The DOI matches its Crossref record; 58 of the 58 references it cites were found in a registry or an index.
Ubiquitin-dependent Proteolytic Control of SUMO Conjugates
Open accessAbstract
Posttranslational protein modification with small ubiquitin-related modifier (SUMO) is an important regulatory mechanism implicated in many cellular processes, including several of biomedical relevance. We report that inhibition of the proteasome leads to accumulation of proteins that are simultaneously conjugated to both SUMO and ubiquitin in yeast and in human cells. A similar accumulation of such conjugates was detected in Saccharomyces cerevisiae ubc4 ubc5 cells as well as in mutants lacking two RING finger proteins, Ris1 and Hex3/Slx5-Slx8, that bind to SUMO as well as to the ubiquitin-conjugating enzyme Ubc4. In vitro, Hex3-Slx8 complexes promote Ubc4-dependent ubiquitylation. Together these data identify a previously unrecognized pathway that mediates the proteolytic down-regulation of sumoylated proteins. Formation of substrate-linked SUMO chains promotes targeting of SUMO-modified substrates for ubiquitin-mediated proteolysis. Genetic and biochemical evidence indicates that SUMO conjugation can ultimately lead to inactivation of sumoylated substrates by polysumoylation and/or ubiquitin-dependent degradation. Simultaneous inhibition of both mechanisms leads to severe phenotypic defects.
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A comprehensive analysis of protein–protein interactions in Saccharomyces cerevisiae
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RAD6-dependent DNA repair is linked to modification of PCNA by ubiquitin and SUMO
Hoege, C., Pfander, B., Moldovan, G.-L., Pyrowolakis, G., & Jentsch, S. (2002) · Nature · doi:10.1038/nature00991 · Cited by 2,198
Function and regulation of cullin–RING ubiquitin ligases
Petroski, M. D., & Deshaies, R. J. (2005) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1547 · Cited by 2,148
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Modification of Proteins by Ubiquitin and Ubiquitin-Like Proteins
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Cited by
RING Domain E3 Ubiquitin Ligases
Deshaies, R. J., & Joazeiro, C. A. P. (2009) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.78.101807.093809 · Cited by 2,679
The increasing complexity of the ubiquitin code
Yau, R., & Rape, M. (2016) · Nature Cell Biology · doi:10.1038/ncb3358 · Cited by 1,054
RNF4 is a poly-SUMO-specific E3 ubiquitin ligase required for arsenic-induced PML degradation
Tatham, M. H., Geoffroy, M.-C., Shen, L., Plechanovova, A., Hattersley, N., Jaffray, E. G., Palvimo, J. J., & Hay, R. T. (2008) · Nature Cell Biology · doi:10.1038/ncb1716 · Cited by 847
Arsenic degrades PML or PML–RARα through a SUMO-triggered RNF4/ubiquitin-mediated pathway
Lallemand-Breitenbach, V., Jeanne, M., Benhenda, S., Nasr, R., Lei, M., Peres, L., Zhou, J., Zhu, J., Raught, B., & de Thé, H. (2008) · Nature Cell Biology · doi:10.1038/ncb1717 · Cited by 734
Function and regulation of SUMO proteases
Hickey, C. M., Wilson, N. R., & Hochstrasser, M. (2012) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3478 · Cited by 638
Metadata
- Authors
- Uzunova, K., Göttsche, K., Miteva, M., Weisshaar, S. R., Glanemann, C., Schnellhardt, M., Niessen, M., Scheel, H., Hofmann, K., Johnson, E. S., Praefcke, G. J. K., & Dohmen, R. J.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2007-11
- Volume
- 282
- Issue
- 47
- Pages
- 34167-34175
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2021618108
- Cited by
- 314
- References
- 58
- FWCI
- 9.94
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Uzunova, K., Göttsche, K., Miteva, M., Weisshaar, S. R., Glanemann, C., Schnellhardt, M., Niessen, M., Scheel, H., Hofmann, K., Johnson, E. S., Praefcke, G. J. K., & Dohmen, R. J. (2007). Ubiquitin-dependent Proteolytic Control of SUMO Conjugates. Journal of Biological Chemistry. https://doi.org/10.1074/jbc.m706505200
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