The DOI matches its Crossref record; 9 of the 9 references it cites were found in a registry or an index.
Deubiquitinases as a Signaling Target of Oxidative Stress
Open accessAbstract
Deubiquitinating enzymes (DUBs) constitute a large family of cysteine proteases that have a broad impact on numerous biological and pathological processes, including the regulation of genomic stability. DUBs are often assembled onto multiprotein complexes to assist in their localization and substrate selection, yet it remains unclear how the enzymatic activity of DUBs is modulated by intracellular signals. Herein, we show that bursts of reactive oxygen species (ROS) reversibly inactivate DUBs through the oxidation of the catalytic cysteine residue. Importantly, USP1, a key regulator of genomic stability, is reversibly inactivated upon oxidative stress. This, in part, explains the rapid nature of PCNA monoubiquitination-dependent DNA damage tolerance in response to oxidative DNA damage in replicating cells. We propose that DUBs of the cysteine protease family act as ROS sensors in human cells and that ROS-mediated DUB inactivation is a critical mechanism for fine-tuning stress-activated signaling pathways.
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Cites
Targeting cancer cells by ROS-mediated mechanisms: a radical therapeutic approach?
Trachootham, D., Alexandre, J., & Huang, P. (2009) · Nature Reviews Drug Discovery · doi:10.1038/nrd2803 · Cited by 5,452
Oxidative stress in neurodegeneration: Cause or consequence?
Andersen, J. K. (2004) · Nature Medicine · doi:10.1038/nrn1434 · Cited by 1,869
Redox regulation of protein tyrosine phosphatase 1B involves a sulphenyl-amide intermediate
Salmeen, A., Andersen, J. N., Myers, M. P., Meng, T.-C., Hinks, J. A., Tonks, N. K., & Barford, D. (2003) · Nature · doi:10.1038/nature01680 · Cited by 951
Ubiquitin-binding domains in Y-family polymerases regulate translesion synthesis.
Bienko, M., Green, C. M., Crosetto, N., Rudolf, F., Zapart, G., Coull, B., Kannouche, P., Wider, G., Peter, M., Lehmann, A. R., et al. (2005) · Science · doi:10.1126/science.1120615 · Cited by 712
A dynamic role of HAUSP in the p53-Mdm2 pathway
Li, M., Brooks, C. L., Kon, N., & Gu, W. (2004) · Molecular Cell · doi:10.1016/s1097-2765(04)00157-1 · Cited by 679
Chemistry-Based Functional Proteomics Reveals Novel Members of the Deubiquitinating Enzyme Family
Borodovsky, A., Ovaa, H., Kolli, N., Gan-Erdene, T., Wilkinson, K. D., Ploegh, H. L., & Kessler, B. M. (2002) · Chemistry & Biology · doi:10.1016/s1074-5521(02)00248-x · Cited by 588
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Fluorescent Proteins as Proteomic Probes
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Cited by
Cellular mechanisms and physiological consequences of redox-dependent signalling
Holmström, K. M., & Finkel, T. (2014) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3801 · Cited by 2,093
Deubiquitylases From Genes to Organism
Clague, M. J., Barsukov, I., Coulson, J. M., Liu, H., Rigden, D. J., & Urbé, S. (2013) · Physiological Reviews · doi:10.1152/physrev.00002.2013 · Cited by 425
Köster, S., Upadhyay, S., Chandra, P., Papavinasasundaram, K., Yang, G., Hassan, A., Grigsby, S. J., Mittal, E., Park, H. S., Jones, V., et al. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1707792114 · Cited by 208
Drummond, E. S., Nayak, S., Ueberheide, B., & Wisniewski, T. (2015) · Scientific Reports · doi:10.1038/srep15456 · Cited by 78
Self-citationUSP7 is a suppressor of PCNA ubiquitination and oxidative-stress-induced mutagenesis in human cells.
Kashiwaba, S.-I., Kanao, R., Masuda, Y., Kusumoto-Matsuo, R., Hanaoka, F., & Masutani, C. (2015) · Cell Reports · doi:10.1016/j.celrep.2015.11.014 · Cited by 71
Metadata
- Authors
- Cotto-Rios, X. M., Békés, M., Chapman, J., Ueberheide, B., & Huang, T. T.
- Venue
- Cell Reports
- Publisher
- Elsevier BV
- Published
- 2012-12
- Volume
- 2
- Issue
- 6
- Pages
- 1475-1484
- ISSN
- 2211-1247 (ISSN-L)
- OpenAlex
- W2087608460
- Cited by
- 159
- References
- 9
- FWCI
- 5.92
- Type
- journal article
- Language
- en
- Open access
- gold
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- Cotto-Rios, X. M., Békés, M., Chapman, J., Ueberheide, B., & Huang, T. T. (2012). Deubiquitinases as a Signaling Target of Oxidative Stress. Cell Reports. https://doi.org/10.1016/j.celrep.2012.11.011
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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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