ArticleBiochemistry2021
Glycine-Rich Peptides from FUS Have an Intrinsic Ability to Self-Assemble into Fibers and Networked Fibrils.
Article in Biochemistry, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed, 49 citations in OpenAlex.
- PolyProline Predictor: A web server for empirical sequence-based prediction of polyproline II helices.Protein science : a publication of the Protein Society · 2026Article
- Shoebill: an interpretable AlphaFold2-informed predictor of protein crystallization propensity using XGBoost.Briefings in bioinformatics · 2026Article
- Oligomerization enables the selective targeting of an intrinsically disordered region by a small molecule.Science advances · 2026Article
- Sequence-Dependent Heterotypic Assemblies of Intrinsically Disordered Peptides.ChemistryEurope · 2026Article
- The Glycine-Rich Region as a Flexible Molecular Glue Promoting hPrPJournal of chemical information and modeling · 2025Article
- Selective engineering of condensation properties of single-stranded DNA binding (SSB) protein via its intrinsically disordered linker region.Nucleic acids research · 2025Article
- Synapsin Condensation is Governed by Sequence-Encoded Molecular Grammars.Journal of molecular biology · 2025Article
- Backbone-mediated weakening of pairwise interactions enables percolation in peptide-based mimics of protein condensates.Communications chemistry · 2025Article
- The mechanobiology of biomolecular condensates.Biophysics reviews · 2025Review
- Phase separation and ageing of glycine-rich protein from tick adhesive.Nature chemistry · 2025Article
- Direct computations of viscoelastic moduli of biomolecular condensates.The Journal of chemical physics · 2024Article
- Protein structure-function continuum model: Emerging nexuses between specificity, evolution, and structure.Protein science : a publication of the Protein Society · 2024Review
- Labile assembly of a tardigrade protein induces biostasis.Protein science : a publication of the Protein Society · 2024Article
- Ensemble structure of the N-terminal domain (1-267) of FUS in a biomolecular condensate.Biophysical journal · 2024Article
- Growth kinetics of amyloid-like fibrils: An integrated atomistic simulation and continuum theory approach.PNAS nexus · 2024Article
- Back in time to the Gly-rich prototype of the phosphate binding elementary function.Current research in structural biology · 2024Review
- Phase separation of protein mixtures is driven by the interplay of homotypic and heterotypic interactions.Nature communications · 2023Article
- Minimum information guidelines for experiments structurally characterizing intrinsically disordered protein regions.Nature methods · 2023Review
- Sequence variations of phase-separating proteins and resources for studying biomolecular condensates.Acta biochimica et biophysica Sinica · 2023Review
- Phase Separation in Mixtures of Prion-Like Low Complexity Domains is Driven by the Interplay of Homotypic and Heterotypic Interactions.Research square · 2023Article
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
Glycine-rich regions feature prominently in intrinsically disordered regions (IDRs) of proteins that drive phase separation and the regulated formation of membraneless biomolecular condensates. Interestingly, the Gly-rich IDRs seldom feature poly-Gly tracts. The protein fused in sarcoma (FUS) is an exception. This protein includes two 10-residue poly-Gly tracts within the prion-like domain (PLD) and at the interface between the PLD and the RNA binding domain. Poly-Gly tracts are known to be highly insoluble, being potent drivers of self-assembly into solid-like fibrils. Given that the internal concentrations of FUS and FUS-like molecules cross the high micromolar and even millimolar range within condensates, we reasoned that the intrinsic insolubility of poly-Gly tracts might be germane to emergent fluid-to-solid transitions within condensates. To assess this possibility, we characterized the concentration-dependent self-assembly for three non-overlapping 25-residue Gly-rich peptides derived from FUS. Two of the three peptides feature 10-residue poly-Gly tracts. These peptides form either long fibrils based on twisted ribbon-like structures or self-supporting gels based on physical cross-links of fibrils. Conversely, the peptide with similar Gly contents but lacking a poly-Gly tract does not form fibrils or gels. Instead, it remains soluble across a wide range of concentrations. Our findings highlight the ability of poly-Gly tracts within IDRs that drive phase separation to undergo self-assembly. We propose that these tracts are likely to contribute to nucleation of fibrillar solids within dense condensates formed by FUS.
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