Evidence map›Paper›PMID 40975059›Full record

ArticleMolecular cell2025

Matrin-3 forms spherical and wormlike assemblies that are modulated by RNA binding and ALS/FTD-associated mutations.

Macy L Sprunger, Min Kyung Shinn, Sabrina K Talir, Ken Lee, Rohit V Pappu, Meredith E Jackrel

Abstract read
In one paragraph

Article in Molecular cell, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing 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

8 citing papers in PubMed.

  1. α-Synuclein Forms Distinct Micelle-Like Assemblies at Low Ionic Strengths.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Article
  2. Distinguishing near- versus off-critical phase behaviors of intrinsically disordered proteins.Reports on progress in physics. Physical Society (Great Britain) · 2026
    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

6 authors.

Macy L SprungerDepartment of Chemistry, Washington University, St. Louis, MO 63130, USA.
Min Kyung ShinnDepartment of Biomedical Engineering, Washington University, St. Louis, MO 63130, USA; Center for Biomolecular Condensates, James McKelvey School of Engineering, St. Louis, MO 63130, USA.
Sabrina K TalirDepartment of Chemistry, Washington University, St. Louis, MO 63130, USA.
Ken LeeDepartment of Chemistry, Washington University, St. Louis, MO 63130, USA.
Rohit V PappuDepartment of Biomedical Engineering, Washington University, St. Louis, MO 63130, USA; Center for Biomolecular Condensates, James McKelvey School of Engineering, St. Louis, MO 63130, USA. Electronic address: pappu@wustl.edu.
Meredith E JackrelDepartment of Chemistry, Washington University, St. Louis, MO 63130, USA; Center for Biomolecular Condensates, James McKelvey School of Engineering, St. Louis, MO 63130, USA. Electronic address: mjackrel@wustl.edu.

Funding

Safeguards of the Proteome: Elucidating the Roles of Protein DisaggregasesR35GM128772 · NIGMS · WASHINGTON UNIVERSITY · PI JACKREL, MEREDITH E. · 2018 to 2022
$2.0M
Elucidating the roles of protein disaggregases and developing enhanced diaggregases to counter diverse protein-misfolding disordersR35GM153303 · NIGMS · WASHINGTON UNIVERSITY · PI Meredith E. Jackrel · 2024 to 2026
$1.4M
Delineating the role of Matrin-3 in driving aberrant liquid-liquid phase separation that underpins ALS/FTDR21AG080393 · NIA · WASHINGTON UNIVERSITY · PI JACKREL, MEREDITH E. · 2023 to 2024
$429k
NIA NIH HHS R21 AG080393NIGMS NIH HHS R35 GM128772NIGMS NIH HHS R35 GM153303
6 · The paper itself

Abstract

Matrin-3 (MATR3) is an RNA-binding protein (RBP) that is associated with familial amyotrophic lateral sclerosis (ALS) and frontotemporal dementia (FTD). MATR3 features two RNA recognition motifs, two zinc-finger motifs, and four intrinsically disordered regions. Here, we report that human MATR3 associates with itself to form nanoscale spherical assemblies at ultralow protein concentrations. Through concentration-dependent associations, the spheres, which are 20-30 nm in diameter, transition into wormlike assemblies. These observations are reminiscent of sphere-to-worm transitions and micellization of amphiphilic molecules. Using computations and experiments, we discovered that the pattern of inter-domain attractions and repulsions gives MATR3 an inverse bolaamphiphile-like architecture that explains the concentration-dependent assembly characteristics. RNA binding causes shortening of wormlike assemblies of MATR3, whereas ALS/FTD-associated mutations render MATR3 assemblies less responsive to modulation by RNA. Overall, our findings highlight the unique assemblies formed by MATR3 while also showing how RNA-dependent interactions and ALS/FTD-associated mutations modulate the assemblies.

Indexed as

Amyotrophic Lateral SclerosisFrontotemporal DementiaMutationRNARNA-Binding ProteinsHumansNuclear Matrix-Associated ProteinsProtein BindingMATR3 protein, humanNuclear Matrix-Associated ProteinsRNARNA-Binding Proteinsamyotrophic lateral sclerosis (ALS)biomolecular condensatesintrinsically disordered proteinsMatrin-3phase separationRNA-binding proteinTDP-43

Identifiers

PMID40975059
PMCPMC13098646

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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.