Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 103, Issue 52, Pages 19777-19782Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.0605907103
Keywords
endothelial nitric oxide synthase; Golgi; targeting
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Funding
- NHLBI NIH HHS [R01 HL064793, P01 HL70295, R01 HL64793, R01 HL61371, P01 HL070295, R01 HL57665, R01 HL061371, R01 HL057665] Funding Source: Medline
- NIDDK NIH HHS [R01 DK059615, K01 DK067933-01, P30 DK34989, P30 DK034989, K01 DK067933] Funding Source: Medline
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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.
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