ArticleArchives of pharmacal research2026
Acetylation-dependent regulation of FOX-Ku interaction by GCN5-SIRT1 axis controls non-homologous end-joining DNA repair.
Article in Archives of pharmacal research, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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
0 citing papers in PubMed.
No citing paper in PubMed yet.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors.
Funding
Abstract
DNA double-strand breaks (DSBs) represent a major threat to genomic integrity. DSBs are primarily repaired through homologous recombination (HR) and non-homologous end-joining (NHEJ). The Ku complex, composed of XRCC5 and XRCC6, initiates NHEJ by binding to the DNA ends in DSBs. Our previous study demonstrated that FOXL2 regulates Ku availability through acetylation-dependent interaction; however, whether related mechanisms operate across other FOX family proteins and how these can be regulated in response to genotoxic stress remain unclear.In this study, we demonstrated that multiple FOX family members interact with XRCC5/6 and acetylation-dependently suppress NHEJ. GCN5 (KAT2A) promoted the acetylation of a conserved lysine residue within the forkhead domain, thereby enhancing FOX-Ku association and limiting Ku availability. In response to DNA damage, SIRT1 underwent SUMOylation at lysine 734, thereby promoting its nuclear accumulation through KPNA2/KPNA3-dependent import. Nuclear SIRT1 acted as a deacetylase and reversed FOX acetylation, thereby reducing FOX-Ku interaction and permitting NHEJ activation.The results of this study define a DNA damage-responsive GCN5-SIRT1 regulatory axis that modulates FOX acetylation, FOX-Ku interaction, and NHEJ activity. Our study extends FOXL2-centered findings and supports a shared, but context-dependent, DNA repair regulation-supporting mechanism involving multiple FOX proteins.
Indexed as
Identifiers
42322495What Socratic 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 Socratic graph.