The DOI matches its Crossref record; 35 of the 35 references it cites were found in a registry or an index.
PALB2 is an integral component of the BRCA complex required for homologous recombination repair
Open accessAbstract
Mutations in breast cancer susceptibility gene 1 and 2 ( BRCA1 and BRCA2 ) predispose individuals to breast and ovarian cancer development. We previously reported an in vivo interaction between BRCA1 and BRCA2. However, the biological significance of their association is thus far undefined. Here, we report that PALB2, the partner and localizer of BRCA2, binds directly to BRCA1, and serves as the molecular scaffold in the formation of the BRCA1-PALB2-BRCA2 complex. The association between BRCA1 and PALB2 is primarily mediated via apolar bonding between their respective coiled-coil domains. More importantly, BRCA1 mutations identified in cancer patients disrupted the specific interaction between BRCA1 and PALB2. Consistent with the converging functions of the BRCA proteins in DNA repair, cells harboring mutations with abrogated BRCA1-PALB2 interaction resulted in defective homologous recombination (HR) repair. We propose that, via its direct interaction with PALB2, BRCA1 fine-tunes recombinational repair partly through its modulatory role in the PALB2-dependent loading of BRCA2-RAD51 repair machinery at DNA breaks. Our findings uncover PALB2 as the molecular adaptor between the BRCA proteins, and suggest that impaired HR repair is one of the fundamental causes for genomic instability and tumorigenesis observed in patients carrying BRCA1 , BRCA2 , or PALB2 mutations.
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PALB2, which encodes a BRCA2-interacting protein, is a breast cancer susceptibility gene
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Self-citationControl of BRCA2 Cellular and Clinical Functions by a Nuclear Partner, PALB2
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Abraxas and RAP80 Form a BRCA1 Protein Complex Required for the DNA Damage Response
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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
Structure and function of WD40 domain proteins
Xu, C., & Min, J. (2011) · Protein & Cell · doi:10.1007/s13238-011-1018-1 · Cited by 647
Metadata
- Authors
- Sy, S. M. H., Huen, M. S. Y., & Chen, J.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2009-04-28
- Volume
- 106
- Issue
- 17
- Pages
- 7155-7160
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2157570211
- Cited by
- 614
- References
- 35
- FWCI
- 12.96
- Type
- journal article
- Language
- en
- Open access
- green
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