The DOI matches its Crossref record; 12 of the 12 references it cites were found in a registry or an index.
Ubiquitin-like Protein Conjugation: Structures, Chemistry, and Mechanism
Open accessAbstract
Ubiquitin-like proteins (Ubl's) are conjugated to target proteins or lipids to regulate their activity, stability, subcellular localization, or macromolecular interactions. Similar to ubiquitin, conjugation is achieved through a cascade of activities that are catalyzed by E1 activating enzymes, E2 conjugating enzymes, and E3 ligases. In this review, we will summarize structural and mechanistic details of enzymes and protein cofactors that participate in Ubl conjugation cascades. Precisely, we will focus on conjugation machinery in the SUMO, NEDD8, ATG8, ATG12, URM1, UFM1, FAT10, and ISG15 pathways while referring to the ubiquitin pathway to highlight common or contrasting themes. We will also review various strategies used to trap intermediates during Ubl activation and conjugation.
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Cites
RING Domain E3 Ubiquitin Ligases
Deshaies, R. J., & Joazeiro, C. A. P. (2009) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.78.101807.093809 · Cited by 2,679
A multiubiquitin chain is confined to specific lysine in a targeted short-lived protein
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Structure of the Cul1–Rbx1–Skp1–F boxSkp2 SCF ubiquitin ligase complex
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The Atg12-Atg5 Conjugate Has a Novel E3-like Activity for Protein Lipidation in Autophagy
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The increasing complexity of the ubiquitin code
Yau, R., & Rape, M. (2016) · Nature Cell Biology · doi:10.1038/ncb3358 · Cited by 1,054
Human intracellular ISG15 prevents interferon-α/β over-amplification and auto-inflammation
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Structure of a RING E3 ligase and ubiquitin-loaded E2 primed for catalysis
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Structure of an E3:E2∼Ub Complex Reveals an Allosteric Mechanism Shared among RING/U-box Ligases
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ATG12 Conjugation to ATG3 Regulates Mitochondrial Homeostasis and Cell Death
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Mechanism of ubiquitin ligation and lysine prioritization by a HECT E3
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Cited by
The role of ubiquitination in tumorigenesis and targeted drug discovery
Deng, L., Meng, T., Chen, L., Wei, W., & Wang, P. (2020) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-020-0107-0 · Cited by 744
Alquezar, C., Arya, S., & Kao, A. W. (2021) · Frontiers in Neurology · doi:10.3389/fneur.2020.595532 · Cited by 367
Protein neddylation and its role in health and diseases
Zhang, S., Yu, Q., Li, Z., Zhao, Y., & Sun, Y. (2024) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-024-01800-9 · Cited by 171
NEDD8 and ubiquitin ligation by cullin-RING E3 ligases
Baek, K., Scott, D. C., & Schulman, B. A. (2021) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2020.10.007 · Cited by 152
An E1–E2 fusion protein primes antiviral immune signalling in bacteria
Ledvina, H. E., Ye, Q., Gu, Y., Sullivan, A. E., Quan, Y., Lau, R. K., Zhou, H., Corbett, K. D., & Whiteley, A. T. (2023) · Nature · doi:10.1038/s41586-022-05647-4 · Cited by 83
Metadata
- Authors
- Cappadocia, L., & Lima, C. D.
- Venue
- Chemical Reviews
- Publisher
- American Chemical Society (ACS)
- Published
- 2017-02-24
- Volume
- 118
- Issue
- 3
- Pages
- 889-918
- ISSN
- 0009-2665 (ISSN-L)
- 1520-6890
- OpenAlex
- W2590813565
- Cited by
- 563
- References
- 12
- FWCI
- 2.75
- Type
- journal article
- Language
- en
- Open access
- hybrid
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