Small ubiquitin-related modifiers in chains - PubMed (original) (raw)
Review
. 2007 Dec;35(Pt 6):1422-3.
doi: 10.1042/BST0351422.
Affiliations
- PMID: 18031236
- DOI: 10.1042/BST0351422
Review
Small ubiquitin-related modifiers in chains
A C O Vertegaal. Biochem Soc Trans. 2007 Dec.
Abstract
Post-translational modification of proteins by SUMOs (small ubiquitin-related modifiers) plays an important role in a wide variety of biological processes. The mammalian SUMO family includes three members, SUMO-1, SUMO-2 and SUMO-3. While target proteins are predominantly conjugated to monomeric SUMO, all three SUMO family members are able to multimerize in vitro. In cells, SUMOs have the potential to multimerize via internal consensus sites for SUMOylation that are present in SUMO-2 and SUMO-3. A SUMO-binding motif in Ubc9 (ubiquitin-conjugating enzyme 9) contributes to SUMO chain formation in vitro and SUMO E3 ligases further enhance SUMO polymerization. SUMO chain formation is reversible; SUMO polymers are disassembled by SUMO proteases both in vitro and in vivo. Despite recent progress, the functional relevance of SUMO polymerization is still unclear and little is known about the identity of the endogenous target proteins that are conjugated to SUMO polymers.
Similar articles
- SUMO chains: polymeric signals.
Vertegaal AC. Vertegaal AC. Biochem Soc Trans. 2010 Feb;38(Pt 1):46-9. doi: 10.1042/BST0380046. Biochem Soc Trans. 2010. PMID: 20074033 - Mechanism of Adenovirus E4-ORF3-Mediated SUMO Modifications.
Sohn SY, Hearing P. Sohn SY, et al. mBio. 2019 Feb 26;10(1):e00022-19. doi: 10.1128/mBio.00022-19. mBio. 2019. PMID: 30808699 Free PMC article. - SUMO: getting it on.
Anckar J, Sistonen L. Anckar J, et al. Biochem Soc Trans. 2007 Dec;35(Pt 6):1409-13. doi: 10.1042/BST0351409. Biochem Soc Trans. 2007. PMID: 18031233 Review. - Molecular mechanisms in SUMO conjugation.
Varejão N, Lascorz J, Li Y, Reverter D. Varejão N, et al. Biochem Soc Trans. 2020 Feb 28;48(1):123-135. doi: 10.1042/BST20190357. Biochem Soc Trans. 2020. PMID: 31872228 Review. - Biochemical characterization of SUMO-conjugating enzymes by in vitro sumoylation assays.
Eisenhardt N, Ilic D, Nagamalleswari E, Pichler A. Eisenhardt N, et al. Methods Enzymol. 2019;618:167-185. doi: 10.1016/bs.mie.2018.12.025. Epub 2019 Feb 11. Methods Enzymol. 2019. PMID: 30850051
Cited by
- Small ubiquitin-like modifier-2 modification of retinoic acid receptor-alpha regulates its subcellular localization and transcriptional activity.
Zhu L, Santos NC, Kim KH. Zhu L, et al. Endocrinology. 2009 Dec;150(12):5586-95. doi: 10.1210/en.2009-0868. Epub 2009 Oct 22. Endocrinology. 2009. PMID: 19850744 Free PMC article. - Viral DNA Binding Protein SUMOylation Promotes PML Nuclear Body Localization Next to Viral Replication Centers.
Stubbe M, Mai J, Paulus C, Stubbe HC, Berscheminski J, Karimi M, Hofmann S, Weber E, Hadian K, Hay R, Groitl P, Nevels M, Dobner T, Schreiner S. Stubbe M, et al. mBio. 2020 Mar 17;11(2):e00049-20. doi: 10.1128/mBio.00049-20. mBio. 2020. PMID: 32184235 Free PMC article. - Viral Mimicry to Usurp Ubiquitin and SUMO Host Pathways.
Wimmer P, Schreiner S. Wimmer P, et al. Viruses. 2015 Aug 28;7(9):4854-72. doi: 10.3390/v7092849. Viruses. 2015. PMID: 26343706 Free PMC article. Review. - Regulation of the transforming growth factor β pathway by reversible ubiquitylation.
Al-Salihi MA, Herhaus L, Sapkota GP. Al-Salihi MA, et al. Open Biol. 2012 May;2(5):120082. doi: 10.1098/rsob.120082. Open Biol. 2012. PMID: 22724073 Free PMC article. Review. - Human polycomb 2 protein is a SUMO E3 ligase and alleviates substrate-induced inhibition of cystathionine beta-synthase sumoylation.
Agrawal N, Banerjee R. Agrawal N, et al. PLoS One. 2008;3(12):e4032. doi: 10.1371/journal.pone.0004032. Epub 2008 Dec 24. PLoS One. 2008. PMID: 19107218 Free PMC article.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Miscellaneous