ArticleOncogene2018
BRCA1 function in the intra-S checkpoint is activated by acetylation via a pCAF/SIRT1 axis.
Article in Oncogene, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
13 citing papers in PubMed, 21 citations in OpenAlex.
- Acetylation-dependent regulation of FOX-Ku interaction by GCN5-SIRT1 axis controls non-homologous end-joining DNA repair.Archives of pharmacal research · 2026Article
- All the Way: A Decade of SIRT1 in Breast Cancer.Biomedicines · 2026Review
- Post-Translational Modifications of Proteins Orchestrate All Hallmarks of Cancer.Life (Basel, Switzerland) · 2025Review
- Review
- Deacetylation of Transcription Factors in Carcinogenesis.International journal of molecular sciences · 2021Review
- SIRT2 promotes BRCA1-BARD1 heterodimerization through deacetylation.Cell reports · 2021Article
- Liquiritigenin decreases tumorigenesis by inhibiting DNMT activity and increasing BRCA1 transcriptional activity in triple-negative breast cancer.Experimental biology and medicine (Maywood, N.J.) · 2021Article
- SIRT6 Through the Brain Evolution, Development, and Aging.Frontiers in aging neuroscience · 2021Article
- NOTCH1 activation compensates BRCA1 deficiency and promotes triple-negative breast cancer formation.Nature communications · 2020Article
- Molecular contribution of BRCA1 and BRCA2 to genome instability in breast cancer patients: review of radiosensitivity assays.Biological procedures online · 2020Review
- Systematic bromodomain protein screens identify homologous recombination and R-loop suppression pathways involved in genome integrity.Genes & development · 2019Article
- Updates on the epigenetic roles of sirtuins.Current opinion in chemical biology · 2019Review
- BRCA1 represses DNA replication initiation through antagonizing estrogen signaling and maintains genome stability in parallel with WEE1-MCM2 signaling during pregnancy.Human molecular genetics · 2019Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Breast cancer associated gene 1 (BRCA1) function has been shown to be regulated by phosphorylation but the role of acetylation has not been determined. Therefore, we tested whether BRCA1 can be acetylated by the acetyltransferases P300/CBP-associated factor (pCAF), GCN5, and p300. p300 exhibited the highest level of BRCA1 acetylation; however, there was also a decrease in the total level of BRCA1. Therefore, we focused on pCAF and GCN5 because they both acetylated BRCA1 without affecting BRCA1 expression. Further analysis indicated that the acetylated form of BRCA1 is deacetylated by wild-type (WT) SIRT1, but not deacetylase mutant SIRT1, suggesting that SIRT1 is a specific deacetylase of BRCA1. We demonstrated that lysine 830 of BRCA1 is a preferential acetylation site by pCAF and tested its function in embryonic stem (ES) cells by changing lysine 830 to arginine using a transcription activator-like effector nuclease (TALEN) system. After exposure to DNA damage-inducing UV radiation, the viability of BRCA1 K830R mutant cells is greater than the WT ES cells. Further analysis using additional cell lines indicated that the BRCA1 K830R mutation impairs the intra-S checkpoint. Also, checkpoint kinase 1 (CHK1) phosphorylation was less in K830R cells as compared with WT cells after UV exposure. These data suggest that acetylation of BRCA1 on lysine 830 activates BRCA1 function at the intra-S checkpoint after DNA damage.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.