2000
Reconstitution of an Endothelial Nitric-oxide Synthase (eNOS), hsp90, and Caveolin-1 Complex in Vitro EVIDENCE THAT hsp90 FACILITATES CALMODULIN STIMULATED DISPLACEMENT OF eNOS FROM CAVEOLIN-1*
Gratton J, Fontana J, O'Connor D, Garcı́a-Cardeña G, McCabe T, Sessa W. Reconstitution of an Endothelial Nitric-oxide Synthase (eNOS), hsp90, and Caveolin-1 Complex in Vitro EVIDENCE THAT hsp90 FACILITATES CALMODULIN STIMULATED DISPLACEMENT OF eNOS FROM CAVEOLIN-1*. Journal Of Biological Chemistry 2000, 275: 22268-22272. PMID: 10781589, DOI: 10.1074/jbc.m001644200.Peer-Reviewed Original ResearchConceptsEndothelial nitric oxide synthaseAssociation of eNOSNitric oxide synthaseLung microvascular endothelial cellsCaveolin-1Microvascular endothelial cellsENOS enzymatic activityAction of CaMBovine lung microvascular endothelial cellsENOS functionCalcium-activated calmodulinConcentration of CaMShock protein 90Addition of CaMEndothelial cellsVitro EvidenceCav-1Protein 90AssociationPresence of Hsp90
1999
Caveolins, Liquid-Ordered Domains, and Signal Transduction
Smart E, Graf G, McNiven M, Sessa W, Engelman J, Scherer P, Okamoto T, Lisanti M. Caveolins, Liquid-Ordered Domains, and Signal Transduction. Molecular And Cellular Biology 1999, 19: 7289-7304. PMID: 10523618, PMCID: PMC84723, DOI: 10.1128/mcb.19.11.7289.Peer-Reviewed Original ResearchTrafficking of Endothelial Nitric-oxide Synthase in Living Cells QUANTITATIVE EVIDENCE SUPPORTING THE ROLE OF PALMITOYLATION AS A KINETIC TRAPPING MECHANISM LIMITING MEMBRANE DIFFUSION*
Sowa G, Liu J, Papapetropoulos A, Rex-Haffner M, Hughes T, Sessa W. Trafficking of Endothelial Nitric-oxide Synthase in Living Cells QUANTITATIVE EVIDENCE SUPPORTING THE ROLE OF PALMITOYLATION AS A KINETIC TRAPPING MECHANISM LIMITING MEMBRANE DIFFUSION*. Journal Of Biological Chemistry 1999, 274: 22524-22531. PMID: 10428829, DOI: 10.1074/jbc.274.32.22524.Peer-Reviewed Original ResearchConceptsPlasma membraneENOS-GFPFluorescent protein fusion constructsProtein-protein interactionsRole of palmitoylationProtein fusion constructsLipid bilayersRate of traffickingEndothelial cell line ECV304Endothelial nitric oxide synthasePalmitoylation stateCellular domainsFusion constructsPerinuclear regionLiving cellsProtein diffusionFluorescence recoveryRegulation of eNOSMembrane markersPalmitoylationMutantsGolgiTraffickingMembrane diffusionEndothelial cells
1997
The First 35 Amino Acids and Fatty Acylation Sites Determine the Molecular Targeting of Endothelial Nitric Oxide Synthase into the Golgi Region of Cells: A Green Fluorescent Protein Study
Liu J, Hughes T, Sessa W. The First 35 Amino Acids and Fatty Acylation Sites Determine the Molecular Targeting of Endothelial Nitric Oxide Synthase into the Golgi Region of Cells: A Green Fluorescent Protein Study. Journal Of Cell Biology 1997, 137: 1525-1535. PMID: 9199168, PMCID: PMC2137822, DOI: 10.1083/jcb.137.7.1525.Peer-Reviewed Original ResearchConceptsPalmitoylation-deficient mutantN-myristoylationNIH 3T3 cellsMembrane associationGolgi regionPalmitoylation sitesAmino acidsGreen fluorescent protein studiesGolgi complexFatty acylation sitesGFP fusion proteinBiochemical studiesFluorescent protein chimerasDiffuse fluorescence patternEndothelial cellsEndothelial nitric oxide synthaseCytosolic natureGFP tagFatty acylationAcylated proteinsGolgi markersProtein chimerasIntracellular membranesAcylation siteIntracellular targeting