The DOI matches its Crossref record; 74 of the 74 references it cites were found in a registry or an index.
The recognition of ubiquitinated proteins by the proteasome
Open accessAbstract
The ability of ubiquitin to form up to eight different polyubiquitin chain linkages generates complexity within the ubiquitin proteasome system, and accounts for the diverse roles of ubiquitination within the cell. Understanding how each type of ubiquitin linkage is correctly interpreted by ubiquitin binding proteins provides important insights into the link between chain recognition and cellular fate. A major function of ubiquitination is to signal degradation of intracellular proteins by the 26S proteasome. Lysine-48 (K48) linked polyubiquitin chains are well established as the canonical signal for proteasomal degradation, but recent studies show a role for other ubiquitin linked chains in facilitating degradation by the 26S proteasome. Here, we review how different types of polyubiquitin linkage bind to ubiquitin receptors on the 26S proteasome, how they signal degradation and discuss the implications of ubiquitin chain linkage in regulating protein breakdown by the proteasome.
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Deng, L., Wang, C., Spencer, E., Yang, L., Braun, A., You, J., Slaughter, C., Pickart, C., & Chen, Z. J. (2000) · Cell · doi:10.1016/s0092-8674(00)00126-4 · Cited by 1,872
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
Recognition of the polyubiquitin proteolytic signal
Thrower, J. S. (2000) · The EMBO Journal · doi:10.1093/emboj/19.1.94 · Cited by 1,716
A multiubiquitin chain is confined to specific lysine in a targeted short-lived protein
Chau, V., Tobias, J. W., Bachmair, A., Marriott, D., Ecker, D. J., Gonda, D. K., & Varshavsky, A. (1989) · Science · doi:10.1126/science.2538923 · Cited by 1,535
Ubiquitin is phosphorylated by PINK1 to activate parkin
Koyano, F., Okatsu, K., Kosako, H., Tamura, Y., Go, E., Kimura, M., Kimura, Y., Tsuchiya, H., Yoshihara, H., Hirokawa, T., et al. (2014) · Nature · doi:10.1038/nature13392 · Cited by 1,477
PINK1 phosphorylates ubiquitin to activate Parkin E3 ubiquitin ligase activity
Kane, L. A., Lazarou, M., Fogel, A. I., Li, Y., Yamano, K., Sarraf, S. A., Banerjee, S., & Youle, R. J. (2014) · Journal of Cell Biology · doi:10.1083/jcb.201402104 · Cited by 1,298
Protein regulation by monoubiquitin
Hicke, L. (2001) · Nature Reviews Molecular Cell Biology · doi:10.1038/35056583 · Cited by 1,211
Mutations in UBQLN2 cause dominant X-linked juvenile and adult-onset ALS and ALS/dementia
Deng, H.-X., Chen, W., Hong, S.-T., Boycott, K. M., Gorrie, G. H., Siddique, N., Yang, Y., Fecto, F., Shi, Y., Zhai, H., et al. (2011) · Nature · doi:10.1038/nature10353 · Cited by 1,174
Xu, P., Duong, D. M., Seyfried, N. T., Cheng, D., Xie, Y., Robert, J., Rush, J., Hochstrasser, M., Finley, D., & Peng, J. (2009) · Cell · doi:10.1016/j.cell.2009.01.041 · Cited by 1,136
Involvement of linear polyubiquitylation of NEMO in NF-κB activation
Tokunaga, F., Sakata, S.-I., Saeki, Y., Satomi, Y., Kirisako, T., Kamei, K., Nakagawa, T., Kato, M., Murata, S., Yamaoka, S., et al. (2009) · Nature Cell Biology · doi:10.1038/ncb1821 · Cited by 942
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Proteolysis-Targeting Chimeras as Therapeutics and Tools for Biological Discovery
Burslem, G. M., & Crews, C. M. (2020) · Cell · doi:10.1016/j.cell.2019.11.031 · Cited by 1,079
E3 ubiquitin ligases: styles, structures and functions
Yang, Q., Zhao, J., Chen, D., & Wang, Y. (2021) · Molecular Biomedicine · doi:10.1186/s43556-021-00043-2 · Cited by 435
Kaji, S., Maki, T., Kinoshita, H., Uemura, N., Ayaki, T., Kawamoto, Y., Furuta, T., Urushitani, M., Hasegawa, M., Kinoshita, Y., et al. (2018) · Stem Cell Reports · doi:10.1016/j.stemcr.2017.12.001 · Cited by 93
“Lysine-48-linked polyubiquitin chains are well established as the signal for 26S proteasomal degradation (Grice and Nathan, 2016).”
BackgroundMu, X., Mu, C., Wang, M., Meng, C., Liu, H., & Lu, H. (2025) · International Journal of Nanomedicine · doi:10.2147/ijn.s552644 · Cited by 16
Metadata
- Authors
- Grice, G. L., & Nathan, J. A.
- Venue
- Cellular and Molecular Life Sciences
- Published
- 2016-05-02
- Volume
- 73
- Issue
- 18
- Pages
- 3497-3506
- ISSN
- 1420-682X (ISSN-L)
- 1420-9071
- OpenAlex
- W2346363069
- Cited by
- 369
- References
- 74
- FWCI
- 10.53
- Type
- journal article
- Language
- en
- Open access
- hybrid
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