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• W1989268736 endingPage "19782" @default.
• W1989268736 startingPage "19777" @default.
• W1989268736 abstract "Nitric oxide (NO) is a highly diffusible and short-lived physiological messenger. Despite its diffusible nature, NO modifies thiol groups of specific cysteine residues in target proteins and alters protein function via S-nitrosylation. Although intracellular S-nitrosylation is a specific posttranslational modification, the defined localization of an NO source (nitric oxide synthase, NOS) with protein S-nitrosylation has never been directly demonstrated. Endothelial NOS (eNOS) is localized mainly on the Golgi apparatus and in plasma membrane caveolae. Here, we show by using eNOS targeted to either the Golgi or the nucleus that S-nitrosylation is concentrated at the primary site of eNOS localization. Furthermore, localization of eNOS on the Golgi enhances overall Golgi protein S-nitrosylation, the specific S-nitrosylation of N-ethylmaleimide-sensitive factor and reduces the speed of protein transport from the endoplasmic reticulum to the plasma membrane in a reversible manner. These data indicate that local NOS action generates organelle-specific protein S-nitrosylation reactions that can regulate intracellular transport processes." @default.
• W1989268736 created "2016-06-24" @default.
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• W1989268736 date "2006-12-26" @default.
• W1989268736 modified "2023-10-16" @default.
• W1989268736 title "Nitric oxide synthase generates nitric oxide locally to regulate compartmentalized protein S-nitrosylation and protein trafficking" @default.
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• W1989268736 doi "https://doi.org/10.1073/pnas.0605907103" @default.
• W1989268736 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/1750883" @default.
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• W1989268736 hasPublicationYear "2006" @default.
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