ArticleCellular and molecular life sciences : CMLS2024
Crucial role of the NSE1 RING domain in Smc5/6 stability and FANCM-independent fork progression.
Article in Cellular and molecular life sciences : CMLS, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed.
- The Multifunctional SMC5/6 Complex in Genome Stability, Antiviral Restriction, and Human Disease.Current issues in molecular biology · 2026Review
- Candidate genes related to growth and milk production in three Anatolian goats revealed by GWAS.Mammalian genome : official journal of the International Mammalian Genome Society · 2026Article
- Assessing SMC Complex Function in Replication Fork Progression with DNA Fiber Assays.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Separation-of-Function Alleles ofBiomolecules · 2025Article
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14 authors.
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Abstract
The Smc5/6 complex is a highly conserved molecular machine involved in the maintenance of genome integrity. While its functions largely depend on restraining the fork remodeling activity of Mph1 in yeast, the presence of an analogous Smc5/6-FANCM regulation in humans remains unknown. We generated human cell lines harboring mutations in the NSE1 subunit of the Smc5/6 complex. Point mutations or truncations in the RING domain of NSE1 result in drastically reduced Smc5/6 protein levels, with differential contribution of the two zinc-coordinating centers in the RING. In addition, nse1-RING mutant cells display cell growth defects, reduced replication fork rates, and increased genomic instability. Notably, our findings uncover a synthetic sick interaction between Smc5/6 and FANCM and show that Smc5/6 controls fork progression and chromosome disjunction in a FANCM-independent manner. Overall, our study demonstrates that the NSE1 RING domain plays vital roles in Smc5/6 complex stability and fork progression through pathways that are not evolutionary conserved.
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