ArticleNucleic acids research2016
Dimerization of SLX4 contributes to functioning of the SLX4-nuclease complex.
Article in Nucleic acids research, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 19 citations in OpenAlex.
- GWAS reveals common SLX4 variants associated with telomere length and hypertension in individuals of African ancestry.Genes & genomics · 2026Article
- Non-covalent SUMO interactions with ligases and effectors: SUMO-interacting motifs and beyond.Essays in biochemistry · 2025Review
- Omics-Based Characterization of BTB Gene Family in T. aestivum, Reveals the Potential of TaBTB11/56/57/58 in Combined Heat and Drought Stress Regulation.Rice (New York, N.Y.) · 2025Article
- In silico analysis of several frequent SLX4 mutations appearing in human cancers.microPublication biology · 2024Article
- Landscape of genetic variants in sporadic meningiomas captured with clinical genomics.Acta neurochirurgica · 2022Article
- Coordinated roles of SLX4 and MutSβ in DNA repair and the maintenance of genome stability.Critical reviews in biochemistry and molecular biology · 2021Review
- Exploring the Structures and Functions of Macromolecular SLX4-Nuclease Complexes in Genome Stability.Frontiers in genetics · 2021Review
- SLX4 interacts with RTEL1 to prevent transcription-mediated DNA replication perturbations.Nature structural & molecular biology · 2020Article
- Saccharomyces cerevisiae Mus81-Mms4 prevents accelerated senescence in telomerase-deficient cells.PLoS genetics · 2020Article
- Review
- The role of SLX4 and its associated nucleases in DNA interstrand crosslink repair.Nucleic acids research · 2019Article
- Review
Corrections and comments
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Authors and funding
11 authors at 6 institutions in 2 countries.
Funding
Abstract
The Fanconi anemia protein SLX4 assembles a genome and telomere maintenance toolkit, consisting of the nucleases SLX1, MUS81 and XPF. Although it is known that SLX4 acts as a scaffold for building this complex, the molecular basis underlying this function of SLX4 remains unclear. Here, we report that functioning of SLX4 is dependent on its dimerization via an oligomerization motif called the BTB domain. We solved the crystal structure of the SLX4BTB dimer, identifying key contacts (F681 and F708) that mediate dimerization. Disruption of BTB dimerization abrogates nuclear foci formation and telomeric localization of not only SLX4 but also of its associated nucleases. Furthermore, dimerization-deficient SLX4 mutants cause defective cellular response to DNA interstrand crosslinking agent and telomere maintenance, underscoring the contribution of BTB domain-mediated dimerization of SLX4 in genome and telomere maintenance.
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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.