The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.
Structural Studies of the Interaction between Ubiquitin Family Proteins and Proteasome Subunit S5a
Abstract
The 26S proteasome is essential for the proteolysis of proteins that have been covalently modified by the attachment of polyubiquitinated chains. Although the 20S core particle performs the degradation, the 19S regulatory cap complex is responsible for recognition of polyubiquitinated substrates. We have focused on how the S5a component of the 19S complex interacts with different ubiquitin-like (ubl) modules, to advance our understanding of how polyubiquitinated proteins are targeted to the proteasome. To achieve this, we have determined the solution structure of the ubl domain of hPLIC-2 and obtained a structural model of hHR23a by using NMR spectroscopy and homology modeling. We have also compared the S5a binding properties of ubiquitin, SUMO-1, and the ubl domains of hPLIC-2 and hHR23a and have identified the residues on their respective S5a contact surfaces. We provide evidence that the S5a-binding surface on the ubl domain of hPLIC-2 is required for its interaction with the proteasome. This study provides structural insights into protein recognition by the proteasome, and illustrates how the protein surface of a commonly utilized fold has highly evolved for various biological roles.
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Cites
Protein backbone angle restraints from searching a database for chemical shift and sequence homology
Cornilescu, G., Delaglio, F., & Bax, A. (1999) · Journal of Biomolecular NMR · doi:10.1023/a:1008392405740 · Cited by 2,957
Masutani, C., Sugasawa, K., Yanagisawa, J., Sonoyama, T., Ui, M., Enomoto, T., Takio, K., Tanaka, K., van der Spek, P. J., & Bootsma, D. (1994) · The EMBO Journal · doi:10.1002/j.1460-2075.1994.tb06452.x · Cited by 400
Cited by
Recognition and Processing of Ubiquitin-Protein Conjugates by the Proteasome
Finley, D. (2009) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.78.081507.101607 · Cited by 1,764
Dao, T. P., Kolaitis, R.-M., Kim, H. J., O’Donovan, K., Martyniak, B., Colicino, E., Hehnly, H., Taylor, J. P., & Castañeda, C. A. (2018) · Molecular Cell · doi:10.1016/j.molcel.2018.02.004 · Cited by 341
PLIC proteins or ubiquilins regulate autophagy‐dependent cell survival during nutrient starvation
N'Diaye, E., Kajihara, K. K., Hsieh, I., Morisaki, H., Debnath, J., & Brown, E. J. (2009) · The EMBO Reports · doi:10.1038/embor.2008.238 · Cited by 323
Fallon, L., Bélanger, C. M. L., Corera, A. T., Kontogiannea, M., Regan-Klapisz, E., Moreau, F., Voortman, J., Haber, M., Rouleau, G., Thorarinsdottir, T., et al. (2006) · Nature Cell Biology · doi:10.1038/ncb1441 · Cited by 317
Massey, L. K., Mah, A. L., & Monteiro, M. J. (2005) · Biochemical Journal · doi:10.1042/bj20050491 · Cited by 66
Metadata
- Authors
- Walters, K. J., Kleijnen, M. F., Goh, A. M., Wagner, G., & Howley, P. M.
- Venue
- Biochemistry
- Publisher
- American Chemical Society (ACS)
- Published
- 2002-01-18
- Volume
- 41
- Issue
- 6
- Pages
- 1767-1777
- ISSN
- 0006-2960 (ISSN-L)
- 1520-4995
- OpenAlex
- W1988170942
- Cited by
- 220
- References
- 2
- FWCI
- 6.37
- Type
- journal article
- Language
- en
- Open access
- closed
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- Walters, K. J., Kleijnen, M. F., Goh, A. M., Wagner, G., & Howley, P. M. (2002). Structural Studies of the Interaction between Ubiquitin Family Proteins and Proteasome Subunit S5a. Biochemistry. https://doi.org/10.1021/bi011892y
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