ArticleDevelopmental cell2025
Co-essentiality analysis identifies PRR12 as a cohesin interacting protein and contributor to genomic integrity.
Article in Developmental cell, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- Conserved 3D genome reorganization during DNA repair.Life science alliance · 2026Review
- RNase MRP subunit composition and role in 40S ribosome biogenesis.Nature structural & molecular biology · 2026Article
- Cohesin in 3D: development, differentiation, and disease.Genes & development · 2025Review
- Transcription factors form a ternary complex with NIPBL/MAU2 to localize cohesin at enhancers.Nucleic acids research · 2025Article
- Molecular determinants of RNase MRP specificity and function.bioRxiv : the preprint server for biology · 2025Article
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Authors and funding
3 authors.
Funding
Abstract
The cohesin complex is critical for genome organization and regulation, relying on specialized co-factors to mediate its diverse functional activities. Here, by analyzing patterns of similar gene requirements across cell lines, we identify PRR12 as a mediator of cohesin and genome integrity. We show that PRR12 interacts with NIPBL/MAU2 and the cohesin complex, and that the loss of PRR12 results in reduced cohesin localization and a substantial increase in DNA double-strand breaks in mouse NIH-3T3 cells. Additionally, PRR12 co-localizes with NIPBL to sites of DNA damage in a NIPBL and cohesin-dependent manner. We find that the requirement for PRR12 differs across cell lines, with human HeLa cells exhibiting reduced sensitivity to PRR12 loss compared with mouse NIH-3T3 cells, indicating context-specific roles. Together, our work identifies PRR12 as a regulator of cohesin and provides insight into how genome integrity is maintained across diverse cellular contexts.
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