RNF168-mediated localization of BARD1 recruits the BRCA1-PALB2 complex to DNA damage
The BRCA1-PALB2-BRCA2-RAD51 (BRCA1-P) complex is well known to play a fundamental role in DNA repair, but how the complex recruitment is regulated is still a matter of interest. Here the authors reveal mechanistic insights into RNF168 activity being responsible for PALB2 recruitment, through BARD1-B...
| Main Authors: | , , , , , |
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| Format: | Article |
| Language: | English |
| Published: |
Nature Portfolio
2021-08-01
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| Series: | Nature Communications |
| Online Access: | https://doi.org/10.1038/s41467-021-25346-4 |
| _version_ | 1823970415664431104 |
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| author | John J. Krais Yifan Wang Pooja Patel Jayati Basu Andrea J. Bernhardy Neil Johnson |
| author_facet | John J. Krais Yifan Wang Pooja Patel Jayati Basu Andrea J. Bernhardy Neil Johnson |
| author_sort | John J. Krais |
| collection | DOAJ |
| description | The BRCA1-PALB2-BRCA2-RAD51 (BRCA1-P) complex is well known to play a fundamental role in DNA repair, but how the complex recruitment is regulated is still a matter of interest. Here the authors reveal mechanistic insights into RNF168 activity being responsible for PALB2 recruitment, through BARD1-BRCA1 during homologous recombination repair. |
| first_indexed | 2024-12-18T03:12:36Z |
| format | Article |
| id | doaj.art-c39dd0ce8b4f496a844c3e220df1fbac |
| institution | Directory Open Access Journal |
| issn | 2041-1723 |
| language | English |
| last_indexed | 2024-12-18T03:12:36Z |
| publishDate | 2021-08-01 |
| publisher | Nature Portfolio |
| record_format | Article |
| series | Nature Communications |
| spelling | doaj.art-c39dd0ce8b4f496a844c3e220df1fbac2022-12-21T21:22:59ZengNature PortfolioNature Communications2041-17232021-08-0112111210.1038/s41467-021-25346-4RNF168-mediated localization of BARD1 recruits the BRCA1-PALB2 complex to DNA damageJohn J. Krais0Yifan Wang1Pooja Patel2Jayati Basu3Andrea J. Bernhardy4Neil Johnson5Molecular Therapeutics Program, Fox Chase Cancer CenterMolecular Therapeutics Program, Fox Chase Cancer CenterMolecular Therapeutics Program, Fox Chase Cancer CenterBlood Cell Development and Function Program, Fox Chase Cancer CenterMolecular Therapeutics Program, Fox Chase Cancer CenterMolecular Therapeutics Program, Fox Chase Cancer CenterThe BRCA1-PALB2-BRCA2-RAD51 (BRCA1-P) complex is well known to play a fundamental role in DNA repair, but how the complex recruitment is regulated is still a matter of interest. Here the authors reveal mechanistic insights into RNF168 activity being responsible for PALB2 recruitment, through BARD1-BRCA1 during homologous recombination repair.https://doi.org/10.1038/s41467-021-25346-4 |
| spellingShingle | John J. Krais Yifan Wang Pooja Patel Jayati Basu Andrea J. Bernhardy Neil Johnson RNF168-mediated localization of BARD1 recruits the BRCA1-PALB2 complex to DNA damage Nature Communications |
| title | RNF168-mediated localization of BARD1 recruits the BRCA1-PALB2 complex to DNA damage |
| title_full | RNF168-mediated localization of BARD1 recruits the BRCA1-PALB2 complex to DNA damage |
| title_fullStr | RNF168-mediated localization of BARD1 recruits the BRCA1-PALB2 complex to DNA damage |
| title_full_unstemmed | RNF168-mediated localization of BARD1 recruits the BRCA1-PALB2 complex to DNA damage |
| title_short | RNF168-mediated localization of BARD1 recruits the BRCA1-PALB2 complex to DNA damage |
| title_sort | rnf168 mediated localization of bard1 recruits the brca1 palb2 complex to dna damage |
| url | https://doi.org/10.1038/s41467-021-25346-4 |
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