ArticleMolecular cell2015
Residue-by-Residue View of In Vitro FUS Granules that Bind the C-Terminal Domain of RNA Polymerase II.
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 576 papers.
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Who cites it
576 citing papers in PubMed.
- Engineering short-sequence elements for condensate-like assemblies by de novo design.Synthetic and systems biotechnology · 2027Article
- A practical guide to investigating biomolecular condensates: a comment from the plant community.Science China. Life sciences · 2026Review
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- Designed IDPs phase separate and mix or demix according to sequence designed parameters.bioRxiv : the preprint server for biology · 2026Article
- Phase Separation of SF3B1 Serves as a Critical Post-Transcriptional Regulator During Early Mouse Embryogenesis.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Valosin-containing protein counteracts ATP-driven dissolution of FUS condensates through its ATPase activity in vitro.FEBS letters · 2026Article
- Communication is key: combinatorial phosphorylation and functional cross-talk in the RNA polymerase II CTD code.Biochemical Society transactions · 2026Review
- Review
- Hydration free energy is an incomplete predictor of globular protein incorporation into condensates.Biophysical journal · 2026Article
- Structural Control of Dual Emission in Coumarin Fluorophores for Visualizing Protein Droplet Maturation.Angewandte Chemie (International ed. in English) · 2026Article
- Opposing roles of serine and charge in IDR condensate miscibility.Nature chemical biology · 2026Article
- Programmable Multiphasic Condensates Formed via Evaporation-Induced Phase Separation of Minimal Peptide Model.Advanced materials (Deerfield Beach, Fla.) · 2026Article
- Redox-Dependent Chaperoning of GBF1 Condensates Regulates Seed Germination in Arabidopsis.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Liquid-Liquid Phase Separation (LLPS) in Tumor Biology: Special Focus on the Process of Transcription.International journal of molecular sciences · 2026Review
- Topological Entanglement in Intrinsically Disordered Proteins: Sequence, Structural, and Functional Determinants.The journal of physical chemistry. B · 2026Article
- Interplay of Noncovalent Interactions in Phase Separation Mediated by Tyrosine-Rich and Arginine-Rich Polypeptides.Journal of the American Chemical Society · 2026Article
- Maintenance of H3K9me2 heterochromatin in the pollen vegetative nucleus requires ARID1 nuclear body formation.The Plant journal : for cell and molecular biology · 2026Article
- Sequence-encoded conformational biases correlate with self-assembly modes of intrinsically disordered proteins.PNAS nexus · 2026Article
- RNA G-quadruplexes function as a tunable switch of FUS phase separation.Nucleic acids research · 2026Article
- The Effect of Protein Tagging on Aggregation and Phase Separation.Journal of cellular biochemistry · 2026Review
516 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
Phase-separated states of proteins underlie ribonucleoprotein (RNP) granules and nuclear RNA-binding protein assemblies that may nucleate protein inclusions associated with neurodegenerative diseases. We report that the N-terminal low-complexity domain of the RNA-binding protein Fused in Sarcoma (FUS LC) is structurally disordered and forms a liquid-like phase-separated state resembling RNP granules. This state directly binds the C-terminal domain of RNA polymerase II. Phase-separated FUS lacks static structures as probed by fluorescence microscopy, indicating they are distinct from both protein inclusions and hydrogels. We use solution nuclear magnetic resonance spectroscopy to directly probe the dynamic architecture within FUS liquid phase-separated assemblies. Importantly, we find that FUS LC retains disordered secondary structure even in the liquid phase-separated state. Therefore, we propose that disordered protein granules, even those made of aggregation-prone prion-like domains, are dynamic and disordered molecular assemblies with transiently formed protein-protein contacts.
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