The DOI matches its Crossref record; 48 of the 48 references it cites were found in a registry or an index.
Nitric oxide synthase generates nitric oxide locally to regulate compartmentalized protein S-nitrosylation and protein trafficking
Open accessAbstract
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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Cites
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Redox-based regulation of signal transduction: principles, pitfalls, and promises
Janssen-Heininger, Y. M. W., Mossman, B. T., Heintz, N. H., Forman, H. J., Kalyanaraman, B., Finkel, T., Stamler, J. S., Rhee, S. G., & van der Vliet, A. (2008) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2008.03.011 · Cited by 784
Protein S-nitrosylation in health and disease: a current perspective
Foster, M. W., Hess, D. T., & Stamler, J. S. (2009) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2009.06.007 · Cited by 752
Protein denitrosylation: enzymatic mechanisms and cellular functions
Benhar, M., Forrester, M. T., & Stamler, J. S. (2009) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2764 · Cited by 522
Thomas, S. R., Witting, P. K., & Drummond, G. R. (2008) · Antioxidants & Redox Signaling · doi:10.1089/ars.2008.2027 · Cited by 383
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Metadata
- Authors
- Iwakiri, Y., Satoh, A., Chatterjee, S., Toomre, D. K., Chalouni, C. M., Fulton, D., Groszmann, R. J., Shah, V. H., & Sessa, W. C.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2006-12-26
- Volume
- 103
- Issue
- 52
- Pages
- 19777-19782
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W1989268736
- Cited by
- 260
- References
- 48
- FWCI
- 10.00
- Type
- journal article
- Language
- en
- Open access
- green
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- Iwakiri, Y., Satoh, A., Chatterjee, S., Toomre, D. K., Chalouni, C. M., Fulton, D., Groszmann, R. J., Shah, V. H., & Sessa, W. C. (2006). Nitric oxide synthase generates nitric oxide locally to regulate compartmentalized protein S-nitrosylation and protein trafficking. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.0605907103
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