The DOI matches its Crossref record; 8 of the 8 references it cites were found in a registry or an index.
Cellular functions of the DUBs
Abstract
Ubiquitylation is a reversible post-translational modification that has emerged as a key regulator of most complex cellular processes. It may rival phosphorylation in scope and exceed it in complexity. The dynamic nature of ubiquitylation events is important for governing protein stability, maintaining ubiquitin homeostasis and controlling ubiquitin-dependent signalling pathways. The human genome encodes ~80 active deubiquitylating enzymes (DUBs, also referred to as deubiquitinases), which exhibit distinct specificity profiles towards the various ubiquitin chain topologies. As a result of their ability to reverse ubiquitylation, these enzymes control a broad range of key cellular processes. In this Commentary we discuss the cellular functions of DUBs, such as their role in governing membrane traffic and protein quality control. We highlight two key signalling pathways – the Wnt and transforming growth factor β (TGF-β) pathways, for which dynamic ubiquitylation has emerged as a key regulator. We also discuss the roles of DUBs in the nucleus, where they govern transcriptional activity and DNA repair pathways.
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Cites
ATM and ATR Substrate Analysis Reveals Extensive Protein Networks Responsive to DNA Damage
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Cited by
Mevissen, T. E. T., Hospenthal, M. K., Geurink, P. P., Elliott, P. R., Akutsu, M., Arnaudo, N., Ekkebus, R., Kulathu, Y., Wauer, T., El Oualid, F., et al. (2013) · Cell · doi:10.1016/j.cell.2013.05.046 · Cited by 626
Atypical ubiquitylation — the unexplored world of polyubiquitin beyond Lys48 and Lys63 linkages
Kulathu, Y., & Komander, D. (2012) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3394 · Cited by 619
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
Self-citationAbdul Rehman, S. A., Kristariyanto, Y. A., Choi, S.-Y., Nkosi, P. J., Weidlich, S., Labib, K., Hofmann, K., & Kulathu, Y. (2016) · Molecular Cell · doi:10.1016/j.molcel.2016.05.009 · Cited by 363
Targeting the ubiquitin-proteasome pathway to overcome anti-cancer drug resistance
Narayanan, S., Cai, C.-Y., Assaraf, Y. G., Guo, H.-Q., Cui, Q., Wei, L., Huang, J.-J., Ashby, C. R., & Chen, Z.-S. (2020) · Drug Resistance Updates · doi:10.1016/j.drup.2019.100663 · Cited by 332
Metadata
- Authors
- Clague, M. J., Coulson, J. M., & Urbé, S.
- Venue
- Journal of Cell Science
- Publisher
- The Company of Biologists
- Published
- 2012-01-15
- Volume
- 125
- Issue
- 2
- Pages
- 277-286
- ISSN
- 0021-9533 (ISSN-L)
- 1477-9137
- OpenAlex
- W2055361823
- Cited by
- 220
- References
- 8
- FWCI
- 9.29
- Type
- journal article
- Language
- en
- Open access
- closed
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