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BASC, a super complex of BRCA1-associated proteins involved in the recognition and repair of aberrant DNA structures.
Open accessAbstract
We report the identities of the members of a group of proteins that associate with BRCA1 to form a large complex that we have named BASC (B RCA1-a ssociated genome s urveillance c omplex). This complex includes tumor suppressors and DNA damage repair proteins MSH2, MSH6, MLH1, ATM, BLM, and the RAD50–MRE11–NBS1 protein complex. In addition, DNA replication factor C (RFC), a protein complex that facilitates the loading of PCNA onto DNA, is also part of BASC. We find that BRCA1, the BLM helicase, and the RAD50–MRE11–NBS1 complex colocalize to large nuclear foci that contain PCNA when cells are treated with agents that interfere with DNA synthesis. The association of BRCA1 with MSH2 and MSH6, which are required for transcription-coupled repair, provides a possible explanation for the role of BRCA1 in this pathway. Strikingly, all members of this complex have roles in recognition of abnormal DNA structures or damaged DNA, suggesting that BASC may serve as a sensor for DNA damage. Several of these proteins also have roles in DNA replication-associated repair. Collectively, these results suggest that BRCA1 may function as a coordinator of multiple activities required for maintenance of genomic integrity during the process of DNA replication and point to a central role for BRCA1 in DNA repair.
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“In addition to ATM, the members of the BASC include the mismatch repair proteins, MLH1, MSH2, and MSH6, the Bloom's syndrome helicase (BLM), and the Mre11-Rad50-NBS1 complex.”
From Cell cycle checkpoint signaling through the ATM and ATR kinases (2001) · cites this paper as Wang et al. 2000
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“Recent findings position ATM and ATR as critical upstream modulators of the breast cancer susceptibility protein, BRCA1”
From Cell cycle checkpoint signaling through the ATM and ATR kinases (2001) · cites this paper as Wang et al. 2000
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Nimonkar, A. V., Özsoy, A. Z., Genschel, J., Modrich, P. L., & Kowalczykowski, S. C. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0809380105 · Cited by 322
Rapid Activation of ATR by Ionizing Radiation Requires ATM and Mre11
Myers, J. S., & Cortez, D. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m513265200 · Cited by 303
Self-citationPaull, T. T., Cortez, D., Bowers, B., Elledge, S. J., & Gellert, M. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.111125998 · Cited by 282
Self-citationControl of the G2/M Transition
Stark, G. R., & Taylor, W. R. (2006) · Molecular Biotechnology · doi:10.1385/mb:32:3:227 · Cited by 282
Activation of Akt/Protein Kinase B Overcomes a G 2 /M Cell Cycle Checkpoint Induced by DNA Damage
Kandel, E., Skeen, J. E., Majewski, N., Cristofano, A. D., Pandolfi, P. P., Feliciano, C. S., Gartel, A. L., & Hay, N. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.22.7831-7841.2002 · Cited by 277
Molecular Pathogenesis of Osteosarcoma
Kansara, M., & Thomas, D. M. (2007) · DNA and Cell Biology · doi:10.1089/dna.2006.0505 · Cited by 280
Metadata
- Authors
- Wang, Y., Cortez, D., Yazdi, P., Neff, N., Elledge, S. J., & Qin, J.
- Affiliations
- New York Blood Center (US)
- Venue
- Genes & Development
- Publisher
- Cold Spring Harbor Laboratory
- Published
- 2000-04-15
- Volume
- 14
- Issue
- 8
- Pages
- 927-939
- ISSN
- 0890-9369 (ISSN-L)
- 1549-5477
- PMC
- PMC316544
- OpenAlex
- W2127566231
- Cited by
- 1,221
- References
- 54
- Citations by year
- 2026: 5 · 2025: 7 · 2024: 10 · 2023: 16 · 2022: 21 · 2021: 27 · 2020: 20 · 2019: 26 · 2018: 20 · 2017: 24 · 2016: 29 · 2015: 33 · 2014: 49 · 2013: 43 · 2012: 35
- Type
- posted content
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Genes & Development (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Howard Hughes Medical Institute
- Jane Coffin Childs Memorial Fund for Medical Research
- U.S. Bureau of Land Management
- U.S. Public Health Service (Q1187)
- National Institute of General Medical Sciences (GM-44664, R37GM044664, R01GM044664)
- 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, BASC, DNA repair, MSH2, MSH6, MLH1, ATM, BLM helicase, PCNA, DNA damage recognition, genome stability, tumor suppressor proteins, nuclear foci
- MeSH terms
- Adenosine Triphosphatases, Cell Cycle, Cell Nucleus, DNA Repair, DNA Helicases, DNA-Binding Proteins, Endodeoxyribonucleases, Exodeoxyribonucleases, Fluorescent Antibody Technique, Fungal Proteins, HeLa Cells, Humans, Nuclear Proteins, Precipitin Tests, Protein Binding, Mass Spectrometry, Transcription, Genetic, Signal Transduction, Cell Cycle Proteins, BRCA1 Protein, Saccharomyces cerevisiae Proteins, Replication Protein C, RecQ Helicases
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.
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