinvest.3780126.Peer-Reviewed Original ResearchConceptsDeath domainGolgi retentionPlasma membraneC-terminal death domainGolgi apparatusNF-kappaBDominant negative inhibitorWild-type receptorDisparate localizationTNF responseIntracellular domainC-terminusEndothelial cellsNegative inhibitorTNF signalsWild typeTumor necrosis factor receptor 1Chimeric receptorsFactor receptor 1Necrosis factor receptor 1Endogenous receptorsBasal expressionReceptor moleculesType receptorTNF action