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Lys11-linked ubiquitin chains adopt compact conformations and are preferentially hydrolyzed by the deubiquitinase Cezanne
Open accessAbstract
Ubiquitin is a versatile cellular signaling molecule that can form polymers of eight different linkages, and individual linkage types have been associated with distinct cellular functions. Though little is currently known about Lys11-linked ubiquitin chains, recent data indicate that they may be as abundant as Lys48 linkages and may be involved in vital cellular processes. Here we report the generation of Lys11-linked polyubiquitin in vitro, for which the Lys11-specific E2 enzyme UBE2S was fused to a ubiquitin binding domain. Crystallographic and NMR analyses of Lys11-linked diubiquitin reveal that Lys11-linked chains adopt compact conformations in which Ile44 is solvent exposed. Furthermore, we identify the OTU family deubiquitinase Cezanne as the first deubiquitinase with Lys11-linkage preference. Our data highlight the intrinsic specificity of the ubiquitin system that extends to Lys11-linked chains and emphasize that differentially linked polyubiquitin chains must be regarded as independent post-translational modifications.
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Emsley, P., & Cowtan, K. (2004) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444904019158 · Cited by 30,571
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Adams, P. D., Grosse-Kunstleve, R. W., Hung, L.-W., Ioerger, T. R., McCoy, A. J., Moriarty, N. W., Read, R. J., Sacchettini, J. C., Sauter, N. K., & Terwilliger, T. C. (2002) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444902016657 · Cited by 4,361
A comprehensive framework of E2-RING E3 interactions of the human ubiquitin-proteasome system
van Wijk, S. J. L., de Vries, S. J., Kemmeren, P., Huang, A., Boelens, R., Bonvin, A. M. J. J., & Timmers, H. T. M. (2009) · Molecular Systems Biology · doi:10.1038/msb.2009.55 · Cited by 164
Analysis of the human E2 ubiquitin conjugating enzyme protein interaction network
Markson, G., Kiel, C., Hyde, R., Brown, S., Charalabous, P., Bremm, A., Semple, J., Woodsmith, J., Duley, S., Salehi-Ashtiani, K., et al. (2009) · Genome Research · doi:10.1101/gr.093963.109 · Cited by 157
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Cited by
Komander, D., & Rape, M. (2012) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060310-170328 · Cited by 3,679
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Yau, R., & Rape, M. (2016) · Nature Cell Biology · doi:10.1038/ncb3358 · Cited by 1,054
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
Self-citationAtypical 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
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Metadata
- Authors
- Bremm, A., Freund, S. M. V., & Komander, D.
- Venue
- Nature Structural & Molecular Biology
- Published
- 2010-07-11
- Volume
- 17
- Issue
- 8
- Pages
- 939-947
- ISSN
- 1545-9985 (ISSN-L)
- 1545-9993
- OpenAlex
- W2119415370
- Cited by
- 332
- References
- 4
- FWCI
- 10.63
- Type
- journal article
- Language
- en
- Open access
- green
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- Bremm, A., Freund, S. M. V., & Komander, D. (2010). Lys11-linked ubiquitin chains adopt compact conformations and are preferentially hydrolyzed by the deubiquitinase Cezanne. Nature Structural & Molecular Biology. https://doi.org/10.1038/nsmb.1873
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