ArticleMolecular cell2015
A specific LSD1/KDM1A isoform regulates neuronal differentiation through H3K9 demethylation.
Article in Molecular cell, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 159 papers.
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159 citing papers in PubMed, 278 citations in OpenAlex.
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- The multifaceted role of post-translational modifications of LSD1 in cellular processes and disease pathogenesis.Genes & diseases · 2025Review
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- Current advances and future directions in targeting histone demethylases for cancer therapy.Molecules and cells · 2025Review
- Coordinated neuron-specific splicing events restrict nucleosome engagement of the LSD1 histone demethylase complex.Cell reports · 2025Article
- Discovery and structural studies of histone demethylases.Frontiers in epigenetics and epigenomics · 2025Review
- Cooperative role of LSD1 and CHD7 in regulating differentiation of mouse embryonic stem cells.Scientific reports · 2024Article
- Discover QTLs for the level of blood components in Shaoxing duck using GWAS and haplotype sharing analysis.Animal biotechnology · 2024Article
- Combined small-molecule treatment accelerates maturation of human pluripotent stem cell-derived neurons.Nature biotechnology · 2024Article
- Article
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- Emerging Functional Connections Between Metabolism and Epigenetic Remodeling in Neural Differentiation.Molecular neurobiology · 2024Review
- SAMD1 suppresses epithelial-mesenchymal transition pathways in pancreatic ductal adenocarcinoma.PLoS biology · 2024Article
- Anticancer Drugs of Lysine Specific Histone Demethylase-1 (LSD1) Display Variable Inhibition on Nucleosome Substrates.Biochemistry · 2024Article
99 more citing papers are in PubMed but not listed here.
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Authors and funding
12 authors at 5 institutions in 2 countries.
Funding
Abstract
Lysine-specific demethylase 1 (LSD1) has been reported to repress and activate transcription by mediating histone H3K4me1/2 and H3K9me1/2 demethylation, respectively. The molecular mechanism that underlies this dual substrate specificity has remained unknown. Here we report that an isoform of LSD1, LSD1+8a, does not have the intrinsic capability to demethylate H3K4me2. Instead, LSD1+8a mediates H3K9me2 demethylation in collaboration with supervillin (SVIL), a new LSD1+8a interacting protein. LSD1+8a knockdown increases H3K9me2, but not H3K4me2, levels at its target promoters and compromises neuronal differentiation. Importantly, SVIL co-localizes to LSD1+8a-bound promoters, and its knockdown mimics the impact of LSD1+8a loss, supporting SVIL as a cofactor for LSD1+8a in neuronal cells. These findings provide insight into mechanisms by which LSD1 mediates H3K9me demethylation and highlight alternative splicing as a means by which LSD1 acquires selective substrate specificities (H3K9 versus H3K4) to differentially control specific gene expression programs in neurons.
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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.