ArticleNature communications2022
Structure of DNMT3B homo-oligomer reveals vulnerability to impairment by ICF mutations.
Article in Nature communications, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 20 citations in OpenAlex.
- Multidomain interaction governs the filamentous assembly of the dominant-negative DNMT3A R882H mutant.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Molecular basis for the inhibition of de novo DNA methylation by TCL1A.Nature communications · 2026Article
- A role of protein conformational dynamics in mammalian DNA methylation.Structural dynamics (Melville, N.Y.) · 2026Review
- ICF syndrome: An epigenetic paradigm for primary immunodeficiencies.Journal of human immunity · 2026Review
- Epigenetics-targeted drugs: current paradigms and future challenges.Signal transduction and targeted therapy · 2024Review
- Using human disease mutations to understand de novo DNA methyltransferase function.Biochemical Society transactions · 2024Review
- Molecular mechanisms for DNA methylation defects induced by ICF syndrome-linked mutations in DNMT3B.Protein science : a publication of the Protein Society · 2024Article
- Structural basis for the H2AK119ub1-specific DNMT3A-nucleosome interaction.Nature communications · 2024Article
- Structure-guided functional suppression of AML-associated DNMT3A hotspot mutations.Nature communications · 2024Article
- DNMT3B PWWP mutations cause hypermethylation of heterochromatin.EMBO reports · 2024Article
- Intrafamily heterooligomerization as an emerging mechanism of methyltransferase regulation.Epigenetics & chromatin · 2024Review
- The epigenetic modification of DNA methylation in neurological diseases.Frontiers in immunology · 2024Review
- Evaluation of Clinical and Immunological Alterations Associated with ICF Syndrome.Journal of clinical immunology · 2023Article
- Structural basis for the allosteric regulation and dynamic assembly of DNMT3B.Nucleic acids research · 2023Article
- Article
- Epigenetic Targets in Schizophrenia Development and Therapy.Brain sciences · 2023Review
- Three's a crowd - why did three N-terminal methyltransferases evolve for one job?Journal of cell science · 2023Article
Corrections and comments
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Authors and funding
12 authors at 2 institutions in 1 country.
Funding
Abstract
DNA methyltransferase DNMT3B plays an essential role in establishment of DNA methylation during embryogenesis. Mutations of DNMT3B are associated with human diseases, notably the immunodeficiency, centromeric instability and facial anomalies (ICF) syndrome. How ICF mutations affect DNMT3B activity is not fully understood. Here we report the homo-oligomeric structure of DNMT3B methyltransferase domain, providing insight into DNMT3B-mediated DNA methylation in embryonic stem cells where the functional regulator DNMT3L is dispensable. The interplay between one of the oligomer interfaces (FF interface) and the catalytic loop renders DNMT3B homo-oligomer a conformation and activity distinct from the DNMT3B-DNMT3L heterotetramer, and a greater vulnerability to certain ICF mutations. Biochemical and cellular analyses further reveal that the ICF mutations of FF interface impair the DNA binding and heterochromatin targeting of DNMT3B, leading to reduced DNA methylation in cells. Together, this study provides a mechanistic understanding of DNMT3B-mediated DNA methylation and its dysregulation in disease.
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