Structural basis of BRCC36 function in DNA repair and immune regulation
Open accessAbstract
In mammals, ∼100 deubiquitinases act on ∼20,000 intracellular ubiquitination sites. Deubiquitinases are commonly regarded as constitutively active, with limited regulatory and targeting capacity. The BRCA1-A and BRISC complexes serve in DNA double-strand break repair and immune signaling and contain the lysine-63 linkage-specific BRCC36 subunit that is functionalized by scaffold subunits ABRAXAS and ABRO1, respectively. The molecular basis underlying BRCA1-A and BRISC function is currently unknown. Here we show that in the BRCA1-A complex structure, ABRAXAS integrates the DNA repair protein RAP80 and provides a high-affinity binding site that sequesters the tumor suppressor BRCA1 away from the break site. In the BRISC structure, ABRO1 binds SHMT2α, a metabolic enzyme enabling cancer growth in hypoxic environments, which we find prevents BRCC36 from binding and cleaving ubiquitin chains. Our work explains modularity in the BRCC36 DUB family, with different adaptor subunits conferring diversified targeting and regulatory functions.
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SHMT2 has a novel function that contributes to immune regulation through the BRISC complex.
“Recent structural studies have identified a novel function of SHMT2 that contributes to immune regulation through the BRISC complex.”
From A review of small-molecule inhibitors of one-carbon enzymes: SHMT2 and MTHFD2 in the spotlight (2021) · cites this paper as [128]
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Modification ofBRCA1-Associated Breast and Ovarian Cancer Risk byBRCA1-Interacting Genes
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The Lys63-deubiquitylating Enzyme BRCC36 Limits DNA Break Processing and Repair
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Structural Analysis of Human FANCL, the E3 Ligase in the Fanconi Anemia Pathway
Hodson, C., Cole, A. R., Lewis, L., Miles, J. A., Purkiss, A. G., & Walden, H. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.244632 · Cited by 51 · see citing works
RAP80, a Novel Nuclear Protein That Interacts with the Retinoid-related Testis-associated Receptor
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RAP80, ubiquitin and SUMO in the DNA damage response
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Three-Dimensional Architecture of the Human BRCA1-A Histone Deubiquitinase Core Complex
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A review of small-molecule inhibitors of one-carbon enzymes: SHMT2 and MTHFD2 in the spotlight
Cuthbertson, C. R., Arabzada, Z., Bankhead, A., Kyani, A., & Neamati, N. (2021) · ACS Pharmacology & Translational Science · doi:10.1021/acsptsci.0c00223 · Cited by 57 · see citing works
BRCA1-A and BRISC: multifunctional molecular machines for ubiquitin signaling
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Self-citation
- Authors
- Rabl, J., Bunker, R. D., Schenk, A. D., Cavadini, S., Gill, M. E., Abdulrahman, W., Andrés-Pons, A., Luijsterburg, M. S., Ibrahim, A. F. M., Branigan, E., Aguirre, J. D., Marceau, A. H., Guérillon, C., Bouwmeester, T., Hassiepen, U., Peters, A. H. F. M., Renatus, M., Gelman, L., Rubin, S. M., Mailand, N., van Attikum, H., Hay, R. T., & Thomä, N. H.
- Affiliations
- University of Basel (CH)
- Leiden University Medical Center (NL)
- University of Dundee (GB)
- University of California, Santa Cruz (US)
- University of Copenhagen (DK)
- Novartis (Switzerland) (CH)
- Corresponding author
- Thomä, Nicolas H.
- ORCID
- Rabl, Julius
- Bunker, Richard D.
- Schenk, Andreas D.
- Cavadini, Simone
- Gill, Mark E.
- Abdulrahman, Wassim
- Luijsterburg, Martijn S.
- Ibrahim, Adel F.M.
- Branigan, Emma
- Aguirre, Jacob D.
- Marceau, Aimee H.
- Guérillon, Claire
- Bouwmeester, Tewis
- Peters, Antoine H.F.M.
- Renatus, Martin
- Gelman, Laurent
- Rubin, Seth M.
- Mailand, Niels
- Hay, Ronald T.
- Thomä, Nicolas H.
- Venue
- Molecular Cell
- Publisher
- Elsevier BV
- Published
- 2019-08
- Volume
- 75
- Issue
- 3
- Pages
- 483-497.e9
- ISSN
- 1097-2765 (ISSN-L)
- PMC
- PMC6695476
- OpenAlex
- W2953453836
- Cited by
- 84
- References
- 108
- Citations by year
- 2026: 19 · 2025: 11 · 2024: 13 · 2023: 4 · 2022: 12 · 2021: 17 · 2020: 8
- FWCI
- 3.06
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Molecular Cell (publishedVersion, cc-by-nc-nd)
- Europe PMC (PubMed Central) (publishedVersion, cc-by-nc-nd)
- PubMed Central (publishedVersion, cc-by-nc-nd)
- PubMed (publishedVersion)
- Research at the University of Copenhagen (University of Copenhagen) (publishedVersion, cc-by-nc-nd)
- Repository for Publications and Research Data (ETH Zurich) (publishedVersion, cc-by-nc-nd)
- Discovery Research Portal (University of Dundee) (submittedVersion, cc-by-nc-nd)
- DORA PSI (Paul Scherrer Institute) (submittedVersion, cc-by-nc-nd)
- Data Archiving and Networked Services (DANS) (submittedVersion)
- Leiden Repository (Leiden University) (submittedVersion)
- ETH Zürich Research Collection
- Funders
- Lundbeckfonden
- National Institutes of Health (R01 GM127707, R01 GM124148)
- Wellcome Trust (098391/Z/12/7)
- Horizon 2020 Framework Programme
- European Commission
- Kræftens Bekæmpelse
- European Research Council (ERC-CoG, 666068)
- Novartis Foundation
- Nederlandse Organisatie voor Wetenschappelijk Onderzoek (016.161.320)
- Schweizerischer Nationalfonds zur Förderung der Wissenschaftlichen Forschung (CRSII3_160734/1)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA Repair Mechanisms
- Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
- Keywords
- BRCC36, deubiquitinase, BRCA1-A complex, DNA double-strand break repair, Abraxas, RAP80, immune signaling, protein complex structure, hypoxia, cancer metabolism
- MeSH terms
- Deubiquitinating Enzymes, Binding Sites, Carrier Proteins, Cell Nucleus, Cytoplasm, DNA Repair, DNA-Binding Proteins, HeLa Cells, Humans, Immunity, Cellular, Neoplasms, Protein Binding, BRCA1 Protein, Ubiquitin, Nuclear Matrix-Associated Proteins, Multiprotein Complexes, DNA Breaks, Double-Stranded, Ubiquitination, Histone Chaperones, Ubiquitin-Specific Proteases
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
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