Molecular Architecture of the Ankyrin SOCS Box Family of Cul5-Dependent E3 Ubiquitin Ligases
Open accessAbstract
Multi-subunit Cullin-RING E3 ligases often use repeat domain proteins as substrate-specific adaptors. Structures of these macromolecular assemblies are determined for the F-box-containing leucine-rich repeat and WD40 repeat families, but not for the suppressor of cytokine signaling (SOCS)-box-containing ankyrin repeat proteins (ASB1-18), which assemble with Elongins B and C and Cul5. We determined the crystal structures of the ternary complex of ASB9-Elongin B/C as well as the interacting N-terminal domain of Cul5 and used structural comparisons to establish a model for the complete Cul5-based E3 ligase. The structures reveal a distinct architecture of the ASB9 complex that positions the ankyrin domain coaxial to the SOCS box-Elongin B/C complex and perpendicular to other repeat protein complexes. This alternative architecture appears favorable to present the ankyrin domain substrate-binding site to the E2-ubiquitin, while also providing spacing suitable for bulky ASB9 substrates, such as the creatine kinases. The presented Cul5 structure also differs from previous models and deviates from other Cullins via a rigid-body rotation between Cullin repeats. This work highlights the adaptability of repeat domain proteins as scaffolds in substrate recognition and lays the foundation for future structure-function studies of this important E3 family.
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Structural data for ASB9 reveal juxtaposed hydrophobic cavities in the substrate-binding domain.
“structural data for ASB9 reveal juxtaposed hydrophobic cavities in the substrate-binding domain”
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Murphy, J. M., Babon, J. J., Nicola, N. A., & Nicholson, S. E. (2015) · Elsevier eBooks · doi:10.1016/b978-0-12-394447-4.30016-5 · Cited by 4 · see citing works
Self-citationThe JAK–STAT–SOCS Signaling Cascade
Murphy, J. M., Babon, J. J., Nicola, N. A., & Nicholson, S. E. (2016) · Elsevier eBooks · doi:10.1016/b978-0-12-821618-7.30016-5
Self-citationThe Mechanism of Histone Ubiquitylation by the ASB9-CUL5 Ubiquitin Ligase
Lin, C. P., Lee, N. H., Alipranti, F. X., Li, H., & Komives, E. A. (2025) · Molecular & Cellular Proteomics · doi:10.1016/j.mcpro.2025.101471
- Authors
- Muniz, J. R. C., Guo, K., Kershaw, N. J., Ayinampudi, V., von Delft, F., Babon, J. J., & Bullock, A. N.
- Affiliations
- University of Oxford (GB)
- The University of Melbourne (AU)
- Corresponding author
- Bullock, Alex N.
- Venue
- Journal of Molecular Biology
- Publisher
- Elsevier BV
- Published
- 2013-09
- Volume
- 425
- Issue
- 17
- Pages
- 3166-3177
- ISSN
- 0022-2836 (ISSN-L)
- PMC
- PMC3779351
- OpenAlex
- W2084647140
- Cited by
- 34
- References
- 62
- Citations by year
- 2025: 2 · 2024: 2 · 2022: 1 · 2021: 1 · 2020: 2 · 2019: 2 · 2018: 2 · 2017: 3 · 2016: 4 · 2015: 9 · 2014: 5 · 2013: 1
- FWCI
- 2.84
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Molecular Biology (publishedVersion, cc-by-nc-nd)
- Europe PMC (PubMed Central) (publishedVersion, cc-by-nc-nd)
- PubMed Central (publishedVersion, cc-by-nc-nd)
- PubMed (publishedVersion)
- Minerva Access (University of Melbourne) (submittedVersion, cc-by-nc-nd)
- Funders
- National Health and Medical Research Council of Australia (NHMRC) (1011804)
- Victorian State Government Operational Infrastructure Support
- NHMRC Independent Research Institutes Infrastructure Support Scheme (361646)
- Australian Research Council
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Keywords
- ankyrin repeat proteins, SOCS box, E3 ubiquitin ligase, Elongin B/C, Cullin-RING E3 ligases, substrate recognition, ankyrin domain, creatine kinase, crystal structure, ternary complex
- MeSH terms
- Amino Acid Sequence, Animals, Binding Sites, Humans, Molecular Sequence Data, Protein Binding, Sequence Alignment, Ankyrins, Crystallography, X-Ray, Ubiquitin-Protein Ligases, Cullin Proteins, Suppressor of Cytokine Signaling Proteins, Mice
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