The DOI matches its Crossref record; 11 of the 11 references it cites were found in a registry or an index.
PALB2 Links BRCA1 and BRCA2 in the DNA-Damage Response
Open accessAbstract
Summary BRCA1 and BRCA2 are often mutated in familial breast and ovarian cancer. Both tumor suppressors play key roles in the DNA-damage response [1, 2]. However, it remains unclear whether these two tumor suppressor function together in the same DNA-damage response pathway. Here, we show that BRCA1 associates with BRCA2 through PALB2/FANCN, a major binding partner of BRCA2 [3]. The interaction between BRCA1 and BRCA2 is abrogated in PALB2-deficient Fanconi anemia cells and in the cells depleted of PALB2 by small interfering RNA. Moreover, we show that BRCA1 promotes the concentration of PALB2 and BRCA2 at DNA-damage sites and the interaction between BRCA1 and PALB2 is important for the homologous recombination repair. Taken together, our results indicate that BRCA1 is an upstream regulator of BRCA2 in the DNA-damage response, and PALB2 is the linker between BRCA1 and BRCA2.
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Cites
Brca1 Controls Homology-Directed DNA Repair
Moynahan, M. E., Chiu, J. W., Koller, B. H., & Jasin, M. (1999) · Molecular Cell · doi:10.1016/s1097-2765(00)80202-6 · Cited by 1,245
Biallelic Inactivation of BRCA2 in Fanconi Anemia
Howlett, N. G., Taniguchi, T., Olson, S., Cox, B., Waisfisz, Q., de Die-Smulders, C., Persky, N., Grompe, M., Joenje, H., Pals, G., et al. (2002) · Science · doi:10.1126/science.1073834 · Cited by 1,149
Emergence of a DNA-damage response network consisting of Fanconi anaemia and BRCA proteins
Wang, W. (2007) · Nature Reviews Genetics · doi:10.1038/nrg2159 · Cited by 663
Biallelic mutations in PALB2 cause Fanconi anemia subtype FA-N and predispose to childhood cancer
Reid, S., Schindler, D., Hanenberg, H., Barker, K., Hanks, S., Kalb, R., Neveling, K., Kelly, P., Seal, S., Freund, M., et al. (2007) · Nature Genetics · doi:10.1038/ng1947 · Cited by 642
Fanconi anemia is associated with a defect in the BRCA2 partner PALB2
Xia, B., Dorsman, J. C., Ameziane, N., de Vries, Y., Rooimans, M. A., Sheng, Q., Pals, G., Errami, A., Gluckman, E., Llera, J., et al. (2007) · Nature Genetics · doi:10.1038/ng1942 · Cited by 465
Self-citationThe DNA helicase BRIP1 is defective in Fanconi anemia complementation group J
Levitus, M., Waisfisz, Q., Godthelp, B. C., Vries, Y. D., Hussain, S., Wiegant, W. W., Elghalbzouri-Maghrani, E., Steltenpool, J., Rooimans, M. A., Pals, G., et al. (2005) · Nature Genetics · doi:10.1038/ng1625 · Cited by 432
Litman, R., Peng, M., Jin, Z., Zhang, F., Zhang, J., Powell, S., Andreassen, P. R., & Cantor, S. B. (2005) · Cancer Cell · doi:10.1016/j.ccr.2005.08.004 · Cited by 396
Self-citationThe BRCA1-interacting helicase BRIP1 is deficient in Fanconi anemia
Levran, O., Attwooll, C., Henry, R. T., Milton, K. L., Neveling, K., Rio, P., Batish, S. D., Kalb, R., Velleuer, E., Barral, S., et al. (2005) · Nature Genetics · doi:10.1038/ng1624 · Cited by 370
Genetic Analysis of BRCA1 Function in a Defined Tumor Cell Line
Scully, R., Ganesan, S., Vlasakova, K., Chen, J., Socolovsky, M., & Livingston, D. M. (1999) · Molecular Cell · doi:10.1016/s1097-2765(00)80238-5 · Cited by 359
Cantor, S., Drapkin, R., Zhang, F., Lin, Y., Han, J., Pamidi, S., & Livingston, D. M. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0308717101 · Cited by 240
Self-citation
Cited by
Playing the End Game: DNA Double-Strand Break Repair Pathway Choice
Chapman, J. R., Taylor, M. R. G., & Boulton, S. J. (2012) · Molecular Cell · doi:10.1016/j.molcel.2012.07.029 · Cited by 1,625
Dynamics of DNA damage response proteins at DNA breaks: a focus on protein modifications
Polo, S. E., & Jackson, S. P. (2011) · Genes & Development · doi:10.1101/gad.2021311 · Cited by 1,092
Mitotic homologous recombination maintains genomic stability and suppresses tumorigenesis
Moynahan, M. E., & Jasin, M. (2010) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2851 · Cited by 930
Homologous Recombination and Human Health: The Roles of BRCA1, BRCA2, and Associated Proteins
Prakash, R., Zhang, Y., Feng, W., & Jasin, M. (2015) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a016600 · Cited by 869
Breast-Cancer Risk in Families with Mutations in PALB2
Antoniou, A. C., Casadei, S., Heikkinen, T., Barrowdale, D., Pylkäs, K., Roberts, J., Lee, A., Subramanian, D., De Leeneer, K., Fostira, F., et al. (2014) · New England Journal of Medicine · doi:10.1056/nejmoa1400382 · Cited by 851
Metadata
- Authors
- Zhang, F., Ma, J., Wu, J., Ye, L., Cai, H., Xia, B., & Yu, X.
- Venue
- Current Biology
- Publisher
- Elsevier BV
- Published
- 2009-03
- Volume
- 19
- Issue
- 6
- Pages
- 524-529
- ISSN
- 0960-9822 (ISSN-L)
- OpenAlex
- W1969513645
- Cited by
- 562
- References
- 11
- FWCI
- 11.64
- Type
- journal article
- Language
- en
- Open access
- bronze
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- Zhang, F., Ma, J., Wu, J., Ye, L., Cai, H., Xia, B., & Yu, X. (2009). PALB2 Links BRCA1 and BRCA2 in the DNA-Damage Response. Current Biology. https://doi.org/10.1016/j.cub.2009.02.018
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