ArticleiScience2026
HP1β recruits RING1A to ubiquitinate histone H2A for BRCA1-mediated resection of double-stand breaks.
Article in iScience, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
What it found
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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
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Who cites it
1 citing paper in PubMed.
- Exploiting DNA damage tolerance for precision oncology.Trends in cancer · 2026Review
Corrections and comments
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Authors and funding
14 authors.
Funding
Abstract
Efficient DNA double-strand break (DSB) repair by homologous recombination (HR), as initiated by BRCA1 recruitment orchestrated by histone and non-histone proteins, is critical to genome stability, replication, transcription, and cancer avoidance. Here we reveal Heterochromatin Protein1 beta (HP1β) promotes BRCA1 enrichment at DNA DSB sites in gene-rich regions, and this is impaired by HP1β depletion. We find that HP1β is specifically enriched at DSBs within gene-rich regions via its Chromo Shadow Domain (CSD) that interacts with both Chromatin Assembly Factor 1 and the RING1A ubiquitinase component of Polycomb Repressor Complex 1. The resulting protein complex facilitates BRCA1 recruitment by promoting H2A lysine 119 ubiquitination. Collective findings reveal a novel mechanism whereby HP1β interactions, mediated through its CSD of HP1β interaction with RING1A, promotes H2AK119 ubiquitination to facilitate BRCA1 recruitment and orchestrate efficient HR and CtIP-dependent DNA resection at DSB sites in gene-rich active chromatin.
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Registered trials
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