ArticleProceedings of the National Academy of Sciences of the United States of America2022
CCAR2 functions downstream of the Shieldin complex to promote double-strand break end-joining.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 15 citations in OpenAlex.
- Article
- Unraveling syndrome-driven osteosarcoma: genetic insights and therapeutic frontiers.Orphanet journal of rare diseases · 2026Review
- Circadian regulation of homologous recombination by cryptochrome1-mediated dampening of DNA end resection.Nature communications · 2025Article
- De novo detection of somatic variants in high-quality long-read single-cell RNA sequencing data.Genome research · 2025Article
- Tissue Factor Pathway Inhibitor 2 Enhances Hepatocellular Carcinoma Chemosensitivity by Activating CCAR2-GADD45A-Mediated DNA Damage Repair.International journal of biological sciences · 2025Article
- De novo detection of somatic variants in high-quality long-read single-cell RNA sequencing data.bioRxiv : the preprint server for biology · 2024Article
- The splicing factor CCAR1 regulates the Fanconi anemia/BRCA pathway.Molecular cell · 2024Article
- Multifaceted roles of CCAR family proteins in the DNA damage response and cancer.Experimental & molecular medicine · 2024Review
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Authors and funding
9 authors at 1 institution in 1 country.
Funding
Abstract
The 53BP1-RIF1 pathway restricts the resection of DNA double-strand breaks (DSBs) and promotes blunt end-ligation by non-homologous end joining (NHEJ) repair. The Shieldin complex is a downstream effector of the 53BP1-RIF1 pathway. Here, we identify a component of this pathway, CCAR2/DBC1, which is also required for restriction of DNA end-resection. CCAR2 co-immunoprecipitates with the Shieldin complex, and knockout of CCAR2 in a BRCA1-deficient cell line results in elevated DSB end-resection, RAD51 loading, and PARP inhibitor (PARPi) resistance. Knockout of CCAR2 is epistatic with knockout of other Shieldin proteins. The S1-like RNA-binding domain of CCAR2 is required for its interaction with the Shieldin complex and for suppression of DSB end-resection. CCAR2 functions downstream of the Shieldin complex, and CCAR2 knockout cells have delayed resolution of Shieldin complex foci. Forkhead-associated (FHA)-dependent targeting of CCAR2 to DSB sites re-sensitized BRCA1-/-SHLD2-/- cells to PARPi. Taken together, CCAR2 is a functional component of the 53BP1-RIF1 pathway, promotes the refill of resected DSBs, and suppresses homologous recombination.
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