The DOI matches its Crossref record; 4 of the 4 references it cites were found in a registry or an index.
S-nitrosylation of Hsp90 promotes the inhibition of its ATPase and endothelial nitric oxide synthase regulatory activities
Open accessAbstract
Nitric oxide is implicated in a variety of signaling pathways in different systems, notably in endothelial cells. Some of its effects can be exerted through covalent modifications of proteins and, among these modifications, increasing attention is being paid to S-nitrosylation as a signaling mechanism. In this work, we show by a variety of methods (ozone chemiluminescence, biotin switch, and mass spectrometry) that the molecular chaperone Hsp90 is a target of S-nitrosylation and identify a susceptible cysteine residue in the region of the C-terminal domain that interacts with endothelial nitric oxide synthase (eNOS). We also show that the modification occurs in endothelial cells when they are treated with S-nitroso-l-cysteine and when they are exposed to eNOS activators. Hsp90 ATPase activity and its positive effect on eNOS activity are both inhibited by S-nitrosylation. Together, these data suggest that S-nitrosylation may functionally regulate the general activities of Hsp90 and provide a feedback mechanism for limiting eNOS activation.
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Activation of nitric oxide synthase in endothelial cells by Akt-dependent phosphorylation
Dimmeler, S., Fleming, I., Fisslthaler, B., Hermann, C., Busse, R., & Zeiher, A. M. (1999) · Nature · doi:10.1038/21224 · Cited by 3,591
Stamler (2001) · doi:10.1016/s0092-8674(01)00495-0 · Cited by 1,261
Meyer, P., Prodromou, C., Hu, B., Vaughan, C., Roe, S. M., Panaretou, B., Piper, P. W., & Pearl, L. H. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00065-0 · Cited by 491
S-Nitrosation of the Insulin Receptor, Insulin Receptor Substrate 1, and Protein Kinase B/Akt
Carvalho-Filho, M. A., Ueno, M., Hirabara, S. M., Seabra, A. B., Carvalheira, J. B. C., de Oliveira, M. G., Velloso, L. A., Curi, R., & Saad, M. J. A. (2005) · Diabetes · doi:10.2337/diabetes.54.4.959 · Cited by 277
Cited by
HSP90 at the hub of protein homeostasis: emerging mechanistic insights
Taipale, M., Jarosz, D. F., & Lindquist, S. (2010) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2918 · Cited by 1,818
Schopf, F. H., Biebl, M. M., & Buchner, J. (2017) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2017.20 · Cited by 1,540
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
The Hsp90 chaperone machinery: Conformational dynamics and regulation by co-chaperones
Li, J., Soroka, J., & Buchner, J. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2011.09.003 · Cited by 498
S -Nitrosylation in Cardiovascular Signaling
Lima, B., Forrester, M. T., Hess, D. T., & Stamler, J. S. (2010) · Circulation Research · doi:10.1161/circresaha.109.207381 · Cited by 490
Metadata
- Authors
- Martínez-Ruiz, A., Villanueva, L., de Orduña, C. G., López-Ferrer, D., Higueras, M. Á., Tarín, C., Rodríguez-Crespo, I., Vázquez, J., & Lamas, S.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2005-06-03
- Volume
- 102
- Issue
- 24
- Pages
- 8525-8530
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2101457798
- Cited by
- 330
- References
- 4
- FWCI
- 5.76
- Type
- journal article
- Language
- en
- Open access
- green
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- Martínez-Ruiz, A., Villanueva, L., de Orduña, C. G., López-Ferrer, D., Higueras, M. Á., Tarín, C., Rodríguez-Crespo, I., Vázquez, J., & Lamas, S. (2005). S-nitrosylation of Hsp90 promotes the inhibition of its ATPase and endothelial nitric oxide synthase regulatory activities. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.0407294102
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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