Evidence map›Paper›PMID 40891053›Full record

ArticleFEBS letters2025

C9orf72 ALS-causing mutations lead to mislocalization and aggregation of nucleoporin Nup107 into stress granules.

Saygın Bilican, Yara Nabawi, William Hongyu Zhang, Dunja Petrovic, Markus Wehrmann, Sara Muñoz-García, Seda Koyuncu, David Vilchez

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in FEBS letters, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Review
  2. Review
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

8 authors.

Saygın BilicanInstitute for Integrated Stress Response Signaling, Faculty of Medicine, University Hospital Cologne, Germany.
Yara NabawiInstitute for Integrated Stress Response Signaling, Faculty of Medicine, University Hospital Cologne, Germany.
William Hongyu ZhangInstitute for Integrated Stress Response Signaling, Faculty of Medicine, University Hospital Cologne, Germany.
Dunja PetrovicInstitute for Integrated Stress Response Signaling, Faculty of Medicine, University Hospital Cologne, Germany.
Markus WehrmannInstitute for Integrated Stress Response Signaling, Faculty of Medicine, University Hospital Cologne, Germany.
Sara Muñoz-GarcíaCologne Excellence Cluster for Cellular Stress Responses in Aging-Associated Diseases (CECAD), University of Cologne, Germany.ORCID https://orcid.org/0009-0003-4126-7238
Seda KoyuncuInstitute for Integrated Stress Response Signaling, Faculty of Medicine, University Hospital Cologne, Germany.
David VilchezInstitute for Integrated Stress Response Signaling, Faculty of Medicine, University Hospital Cologne, Germany.ORCID https://orcid.org/0000-0002-0801-0743

Funding

Deutsche Forschungsgemeinschaft CRC1678 (project B06 to D.V)Deutsche Forschungsgemeinschaft Germany's Excellence Strategy-CECAD (EXC2030-39390661388)Deutsche Forschungsgemeinschaft Largeinstrument grant (INST216/1329-1 FUGG to CECAD Proteomics Facility)Deutsche Forschungsgemeinschaft Research Unit FOR5762 (project VI742/10-1 to D.V)Else Kröner-Fresenius-Stiftung 2021-EKSE.95 to D.V
6 · The paper itself

Abstract

Amyotrophic lateral sclerosis (ALS) is a fatal disorder caused by motor neuron degeneration. Hexanucleotide repeat expansions in the C9orf72 gene, the most common genetic cause of ALS (C9-ALS), drive toxicity through different mechanisms. These pathological changes include alterations in stress granules (SGs), ribonucleoprotein complexes formed under stress conditions. Here, we show that G3BP1, a core component of SGs, exhibits enhanced interaction with the nucleoporin Nup107 in motor neurons derived from patient iPSCs carrying C9orf72 mutations. Moreover, Nup107 colocalizes with SGs and aggregates in C9-ALS motor neurons. Notably, knockdown of npp-5, the Caenorhabditis elegans ortholog of Nup107, alleviates ALS-associated phenotypes in worm models, including reduced lifespan and impaired motility. Together, our findings provide insights into disease-related changes in C9-ALS pathogenesis.

Indexed as

Amyotrophic Lateral SclerosisC9orf72 ProteinMutationNuclear Pore Complex ProteinsStress GranulesAnimalsCaenorhabditis elegansCaenorhabditis elegans ProteinsDNA HelicasesHumansInduced Pluripotent Stem CellsMotor NeuronsPoly-ADP-Ribose Binding ProteinsProtein AggregatesRNA HelicasesRNA Recognition Motif ProteinsC9orf72 ProteinC9orf72 protein, humanCaenorhabditis elegans ProteinsDNA HelicasesG3BP1 protein, humanNuclear Pore Complex ProteinsPoly-ADP-Ribose Binding ProteinsProtein AggregatesRNA HelicasesRNA Recognition Motif ProteinsAmyotrophic lateral sclerosisC. elegansiPSC‐disease modelingNucleoporinsProteostasisStress granules

Identifiers

PMID40891053
PMCPMC12599624

What Socratic holds

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LicenceCC BY
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 Socratic graph.