The DOI matches its Crossref record; 7 of the 7 references it cites were found in a registry or an index.
Protein Modification by SUMO
Abstract
▪ Abstract Small ubiquitin-related modifier (SUMO) family proteins function by becoming covalently attached to other proteins as post-translational modifications. SUMO modifies many proteins that participate in diverse cellular processes, including transcriptional regulation, nuclear transport, maintenance of genome integrity, and signal transduction. Reversible attachment of SUMO is controlled by an enzyme pathway that is analogous to the ubiquitin pathway. The functional consequences of SUMO attachment vary greatly from substrate to substrate, and in many cases are not understood at the molecular level. Frequently SUMO alters interactions of substrates with other proteins or with DNA, but SUMO can also act by blocking ubiquitin attachment sites. An unusual feature of SUMO modification is that, for most substrates, only a small fraction of the substrate is sumoylated at any given time. This review discusses our current understanding of how SUMO conjugation is controlled, as well as the roles of SUMO in a number of biological processes.
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Cites
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Chung, C. D., Liao, J., Liu, B., Rao, X., Jay, P., Berta, P., & Shuai, K. (1997) · Science · doi:10.1126/science.278.5344.1803 · Cited by 980
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Dynamic Interplay of the SUMO and ERK Pathways in Regulating Elk-1 Transcriptional Activity
Yang, S.-H., Jaffray, E., Hay, R. T., & Sharrocks, A. D. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00265-x · Cited by 253
SUMO-1 modification of histone deacetylase 1 (HDAC1) modulates its biological activities
David, G., Neptune, M. A., & DePinho, R. A. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m203690200 · Cited by 236
MDM2-ARF complex regulates p53 sumoylation
Chen, L., & Chen, J. (2003) · Oncogene · doi:10.1038/sj.onc.1206851 · Cited by 134
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Cited by
Divorcing ARF and p53: an unsettled case
Sherr, C. J. (2006) · Nature reviews. Cancer · doi:10.1038/nrc1954 · Cited by 595
Crosstalk between SUMO and Ubiquitin on PCNA Is Mediated by Recruitment of the Helicase Srs2p
Papouli, E., Chen, S., Davies, A. A., Huttner, D., Krejci, L., Sung, P., & Ulrich, H. D. (2005) · Molecular Cell · doi:10.1016/j.molcel.2005.06.001 · Cited by 522
A comprehensive compilation of SUMO proteomics
Hendriks, I. A., & Vertegaal, A. C. O. (2016) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2016.81 · Cited by 514
Metabolic flux and the regulation of mammalian cell growth
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Metadata
- Authors
- Johnson, E. S.
- Venue
- Annual Review of Biochemistry
- Publisher
- Annual Reviews
- Published
- 2004-06
- Volume
- 73
- Issue
- 1
- Pages
- 355-382
- ISSN
- 0066-4154 (ISSN-L)
- 1545-4509
- OpenAlex
- W2112441454
- Cited by
- 1,675
- References
- 7
- FWCI
- 6.21
- Type
- journal article
- Language
- en
- Open access
- closed
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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).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
