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New structural features of the APC/C revealed by high resolution cryo-EM structures of apo-APC/C and the APC/CCDH1:EMI1 complex
Open accessPreprint — published as 10.1038/s41467-024-54398-5 · Paper page
Abstract
The multi-subunit anaphase-promoting complex/cyclosome (APC/C) is a master regulator of cell division. It controls progression through the cell cycle by timely marking mitotic cyclins and other cell cycle regulatory proteins for degradation via the ubiquitin-proteasome pathway. The APC/C itself is regulated by the sequential action of its coactivator subunits CDC20 and CDH1, post-translational modifications, and its inhibitory binding partners EMI1 and the mitotic checkpoint complex (MCC). In this study, we took advantage of the latest developments in cryo-electron microscopy (cryo-EM) to determine the structures of human APC/C Cdh1:EMI1 and apo-APC/C at 2.9 Å and 3.2 Å, respectively, providing novel insights into the regulation of APC/C activity. The high resolution maps allowed the unambigious assignment of a previously unassigned a-helix to the N-terminus of CDH1 (CDH1 α1) in the APC/C Cdh1:EMI1 ternary complex. CDH1 α1 binds at the APC1:APC8 interface, thereby interacting with a loop segment of APC1 through electrostatic interactions only provided by CDH1 but not CDC20. We also indentified a novel zinc-binding module in APC2, and confirmed the presence of zinc ions experimentally. Finally, due to the higher resolution and well defined density of these maps we were able to build, aided by AlphaFold predictions, several intrinsically disordered regions in different APC/C subunits that play a fundamental role in proper complex assembly.
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Cites
Highly accurate protein structure prediction with AlphaFold
Jumper, J., Evans, R., Pritzel, A., Green, T., Figurnov, M., Ronneberger, O., Tunyasuvunakool, K., Bates, R., Žídek, A., Potapenko, A., et al. (2021) · Nature · doi:10.1038/s41586-021-03819-2 · Cited by 43,764
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Metadata
- Authors
- Barford, D., Höfler, A., Yu, J., Yan, J., Zhang, Z., Chang, L., Grime, G., Garman, E., & Boland, A.
- Affiliations
- MRC Laboratory of Molecular Biology (GB)
- University of Geneva (CH)
- MRC Laboratory of Molecular Biology
- University of Surrey (GB)
- University of Oxford (GB)
- Corresponding author
- Barford, David
- Boland, Andreas
- ORCID
- Venue
- Nature Communications
- Published
- 2023-09-18
- Volume
- 15
- Issue
- 1
- Pages
- 10074-10074
- ISSN
- 2041-1723 (ISSN-L)
- PMC
- PMC11579458
- OpenAlex
- W4404532716
- Cited by
- 18
- References
- 1
- Citations by year
- 2026: 6 · 2025: 8 · 2024: 4
- FWCI
- 4.03
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Locations
- Nature Communications (publishedVersion, cc-by)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by)
- Research Square (acceptedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Apollo (University of Cambridge) (submittedVersion, cc-by)
- RePEc: Research Papers in Economics (submittedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Funders
- National Science Foundation
- UK Research and Innovation (MC_UP_1201/6)
- Cancer Research UK (C576/A14109)
- Schweizerischer Nationalfonds zur Förderung der Wissenschaftlichen Forschung (211581, 185235, 310030)
- Medical Research Council (MC_UP_1201/6)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Health Sciences › Medicine › Oncology › Cancer-related Molecular Pathways
- Keywords
- anaphase-promoting complex, CDH1, Emi1, CDC20, APC2, intrinsically disordered regions, protein complex structure, cell cycle regulation, spindle assembly checkpoint, protein assembly
- MeSH terms
- Humans, Models, Molecular, Protein Binding, Zinc, Antigens, CD, Cadherins, Cell Cycle Proteins, Cryoelectron Microscopy, Anaphase-Promoting Complex-Cyclosome, Cdc20 Proteins, Cdh1 Proteins
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