ArticleProceedings of the National Academy of Sciences of the United States of America2015
Interplay among nucleosomal DNA, histone tails, and corepressor CoREST underlies LSD1-mediated H3 demethylation.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 59 papers.
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Who cites it
59 citing papers in PubMed, 112 citations in OpenAlex.
- Histone probes for reader and eraser investigations.Chemical science · 2025Review
- RCOR1 promotes myoblast differentiation and muscle regeneration.Cell death discovery · 2025Article
- Covalent adduct Grob fragmentation underlies LSD1 demethylase-specific inhibitor mechanism of action and resistance.Nature communications · 2025Article
- Uncoupling histone modification crosstalk by engineering lysine demethylase LSD1.Nature chemical biology · 2025Article
- Molecular Dynamics Simulations of Nucleosomes Containing Histone Variant H2A.J.International journal of molecular sciences · 2024Article
- The kinase NEK6 positively regulates LSD1 activity and accumulation in local chromatin sub-compartments.Communications biology · 2024Article
- Epigenetic modulation via the C-terminal tail of H2A.Z.Nature communications · 2024Article
- Anticancer Drugs of Lysine Specific Histone Demethylase-1 (LSD1) Display Variable Inhibition on Nucleosome Substrates.Biochemistry · 2024Article
- Comprehensive analysis of the REST transcription factor regulatory networks in IDH mutant and IDH wild-type glioma cell lines and tumors.Acta neuropathologica communications · 2024Article
- Evolution of lysine-specific demethylase 1 and REST corepressor gene families and their molecular interaction.Communications biology · 2023Article
- The Role of Selected Epigenetic Pathways in Cardiovascular Diseases as a Potential Therapeutic Target.International journal of molecular sciences · 2023Review
- Chromatin Sensing by the Auxiliary Domains of KDM5C Regulates Its Demethylase Activity and Is Disrupted by X-linked Intellectual Disability Mutations.Journal of molecular biology · 2023Article
- LSD1 inhibitors for cancer treatment: Focus on multi-target agents and compounds in clinical trials.Frontiers in pharmacology · 2023Review
- Role of primary aging hallmarks in Alzheimer´s disease.Theranostics · 2023Review
- A developmental role for the chromatin-regulating CoREST complex in the cnidarian Nematostella vectensis.BMC biology · 2022Article
- Fine-tuned KDM1A alternative splicing regulates human cardiomyogenesis through an enzymatic-independent mechanism.iScience · 2022Article
- Alternative Mechanisms for DNA Engagement by BET Bromodomain-Containing Proteins.Biochemistry · 2022Article
- Unveiling RCOR1 as a rheostat at transcriptionally permissive chromatin.Nature communications · 2022Article
- Histone demethylase Lsd1 is required for the differentiation of neural cells in Nematostella vectensis.Nature communications · 2022Article
- Functions and Interactions of Mammalian KDM5 Demethylases.Frontiers in genetics · 2022Review
Corrections and comments
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Authors and funding
11 authors at 4 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
With its noncatalytic domains, DNA-binding regions, and a catalytic core targeting the histone tails, LSD1-CoREST (lysine-specific demethylase 1; REST corepressor) is an ideal model system to study the interplay between DNA binding and histone modification in nucleosome recognition. To this end, we covalently associated LSD1-CoREST to semisynthetic nucleosomal particles. This enabled biochemical and biophysical characterizations of nucleosome binding and structural elucidation by small-angle X-ray scattering, which was extensively validated through binding assays and site-directed mutagenesis of functional interfaces. Our results suggest that LSD1-CoREST functions as an ergonomic clamp that induces the detachment of the H3 histone tail from the nucleosomal DNA to make it available for capture by the enzyme active site. The key notion emerging from these studies is the inherently competitive nature of the binding interactions because nucleosome tails, chromatin modifiers, transcription factors, and DNA represent sites for multiple and often mutually exclusive interactions.
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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.