ArticleScience advances2024
Growth factor-induced activation of MSK2 leads to phosphorylation of H3K9me2S10 and corresponding changes in gene expression.
Article in Science advances, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed, 6 citations in OpenAlex.
- Antibody-trapping presents a widespread pitfall for microscopy and genomics in the nucleus.Nucleic acids research · 2026Article
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- Immune activation of primary human macrophages is suppressed by the coordinated action ofmBio · 2026Article
- Fucoidan as a renal protectant: mechanistic insights and therapeutic implications of endothelial glycocalyx targeting.Frontiers in pharmacology · 2026Review
- Inside-out integrin activation is essential for early mammalian development.Molecular biology of the cell · 2025Article
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Authors and funding
8 authors at 1 institution in 1 country.
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Abstract
Extracellular signals are transmitted through kinase cascades to modulate gene expression, but it remains unclear how epigenetic changes regulate this response. Here, we provide evidence that growth factor-stimulated changes in the transcript levels of many responsive genes are accompanied by increases in histone phosphorylation levels, specifically at histone H3 serine-10 when the adjacent lysine-9 is dimethylated (H3K9me2S10). Imaging and proteomic approaches show that epidermal growth factor (EGF) stimulation results in H3K9me2S10 phosphorylation, which occurs in genomic regions enriched for regulatory enhancers of EGF-responsive genes. We also demonstrate that the EGF-induced increase in H3K9me2S10ph is dependent on the nuclear kinase MSK2, and this subset of EGF-induced genes is dependent on MSK2 for transcription. Together, our work indicates that growth factor-induced changes in chromatin state can mediate the activation of downstream genes.
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Registered trials
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