Bremm, A., Freund, S.M.V. and Komander, D. (2010) Lys11-linked ubiquitin chains adopt compact conformations and are preferentially hydrolyzed by the deubiquitinase Cezanne Nature Structural and Molecular Biology Aug; 17(8), 939-47.
Kulathu Y., Akutsu M., Bremm, A., Hofmann, K. and Komander, D. (2009) Two-sided ubiquitin binding explains specificity of the TAB2 NZF domain. Nature Structural and Molecular Biology, Dec; 16(12), 1328-1330.
Komander, D. (2009) The emerging complexity of the ubiquitin system. Biochemical Society Transactions, Oct; 37(Pt 5), 937-953.
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Group Members
- Yu Ye
- Anja Bremm
- Yogesh Kulathu
- Manuela Hospenthal
- Kirstin Keusekotten
- Tobias Wauer
- Paul Elliott
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Protein ubiquitination affects many fundamental cellular processes. This versatility is achieved by the ability of ubiquitin to form at least eight types of polymers, and cells utilise this repertoire of modifications extensively.
The best-understood ubiquitin polymers are Lys48-linked chains, which target proteins for proteasomal degradation, and Lys63-linked chains, which have important non-degradative functions in cell signalling, endocytosis and the DNA damage response.
The roles of other polyubiquitin chains are currently less clear, and little is known about the machinery for their specific assembly and disassembly. |
Lys63-linked tetraubiquitin
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 Lys48-linked tetraubiquitin |
| As polymers of ubiquitin are chemically identical, the only distinguishing feature between them is their three-dimensional structure (see figure). Importantly, specific enzymes and ubiquitin binding domains exist which recognise only particular types of polyubiquitin.
We aim to study the cellular machinery for specific ubiquitin assembly, disassembly, and binding on a structural and biochemical level. In particular, we want to understand how novel non-degradative ubiquitin chains can regulate cellular processes, how ubiquitin can activate kinase cascades during NF-κB activation, and how selective deubiquitination is controlled during signalling.
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