2012
Proteomic Identification of S-Nitrosylated Golgi Proteins: New Insights into Endothelial Cell Regulation by eNOS-Derived NO
Sangwung P, Greco TM, Wang Y, Ischiropoulos H, Sessa WC, Iwakiri Y. Proteomic Identification of S-Nitrosylated Golgi Proteins: New Insights into Endothelial Cell Regulation by eNOS-Derived NO. PLOS ONE 2012, 7: e31564. PMID: 22363674, PMCID: PMC3283662, DOI: 10.1371/journal.pone.0031564.Peer-Reviewed Original ResearchConceptsGolgi proteinsGolgi phosphoprotein 3S-nitrosylationGolgi apparatusCysteine residuesSelective S-nitrosylationPlasma membrane caveolaeGolgi/endoplasmic reticulumProtein S-nitrosylationTarget cysteine residuesEndothelial cellsEndothelial nitric oxide synthaseMembrane caveolaeEndothelial cell lysatesProteomic identificationEndothelial cell regulationGolgi membranesBiotin switchCell regulationEndoplasmic reticulumENOS stimulationCell lysatesProteinImmunoprecipitationWestern blot
2006
Nitric oxide synthase generates nitric oxide locally to regulate compartmentalized protein S-nitrosylation and protein trafficking
Iwakiri Y, Satoh A, Chatterjee S, Toomre DK, Chalouni CM, Fulton D, Groszmann RJ, Shah VH, Sessa WC. Nitric oxide synthase generates nitric oxide locally to regulate compartmentalized protein S-nitrosylation and protein trafficking. Proceedings Of The National Academy Of Sciences Of The United States Of America 2006, 103: 19777-19782. PMID: 17170139, PMCID: PMC1750883, DOI: 10.1073/pnas.0605907103.Peer-Reviewed Original ResearchConceptsProtein S-nitrosylationS-nitrosylationN-ethylmaleimide-sensitive factorPlasma membrane caveolaeAlters protein functionSpecific cysteine residuesSpecific posttranslational modificationsSpecific S-nitrosylationS-nitrosylation reactionsIntracellular transport processesProtein traffickingMembrane caveolaeProtein functionProtein transportPosttranslational modificationsCysteine residuesPlasma membraneTarget proteinsENOS localizationGolgi apparatusEndoplasmic reticulumGolgiDiffusible natureNOS actionGenerate nitric oxide