Structural regulation of cullin-RING ubiquitin ligase complexes
Open accessAbstract
Cullin-RING ligases (CRLs) compose the largest class of E3 ubiquitin ligases. CRLs are modular, multisubunit enzymes, comprising interchangeable substrate receptors dedicated to particular Cullin-RING catalytic cores. Recent structural studies have revealed numerous ways in which CRL E3 ligase activities are controlled, including multimodal E3 ligase activation by covalent attachment of the ubiquitin-like protein NEDD8, inhibition of CRL assembly/activity by CAND1, and several mechanisms of regulated substrate recruitment. These features highlight the potential for CRL activities to be tuned in responses to diverse cellular cues, and for modulating CRL functions through small-molecule agonists or antagonists. As the second installment of a two-review series, this article focuses on recent structural studies advancing our knowledge of how CRL activities are regulated.
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Ubiquitin E3 ligases serve as scaffolds between a target protein and an activated E2-Ub, binding both and catalysing transfer of ubiquitin from the E2 active site cysteine to a lysine on the target.
“ubiquitin E3 ligases serve as scaffolds between a target protein and an activated ubiquitin E2 conjugating enzyme charged with a ubiquitin molecule (E2–Ub), by binding both molecules, then catalysing the transfer of ubiquitin from the active site cysteine of the E2 onto a lysine side chain of a target protein104–107.”
From PROTAC targeted protein degraders: the past is prologue (2022) · cites this paper as [105]
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References 49 · Cited by 205
- Authors
- Duda, D. M., Scott, D. C., Calabrese, M. F., Zimmerman, E. S., Zheng, N., & Schulman, B. A.
- Affiliations
- St. Jude Children's Research Hospital (US)
- University of Washington (US)
- Howard Hughes Medical Institute (US)
- Corresponding author
- Schulman, Brenda A
- Venue
- Current Opinion in Structural Biology
- Publisher
- Elsevier BV
- Published
- 2011-04
- Volume
- 21
- Issue
- 2
- Pages
- 257-264
- ISSN
- 0959-440X (ISSN-L)
- PMC
- PMC3151539
- OpenAlex
- W2043405594
- Cited by
- 205
- References
- 49
- Citations by year
- 2026: 5 · 2025: 5 · 2024: 10 · 2023: 8 · 2022: 9 · 2021: 9 · 2020: 16 · 2019: 9 · 2018: 13 · 2017: 16 · 2016: 15 · 2015: 15 · 2014: 19 · 2013: 21 · 2012: 25
- FWCI
- 2.18
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- Locations
- Current Opinion in Structural Biology (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- Howard Hughes Medical Institute
- National Cancer Institute (R01CA107134, P30CA021765)
- National Institute of General Medical Sciences (R01GM077053, F32GM093497, R01GM069530)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Degradation and Inhibitors
- Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
- Keywords
- cullin-RING ubiquitin ligases, E3 ubiquitin ligase, NEDD8, CAND1, small molecule inhibitors, protein structure
- MeSH terms
- Allosteric Regulation, Computer Simulation, Enzyme Inhibitors, Models, Molecular, Protein Conformation, Substrate Specificity, Ubiquitins, Gene Expression Regulation, Enzymologic, Ubiquitin-Protein Ligases, Cullin Proteins
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