The DOI matches its Crossref record; 7 of the 7 references it cites were found in a registry or an index.
Superoxide dismutase 1 acts as a nuclear transcription factor to regulate oxidative stress resistance
Open accessAbstract
Superoxide dismutase 1 (Sod1) has been known for nearly half a century for catalysis of superoxide to hydrogen peroxide. Here we report a new Sod1 function in oxidative signalling: in response to elevated endogenous and exogenous reactive oxygen species (ROS), Sod1 rapidly relocates into the nucleus, which is important for maintaining genomic stability. Interestingly, H2O2 is sufficient to promote Sod1 nuclear localization, indicating that it is responding to general ROS rather than Sod1 substrate superoxide. ROS signalling is mediated by Mec1/ATM and its effector Dun1/Cds1 kinase, through Dun1 interaction with Sod1 and regulation of Sod1 by phosphorylation at S60, 99. In the nucleus, Sod1 binds to promoters and regulates the expression of oxidative resistance and repair genes. Altogether, our study unravels an unorthodox function of Sod1 as a transcription factor and elucidates the regulatory mechanism for its localization. Superoxide dismutase 1 protects cells from reactive oxygen species by catalysing the conversion of superoxide into hydrogen peroxide. Tsang et al.show that this enzyme also plays a transcriptional role in the nucleus, regulating antioxidant gene expression in response to oxidative stress signalling.
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ROS in cancer therapy: the bright side of the moon
Perillo, B., Di Donato, M., Pezone, A., Di Zazzo, E., Giovannelli, P., Galasso, G., Castoria, G., & Migliaccio, A. (2020) · Experimental & Molecular Medicine · doi:10.1038/s12276-020-0384-2 · Cited by 2,176
Paradoxical Roles of Antioxidant Enzymes: Basic Mechanisms and Health Implications
Lei, X. G., Zhu, J.-H., Cheng, W.-H., Bao, Y., Ho, Y.-S., Reddi, A. R., Holmgren, A., & Arnér, E. S. J. (2016) · Physiological Reviews · doi:10.1152/physrev.00010.2014 · Cited by 429
Noctor, G., Mhamdi, A., & Foyer, C. H. (2016) · Plant, Cell & Environment · doi:10.1111/pce.12726 · Cited by 406
Superoxide dismutase: An updated review on its health benefits and industrial applications
Islam, M. N., Rauf, A., Fahad, F. I., Emran, T. B., Mitra, S., Olatunde, A., Shariati, M. A., Rebezov, M., Rengasamy, K. R. R., & Mubarak, M. S. (2022) · Critical Reviews in Food Science and Nutrition · doi:10.1080/10408398.2021.1913400 · Cited by 307
Expanding roles of superoxide dismutases in cell regulation and cancer
Che, M., Wang, R., Li, X., Wang, H.-Y., & Zheng, X. F. S. (2016) · Drug Discovery Today · doi:10.1016/j.drudis.2015.10.001 · Cited by 270
Self-citation
Metadata
- Authors
- Tsang, C. K., Liu, Y., Thomas, J., Zhang, Y., & Zheng, X. F. S.
- Venue
- Nature Communications
- Published
- 2014-03-19
- Volume
- 5
- Issue
- 1
- Pages
- 3446-3446
- ISSN
- 2041-1723 (ISSN-L)
- OpenAlex
- W2050280746
- Cited by
- 496
- References
- 7
- FWCI
- 9.25
- Type
- journal article
- Language
- en
- Open access
- bronze
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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