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SUMO—Nonclassical Ubiquitin
Abstract
▪ Abstract SUMO (small ubiquitin-related modifier) is the best-characterized member of a growing family of ubiquitin-related proteins. It resembles ubiquitin in its structure, its ability to be ligated to other proteins, as well as in the mechanism of ligation. However, in contrast to ubiquitination—often the first step on a one-way road to protein degradation—SUMOlation does not seem to mark proteins for degradation. In fact, SUMO may even function as an antagonist of ubiquitin in the degradation of selected proteins. While most SUMO targets are still at large, available data provide compelling evidence for a role of SUMO in the regulation of protein-protein interactions and/or subcellular localization.
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Citations
Cited by
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Balancing cell adhesion and Wnt signaling, the key role of β-catenin
Brembeck, F. H., Rosário, M., & Birchmeier, W. (2006) · Current Opinion in Genetics & Development · doi:10.1016/j.gde.2005.12.007 · Cited by 668
Divorcing ARF and p53: an unsettled case
Sherr, C. J. (2006) · Nature reviews. Cancer · doi:10.1038/nrc1954 · Cited by 595
GPS-SUMO: a tool for the prediction of sumoylation sites and SUMO-interaction motifs
Zhao, Q., Xie, Y., Zheng, Y., Jiang, S., Liu, W., Mu, W., Liu, Z., Zhao, Y., Xue, Y., & Ren, J. (2014) · Nucleic Acids Research · doi:10.1093/nar/gku383 · Cited by 522
Members of the PIAS family act as SUMO ligases for c-Jun and p53 and repress p53 activity
Schmidt, D., & Müller, S. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.052559499 · Cited by 448
Metadata
- Authors
- Melchior, F.
- Venue
- Annual Review of Cell and Developmental Biology
- Publisher
- Annual Reviews
- Published
- 2000-11
- Volume
- 16
- Issue
- 1
- Pages
- 591-626
- ISSN
- 1081-0706 (ISSN-L)
- 1530-8995
- OpenAlex
- W2122044343
- Cited by
- 774
- References
- 0
- FWCI
- 3.04
- Type
- journal article
- Language
- en
- Open access
- closed
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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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