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Structural Basis for Cul3 Protein Assembly with the BTB-Kelch Family of E3 Ubiquitin Ligases
Open accessAbstract
Cullin-RING ligases are multisubunit E3 ubiquitin ligases that recruit substrate-specific adaptors to catalyze protein ubiquitylation. Cul3-based Cullin-RING ligases are uniquely associated with BTB adaptors that incorporate homodimerization, Cul3 assembly, and substrate recognition into a single multidomain protein, of which the best known are BTB-BACK-Kelch domain proteins, including KEAP1. Cul3 assembly requires a BTB protein "3-box" motif, analogous to the F-box and SOCS box motifs of other Cullin-based E3s. To define the molecular basis for this assembly and the overall architecture of the E3, we determined the crystal structures of the BTB-BACK domains of KLHL11 both alone and in complex with Cul3, along with the Kelch domain structures of KLHL2 (Mayven), KLHL7, KLHL12, and KBTBD5. We show that Cul3 interaction is dependent on a unique N-terminal extension sequence that packs against the 3-box in a hydrophobic groove centrally located between the BTB and BACK domains. Deletion of this N-terminal region results in a 30-fold loss in affinity. The presented data offer a model for the quaternary assembly of this E3 class that supports the bivalent capture of Nrf2 and reveals potential new sites for E3 inhibitor design.
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“Accordingly, Keap1 contains three functional domains (Figure 5). The N-terminal BTB (broad complex, tramtrack, and bric à brac) domain mediates Keap1 homodimerization and contributes to its interaction with Cul3 [68]. Additional Cul3 interaction is provided by a 3-box motif found within the proximal part of the intervening region (IVR) [67]. The IVR contains key reactive cysteine residues through”
From Nrf2 and Oxidative Stress: A General Overview of Mechanisms and Implications in Human Disease (2022) · cites this paper as [67]
In the citing paper
“BTB-containing E3 ligases are typically distinguished by the presence of a 3-box motif that enables high-affinity binding of Cullin 3 (refs 74,75 ).”
From Targeted protein degradation: expanding the toolbox (2019) · cites this paper as [74]
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Metadata
- Authors
- Canning, P., Cooper, C. D. O., Krojer, T., Murray, J. W., Pike, A. C. W., Chaikuad, A., Keates, T., Thangaratnarajah, C., Hojzan, V., Marsden, B. D., Gileadi, O., Knapp, S., von Delft, F., & Bullock, A. N.
- Affiliations
- University of Oxford (GB)
- Corresponding author
- Bullock, Alex N.
- ORCID
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2013-03
- Volume
- 288
- Issue
- 11
- Pages
- 7803-7814
- ISSN
- 0021-9258 (ISSN-L)
- PMC
- PMC3597819
- OpenAlex
- W2029330932
- Cited by
- 284
- References
- 71
- Citations by year
- 2026: 16 · 2025: 22 · 2024: 22 · 2023: 18 · 2022: 25 · 2021: 28 · 2020: 32 · 2019: 22 · 2018: 13 · 2017: 23 · 2016: 15 · 2015: 20 · 2014: 15 · 2013: 13
- FWCI
- 9.41
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion, cc-by-nc)
- PubMed Central (publishedVersion, cc-by-nc)
- PubMed (publishedVersion)
- University of Huddersfield Repository (University of Huddersfield) (acceptedVersion)
- DORA PSI (Paul Scherrer Institute) (submittedVersion, cc-by)
- Funders
- Eli Lilly and Company
- Pfizer (1097737)
- GlaxoSmithKline
- Genome Canada (1097737)
- Wellcome Trust (092809, 092809/Z/10/Z, 1097737, 092809/Z/10)
- Diamond Light Source (1097737)
- Ontario Ministry of Economic Development and Innovation (092809/Z/10/Z, 1097737)
- Ministero dello Sviluppo Economico
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Degradation and Inhibitors
- Keywords
- CUL3, cullin-RING ligases, protein assembly, Kelch domain, N-terminal extension, Keap1, E3 ubiquitin ligase inhibitors, crystal structure
- MeSH terms
- Binding Sites, Calorimetry, Carrier Proteins, Humans, Models, Molecular, Molecular Conformation, Phylogeny, Protein Binding, Protein Conformation, Substrate Specificity, Protein Structure, Secondary, Protein Structure, Tertiary, Crystallography, X-Ray, Dimerization, Ubiquitin, Protein Interaction Mapping, Ubiquitin-Protein Ligases, Cullin Proteins, Proteasome Endopeptidase Complex
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