Evidence map›Paper›PMID 41238911›Full record

ArticleNature nanotechnology2026

Nanoscale domains govern local diffusion and ageing within fused-in-sarcoma condensates.

Guoming Gao, Emily R Sumrall, Nils G Walter

Abstract read
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In one paragraph

Article in Nature nanotechnology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

19 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Review
  5. The exchange dynamics of client molecules in biomolecular condensates.bioRxiv : the preprint server for biology · 2026
    Article
  6. Single-Molecule Dwell Times in Biomolecular Condensates.bioRxiv : the preprint server for biology · 2026
    Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Clustering within a single-component biomolecular condensate.bioRxiv : the preprint server for biology · 2025
    Article
  18. Review
  19. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

3 authors.

Guoming Gao *Biophysics Graduate Program, University of Michigan, Ann Arbor, MI, USA.ORCID http://orcid.org/0000-0001-6791-3902
Emily R Sumrall *Biophysics Graduate Program, University of Michigan, Ann Arbor, MI, USA.ORCID http://orcid.org/0000-0001-7789-4119
Nils G WalterCenter for RNA Biomedicine, University of Michigan, Ann Arbor, MI, USA. nwalter@umich.edu.ORCID http://orcid.org/0000-0002-7301-1275

Funding

The RNA nanomachines of the gene expression machinery dissected at the single molecule levelR35GM131922 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI NILS G WALTER · 2019 to 2026
$6.9M
National Science Foundation (NSF) DGE2241144NIGMS NIH HHS R35 GM131922U.S. Department of Health & Human Services | National Institutes of Health (NIH) GM131922U.S. Department of Health & Human Services | National Institutes of Health (NIH) NS097542
6 · The paper itself

Abstract

Biomolecular condensates regulate cellular physiology by sequestering and processing RNAs and proteins, yet how these processes are locally tuned within condensates remains unclear. Moreover, in neurodegenerative diseases such as amyotrophic lateral sclerosis, condensates undergo liquid-to-solid phase transitions, but capturing early intermediates in this process has been challenging. Here we present a surface multi-tethering approach to achieve intra-condensate single-molecule tracking of fluorescently labelled RNA and protein molecules within liquid-like condensates. Using RNA-binding protein fused-in-sarcoma as a model for condensates implicated in amyotrophic lateral sclerosis, we discover that RNA and protein diffusion is confined within distinct nanometre-scale domains, or nanodomains, which exhibit unique connectivity and chemical environments. The properties of these nanodomains are tunable by guest molecules. As condensates age, nanodomains reposition, facilitating fused-in-sarcoma fibrilization at the condensate surface, a process further enhanced by anti-amyotrophic lateral sclerosis drugs. Our findings demonstrate that nanodomain formation governs condensate function by modulating the residence time and spatial organization of constituent biomolecules, providing previously unattainable insights into condensate ageing and mechanisms underlying disease.

Indexed as

Biomolecular CondensatesRNARNA-Binding Protein FUSAmyotrophic Lateral SclerosisDiffusionHumansRNARNA-Binding Protein FUS

Identifiers

What OpenQuestion holds

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Registered trials

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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.