The DOI matches its Crossref record; 4 of the 4 references it cites were found in a registry or an index.
Structural Basis for Recognition of Diubiquitins by NEMO
Open accessAbstract
SUMMARY NEMO is the regulatory subunit of the IκB kinase (IKK) in NF-κB activation and its CC2-LZ region interacts with Lys63 (K63)-linked polyubiquitin to recruit IKK to receptor signaling complexes. In vitro, CC2-LZ also interacts with tandem diubiquitin. Here we report the crystal structure of CC2-LZ with two dimeric coiled coils representing CC2 and LZ, respectively. Surprisingly, mutagenesis and nuclear magnetic resonance experiments reveal that the binding sites for diubiquitins at LZ are composites of both chains and that each ubiquitin in diubiquitins interacts with symmetrical NEMO asymmetrically. For tandem diubiquitin, the first ubiquitin uses the conserved hydrophobic patch and the C-terminal tail while the second ubiquitin uses an adjacent surface patch. For K63-linked diubiquitin, the proximal ubiquitin uses its conserved hydrophobic patch while the distal ubiquitin mostly employs the C-terminal arm including the K63-linkage residue. These studies uncover the energetics and the common U-shaped geometry for mutual recognition of NEMO and diubiquitins.
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Coot : model-building tools for molecular graphics
Emsley, P., & Cowtan, K. (2004) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444904019158 · Cited by 30,571
HADDOCK: A Protein−Protein Docking Approach Based on Biochemical or Biophysical Information
Dominguez, C., Boelens, R., & Bonvin, A. M. J. J. (2003) · Journal of the American Chemical Society · doi:10.1021/ja026939x · Cited by 3,187
Ubiquitin signalling in the NF-κB pathway
Chen, Z. J. (2005) · Nature Cell Biology · doi:10.1038/ncb0805-758 · Cited by 1,184
NEMO Trimerizes through Its Coiled-coil C-terminal Domain
Agou, F., Ye, F., Goffinont, S., Courtois, G., Yamaoka, S., Israël, A., & Véron, M. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m201964200 · Cited by 79
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Kawai, T., & Akira, S. (2010) · Nature Immunology · doi:10.1038/ni.1863 · Cited by 9,304
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Brenner, D., Blaser, H., & Mak, T. W. (2015) · Nature Reviews Immunology · doi:10.1038/nri3834 · Cited by 998
Linear ubiquitination prevents inflammation and regulates immune signalling
Gerlach, B., Cordier, S. M., Schmukle, A. C., Emmerich, C. H., Rieser, E., Haas, T. L., Webb, A. I., Rickard, J. A., Anderton, H., Wong, W. W.-L., et al. (2011) · Nature · doi:10.1038/nature09816 · Cited by 940
The emerging complexity of protein ubiquitination
Komander, D. (2009) · Biochemical Society Transactions · doi:10.1042/bst0370937 · Cited by 821
Atypical 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
Metadata
- Authors
- Lo, Y.-C., Lin, S.-C., Rospigliosi, C. C., Conze, D. B., Wu, C.-J., Ashwell, J. D., Eliezer, D., & Wu, H.
- Venue
- Molecular Cell
- Publisher
- Elsevier BV
- Published
- 2009-03
- Volume
- 33
- Issue
- 5
- Pages
- 602-615
- ISSN
- 1097-2765 (ISSN-L)
- OpenAlex
- W2033703058
- Cited by
- 259
- References
- 4
- FWCI
- 9.71
- Type
- journal article
- Language
- en
- Open access
- bronze
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- Lo, Y.-C., Lin, S.-C., Rospigliosi, C. C., Conze, D. B., Wu, C.-J., Ashwell, J. D., Eliezer, D., & Wu, H. (2009). Structural Basis for Recognition of Diubiquitins by NEMO. Molecular Cell. https://doi.org/10.1016/j.molcel.2009.01.012
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