Nitric Oxide Synthase Generates Nitric Oxide Locally to Regulate Compartmentalized Protein S-Nitrosylation and Protein Trafficking

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 posttransla...

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Published inProceedings of the National Academy of Sciences - PNAS Vol. 103; no. 52; pp. 19777 - 19782
Main Authors Iwakiri, Yasuko, Satoh, Ayano, Chatterjee, Suvro, Toomre, Derek K., Chalouni, Cecile M., Fulton, David, Groszmann, Roberto J., Shah, Vijay H., Sessa, William C.
Format Journal Article
LanguageEnglish
Published United States National Academy of Sciences 26.12.2006
National Acad Sciences
Subjects
Animals
Antibodies
Biological Sciences
Cattle
Cell Line
Cell lines
Cell membranes
Cellular biology
Cercopithecus aethiops
COS cells
Endothelial cells
Fluorescence
Gene expression regulation
Golgi apparatus
Golgi Apparatus - metabolism
Kinetics
Membranes
Nitric oxide
Nitric Oxide - metabolism
Nitric Oxide Synthase Type III - genetics
Nitric Oxide Synthase Type III - metabolism
Oxides
Protein Transport
S-Nitrosothiols - metabolism
Transfection
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Summary: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 Snitrosylation 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-ethylmaleimidesensitive 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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Edited by Louis J. Ignarro, University of California School of Medicine, Los Angeles, CA, and approved October 23, 2006d
Author contributions: Y.I., C.M.C., and R.J.G. designed research; Y.I., A.S., S.C., and C.M.C. performed research; D.K.T., D.F., and V.H.S. contributed new reagents/analytic tools; Y.I., S.C., D.K.T., C.M.C., V.H.S., and W.C.S. analyzed data; and Y.I., R.J.G., V.H.S., and W.C.S. wrote the paper.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.0605907103