The DOI matches its Crossref record; 42 of the 42 references it cites were found in a registry or an index.
Rad51 Paralog Complexes BCDX2 and CX3 Act at Different Stages in the BRCA1-BRCA2-Dependent Homologous Recombination Pathway
Open accessAbstract
The Rad51 paralogs are required for homologous recombination (HR) and the maintenance of genomic stability. The molecular mechanisms by which the five vertebrate Rad51 paralogs regulate HR and genomic integrity remain unclear. The Rad51 paralogs associate with one another in two distinct complexes: Rad51B-Rad51C-Rad51D-XRCC2 (BCDX2) and Rad51C-XRCC3 (CX3). We find that the BCDX2 and CX3 complexes act at different stages of the HR pathway. In response to DNA damage, the BCDX2 complex acts downstream of BRCA2 recruitment but upstream of Rad51 recruitment. In contrast, the CX3 complex acts downstream of Rad51 recruitment but still has a marked impact on the measured frequency of homologous recombination. Both complexes are epistatic with BRCA2 and synthetically lethal with Rad52. We conclude that human Rad51 paralogs facilitate BRCA2-Rad51-dependent homologous recombination at different stages in the pathway and function independently of Rad52.
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“Given that these three genes all belong to the RAD51 paralog complex BCDX223, the BRCA2-type HRD suggests that RAD51B and XRCC2 deficiency could have led to HRD in these patients.”
From Pan-cancer landscape of homologous recombination deficiency. (2020) · cites this paper as [23]
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Cites
BRCA1 and BRCA2: different roles in a common pathway of genome protection
Roy, R., Chun, J., & Powell, S. N. (2011) · Nature reviews. Cancer · doi:10.1038/nrc3181 · Cited by 1,555
Self-citationXRCC3 promotes homology-directed repair of DNA damage in mammalian cellsPreprint
Pierce, A. J., Johnson, R. D., Thompson, L. H., & Jasin, M. (1999) · Genes & Development · doi:10.1101/gad.13.20.2633 · Cited by 1,384
Regulation of Homologous Recombination in Eukaryotes
Heyer, W.-D., Ehmsen, K. T., & Liu, J. (2010) · Annual Review of Genetics · doi:10.1146/annurev-genet-051710-150955 · Cited by 1,066
Takata, M., Sasaki, M. S., Tachiiri, S., Fukushima, T., Sonoda, E., Schild, D., Thompson, L. H., & Takeda, S. (2001) · Molecular and Cellular Biology · doi:10.1128/mcb.21.8.2858-2866.2001 · Cited by 523
Rad51 Recombinase and Recombination Mediators
Sung, P., Krejčí, L., Komen, S. V., & Sehorn, M. G. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.r300027200 · Cited by 446
Recombinational DNA repair and human disease
Thompson, L. H., & Schild, D. (2002) · Mutation Research - Fundamental and Molecular Mechanisms of Mutagenesis · doi:10.1016/s0027-5107(02)00224-5 · Cited by 417
Identification and purification of two distinct complexes containing the five RAD51 paralogsPreprint
Masson, J., Tarsounas, M., Stasiak, A. Z., Stasiak, A., Punatar, R. S., McIlwraith, M. J., Benson, F. E., & West, S. C. (2001) · Genes & Development · doi:10.1101/gad.947001 · Cited by 395
Rad52 inactivation is synthetically lethal with BRCA2 deficiency
Feng, Z., Scott, S. P., Bussen, W., Sharma, G. G., Guo, G., Pandita, T. K., & Powell, S. N. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1010959107 · Cited by 346
Self-citationChk2 Phosphorylation of BRCA1 Regulates DNA Double-Strand Break Repair
Zhang, J., Willers, H., Feng, Z., Ghosh, J. C., Kim, S., Weaver, D. T., Chung, J. H., Powell, S. N., & Xia, F. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.2.708-718.2004 · Cited by 323
Self-citationHu, Y., Raynard, S. J., Sehorn, M. G., Lu, X., Bussen, W., Zheng, L., Stark, J. M., Barnes, E. L., Chi, P., Janščák, P., et al. (2007) · Genes & Development · doi:10.1101/gad.1609107 · Cited by 322
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In vitro and in cellulo profiling of a novel phosphorylated form of RAD51 at serine 97
Alaouid, M. (2023) · theses.fr (ABES) · doi:10.70675/1f4bfdc7zc3efz4073zafe4zf37e7b667c7b
Genetic polymorphisms of DNA repair pathways in pancreatic cancer progression and treatment
Saraf, F., Purohit, M. R., Lakshmisundaram, R., Verma, H. K., & Bhaskar, L. V. K. S. (2026) · Elsevier eBooks · doi:10.1016/b978-0-443-43976-6.00017-x
Бабушкина, Н. П., Bragina, E. Y., Владимирович, Н. Е., & Николаевна, К. А. (2026) · Russian Journal of Genetics · doi:10.1134/s102279542670033x
Bocquet, N., Potenza, A., Clochard, J., Kuster, A., Kok, H., Iacovino, L., Jin, T., Xu, Z., Powell, A. J., Barker, I. A., et al. (2026) · Journal of the American Chemical Society · doi:10.1021/jacs.6c16278
Vargas, E., Santiago‐Tovar, N., Murcia-Soriano, L. F., PatinoHerrera, A., Parra-Medina, R. S., & Riaño-Moreno, J. C. (2026) · AJOG Global Reports · doi:10.1016/j.xagr.2026.100693
Metadata
- Authors
- Chun, J., Buechelmaier, E. S., & Powell, S. N.
- Affiliations
- Memorial Sloan Kettering Cancer Center (US)
- Venue
- Molecular and Cellular Biology
- Publisher
- Informa UK Limited
- Published
- 2013-01-01
- Volume
- 33
- Issue
- 2
- Pages
- 387-395
- ISSN
- 0270-7306 (ISSN-L)
- 1098-5549
- PMC
- PMC3554112
- OpenAlex
- W2098812676
- Cited by
- 207
- References
- 42
- Citations by year
- 2026: 10 · 2025: 8 · 2024: 8 · 2023: 21 · 2022: 14 · 2021: 22 · 2020: 16 · 2019: 19 · 2018: 22 · 2017: 8 · 2016: 21 · 2015: 13 · 2014: 14 · 2013: 9
- FWCI
- 4.76
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Molecular and Cellular Biology (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- U.S. Public Health Service
- National Cancer Institute (R01CA107640, R01CA169306, CA107640, P30CA008748)
- 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
- RAD51 paralogs, homologous recombination, BRCA1, BRCA2, RAD52, epistasis, synthetic lethality, DNA damage response, genome stability
- MeSH terms
- Cell Line, DNA Damage, DNA-Binding Proteins, Epistasis, Genetic, Humans, Microscopy, Confocal, BRCA2 Protein, Ubiquitin-Protein Ligases, Rad51 Recombinase, Rad52 DNA Repair and Recombination Protein, Homologous Recombination, MCF-7 Cells
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