ArticleNature communications2023
Pharmacological perturbation of the phase-separating protein SMNDC1.
Article in Nature communications, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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The trial behind it
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Who cites it
9 citing papers in PubMed, 13 citations in OpenAlex.
- Transfer RNA-Derived Small RNA-5'tiRNAGln Drives HNRNPC Phase Separation to Promote Breast Cancer Bone Metastasis by Regulating IGF1R.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Small molecule splicing modulators that disrupt O-GlcNAc homeostasis.Nature communications · 2026Article
- Alternative Splicing: Molecular Mechanisms, Biological Functions, Diseases, and Potential Therapeutic Targets.MedComm · 2025Review
- hnRNPL phase separation activates PIK3CB transcription and promotes glycolysis in ovarian cancer.Nature communications · 2025Article
- Splicing regulation through biomolecular condensates and membraneless organelles.Nature reviews. Molecular cell biology · 2024Review
- An autoregulatory poison exon in Smndc1 is conserved across kingdoms and influences organism growth.PLoS genetics · 2024Article
- SART3 reads methylarginine-marked glycine- and arginine-rich motifs.Cell reports · 2024Article
- Loss of the methylarginine reader function of SND1 confers resistance to hepatocellular carcinoma.The Biochemical journal · 2023Article
- Pharmacological perturbation of the phase-separating protein SMNDC1.Nature communications · 2023Article
Corrections and comments
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Authors and funding
18 authors at 2 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
SMNDC1 is a Tudor domain protein that recognizes di-methylated arginines and controls gene expression as an essential splicing factor. Here, we study the specific contributions of the SMNDC1 Tudor domain to protein-protein interactions, subcellular localization, and molecular function. To perturb the protein function in cells, we develop small molecule inhibitors targeting the dimethylarginine binding pocket of the SMNDC1 Tudor domain. We find that SMNDC1 localizes to phase-separated membraneless organelles that partially overlap with nuclear speckles. This condensation behavior is driven by the unstructured C-terminal region of SMNDC1, depends on RNA interaction and can be recapitulated in vitro. Inhibitors of the protein's Tudor domain drastically alter protein-protein interactions and subcellular localization, causing splicing changes for SMNDC1-dependent genes. These compounds will enable further pharmacological studies on the role of SMNDC1 in the regulation of nuclear condensates, gene regulation and cell identity.
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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.