Evidence map›Paper›PMID 34654750›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2021

The low-complexity domain of the FUS RNA binding protein self-assembles via the mutually exclusive use of two distinct cross-β cores.

Masato Kato, Steven L McKnight

Open access · hybridAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
2.4field-weighted citation impact, top 10% of its field
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

30 citing papers in PubMed, 40 citations in OpenAlex.

  1. Review
  2. Article
  3. The Polymers of Life: Exploring Cellular Function Through Polymer Concepts.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Review
  4. Droplet growth, Ostwald's rule, and emergence of order in Fused in Sarcoma.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
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  11. Article
  12. International journal of molecular sciences · 2024
    Article
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors at 2 institutions in 2 countries.

Masato KatoDepartment of Biochemistry, University of Texas Southwestern Medical Center, Dallas, TX 75390; Steven.McKnight@UTSouthwestern.edu masato.kato@utsouthwestern.edu.ORCID 0000-0001-8437-6248
Steven L McKnightDepartment of Biochemistry, University of Texas Southwestern Medical Center, Dallas, TX 75390; Steven.McKnight@UTSouthwestern.edu masato.kato@utsouthwestern.edu.ORCID 0000-0002-9014-9364
National Institutes for Quantum Science and Technology · JPThe University of Texas Southwestern Medical Center · US

Funding

Targeting EWSR1-FLI1 through Functional, Structural and Chemical ApproachesU54CA231649 · NCI · UT SOUTHWESTERN MEDICAL CENTER · PI AMATRUDA, JAMES F, MCFADDEN, DAVID GLENN · 2019 to 2019
$10.0M
A solid state conceptualization of information transfer from gene to message to proteinR35GM130358 · NIGMS · UT SOUTHWESTERN MEDICAL CENTER · PI STEVEN L MCKNIGHT · 2019 to 2026
$4.0M
TEM for UT Southwestern Electron Microscopy Core FacilityS10OD021685 · OD · UT SOUTHWESTERN MEDICAL CENTER · PI LUBY-PHELPS, KATHERINE J · 2017 to 2017
$398k
NCI NIH HHS U54 CA231649NIGMS NIH HHS R35 GM130358NIH HHS S10 OD021685
6 · The paper itself

Abstract

The low-complexity (LC) domain of the fused in sarcoma (FUS) RNA binding protein self-associates in a manner causing phase separation from an aqueous environment. Incubation of the FUS LC domain under physiologically normal conditions of salt and pH leads to rapid formation of liquid-like droplets that mature into a gel-like state. Both examples of phase separation have enabled reductionist biochemical assays allowing discovery of an N-terminal region of 57 residues that assembles into a labile, cross-β structure. Here we provide evidence of a nonoverlapping, C-terminal region of the FUS LC domain that also forms specific cross-β interactions. We propose that biologic function of the FUS LC domain may operate via the mutually exclusive use of these N- and C-terminal cross-β cores. Neurodegenerative disease-causing mutations in the FUS LC domain are shown to imbalance the two cross-β cores, offering an unanticipated concept of LC domain function and dysfunction.

Indexed as

Protein DomainsAmino Acid SubstitutionAmyotrophic Lateral SclerosisHumansHydrogelsRNA-Binding Protein FUSHydrogelsRNA-Binding Protein FUSALS mutationcross-beta polymerFUSlow-complexity sequenceneurodegenerative disease

Identifiers

PMID34654750
PMCPMC8545455
OpenAlexW3207532595

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
Read underepoch 390

Registered trials

None linked

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.