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Multifactorial contributions to an acute DNA damage response by BRCA1/BARD1-containing complexes
Open accessAbstract
The BRCA1 gene product and its stoichiometric binding partner, BARD1, play a vital role in the cellular response to DNA damage. However, how they acquire specific biochemical functions after DNA damage is poorly understood. Following exposure to genotoxic stress, DNA damage-specific interactions were observed between BRCA1/BARD1 and the DNA damage-response proteins, TopBP1 and Mre11/Rad50/NBS1. Two distinct DNA damage-dependent super complexes emerged; their activation was dependent, in part, on the actions of specific checkpoint kinases, and each super complex contributed to a distinctive aspect of the DNA damage response. The results support a new, multifactorial model that describes how genotoxic stress enables BRCA1 to execute a diverse set of DNA damage-response functions.
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“Three proteins, Abraxas (also known as Abra1, FAM175A, CCDC98), Bach1 (also known as Brip1, FancJ) and CtIP (also known as RBBP8), directly interact with the BRCA1 BRCT domains through the pSPxF motif in a phosphorylation-dependent manner forming mutually exclusive complexes, which were thus named as the A, B and C complexes of BRCA1 (Greenberg et al., 2006; Kim et al., 2007; Liu et al., 2007;”
From The BRCA1-Interacting Protein Abraxas Is Required for Genomic Stability and Tumor Suppression (2014) · cites this paper as Greenberg et al., 2006
In the citing paper
“FANCJ helicase activity induced in S phase is also required for FANCJ to promote S phase progression and possibly intra-S phase checkpoints [71,72].”
From Hereditary Breast Cancer and the BRCA1-Associated FANCJ/BACH1/BRIP1 (2011) · cites this paper as [72]
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Self-citation
Metadata
- Authors
- Greenberg, R. A., Sobhian, B., Pathania, S., Cantor, S. B., Nakatani, Y., & Livingston, D. M.
- Affiliations
- Harvard University (US)
- Venue
- Genes & Development
- Publisher
- Cold Spring Harbor Laboratory
- Published
- 2006-01-01
- Volume
- 20
- Issue
- 1
- Pages
- 34-46
- ISSN
- 0890-9369 (ISSN-L)
- 1549-5477
- PMC
- PMC1356099
- OpenAlex
- W2164458581
- Cited by
- 308
- References
- 61
- Citations by year
- 2026: 2 · 2025: 3 · 2024: 4 · 2023: 9 · 2022: 12 · 2021: 17 · 2020: 13 · 2019: 4 · 2018: 14 · 2017: 12 · 2016: 10 · 2015: 19 · 2014: 21 · 2013: 19 · 2012: 22
- Type
- posted content
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Genes & Development (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- eScholarship@UMassChan (submittedVersion)
- Funders
- Leukemia Research Foundation
- Broad Institute
- Österreichischen Akademie der Wissenschaften
- National Cancer Institute
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA Repair Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › BRCA gene mutations in cancer
- Health Sciences › Medicine › Oncology › PARP inhibition in cancer therapy
- Keywords
- BRCA1, BARD1, DNA damage response, TopBP1, Mre11-Rad50-Nbs1, checkpoint kinase, genotoxic stress
- MeSH terms
- MRE11 Homologue Protein, Carrier Proteins, Cell Cycle, DNA Damage, DNA Repair, DNA-Binding Proteins, Humans, Nuclear Proteins, Protein Binding, Acid Anhydride Hydrolases, Cell Cycle Proteins, BRCA1 Protein, Tumor Suppressor Proteins, Ubiquitin-Protein Ligases, DNA Repair Enzymes, Cell Line, Tumor
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