2000
Direct Interaction between Endothelial Nitric-oxide Synthase and Dynamin-2 IMPLICATIONS FOR NITRIC-OXIDE SYNTHASE FUNCTION*
Cao S, Yao J, McCabe T, Yao Q, Katusic Z, Sessa W, Shah V. Direct Interaction between Endothelial Nitric-oxide Synthase and Dynamin-2 IMPLICATIONS FOR NITRIC-OXIDE SYNTHASE FUNCTION*. Journal Of Biological Chemistry 2000, 276: 14249-14256. PMID: 11120737, DOI: 10.1074/jbc.m006258200.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAortaBlotting, WesternCalcimycinCattleCell LineDose-Response Relationship, DrugDynamin IDynaminsEndothelium, VascularGlutathione TransferaseGolgi ApparatusGTP PhosphohydrolasesIonophoresKineticsMicroscopy, ConfocalMicroscopy, FluorescenceNitric Oxide SynthaseNitric Oxide Synthase Type IIIPrecipitin TestsProtein BindingProtein BiosynthesisRatsRecombinant Fusion ProteinsTransfectionConceptsDynamin 2Bovine aortic endothelial cellsRecombinant eNOS proteinDirect protein-protein interactionDouble-label confocal immunofluorescenceProtein-protein interactionsSpecific protein interactionsDirect interactionClone 9 cellsEndothelial nitric oxide synthaseMembrane compartmentsLarge GTPaseGlutathione S-transferaseProtein interactionsNovel functionDynaminECV-304 cellsSynthase functionIntracellular signalsMembrane distributionConfocal immunofluorescenceFluorescent proteinENOS regulationGreen fluorescentProtein
1999
Trafficking 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
1996
Palmitoylation of Endothelial Nitric Oxide Synthase Is Necessary for Optimal Stimulated Release of Nitric Oxide: Implications for Caveolae Localization †
Liu J, García-Cardeña G, Sessa W. Palmitoylation of Endothelial Nitric Oxide Synthase Is Necessary for Optimal Stimulated Release of Nitric Oxide: Implications for Caveolae Localization †. Biochemistry 1996, 35: 13277-13281. PMID: 8873592, DOI: 10.1021/bi961720e.Peer-Reviewed Original ResearchConceptsPalmitoylation-deficient mutantMembrane associationN-myristoylationWT enzymeLocalization of eNOSActivation of eNOSEndothelial nitric oxide synthaseCaveolae membranesCaveolar localizationPalmitoylationCysteine palmitoylationWT proteinGolgi complexMutantsIntact cellsCaveolaeVivo significanceHigh saltEnzymeCellsSynthaseNitric oxide synthaseTriton XLocalizationImportant role
1995
The Golgi Association of Endothelial Nitric Oxide Synthase Is Necessary for the Efficient Synthesis of Nitric Oxide(∗)
Sessa W, Garca-Cardea G, Liu J, Keh A, Pollock J, Bradley J, Thiru S, Braverman I, Desai K. The Golgi Association of Endothelial Nitric Oxide Synthase Is Necessary for the Efficient Synthesis of Nitric Oxide(∗). Journal Of Biological Chemistry 1995, 270: 17641-17644. PMID: 7543089, DOI: 10.1074/jbc.270.30.17641.Peer-Reviewed Original ResearchConceptsHEK-293 cellsHeterologous expression systemEndothelial nitric oxide synthaseNovel GolgiGolgi associationExpression systemIntracellular signalsCultured endothelial cellsGolgiIntact blood vesselsEnzymeParticulate enzymeProteinEndothelial cellsCellsSynthaseNitric oxide synthaseOxide synthaseBlood vesselsCompartmentalizationNitric oxideTarget