Evidence map›Paper›PMID 41117937›Full record

ArticleCellular and molecular life sciences : CMLS2025

Comparing loss of individual fragile X proteins suggests strong links to cellular senescence and aging.

Sonja Menge, Inmaculada Segura, Max Hartmann, Lorena Decker, Selin Kiran, Karin M Danzer, Sebastian Iben, Angelika B Harbauer, Patrick Oeckl, Axel Freischmidt

Abstract read
In one paragraph

Article in Cellular and molecular life sciences : CMLS, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. 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

10 authors.

Sonja MengeDepartment of Neurology, Ulm University, ZBMF, Helmholtzstr. 8/1, Ulm, 89081, Germany.ORCID http://orcid.org/0000-0003-3445-2753
Inmaculada SeguraMax Planck Institute for Biological Intelligence, Martinsried, Germany.ORCID http://orcid.org/0000-0003-1849-5569
Max HartmannDepartment of Dermatology and Allergic Diseases, Ulm University, Ulm, Germany.
Lorena DeckerDepartment of Neurology, Ulm University, ZBMF, Helmholtzstr. 8/1, Ulm, 89081, Germany.
Selin KiranDepartment of Neurology, Ulm University, ZBMF, Helmholtzstr. 8/1, Ulm, 89081, Germany.ORCID http://orcid.org/0000-0003-0133-7046
Karin M DanzerDepartment of Neurology, Ulm University, ZBMF, Helmholtzstr. 8/1, Ulm, 89081, Germany.
Sebastian IbenDepartment of Dermatology and Allergic Diseases, Ulm University, Ulm, Germany.
Angelika B HarbauerMax Planck Institute for Biological Intelligence, Martinsried, Germany.ORCID http://orcid.org/0000-0002-4568-9003
Patrick OecklDepartment of Neurology, Ulm University, ZBMF, Helmholtzstr. 8/1, Ulm, 89081, Germany.ORCID http://orcid.org/0000-0002-7652-7023
Axel FreischmidtDepartment of Neurology, Ulm University, ZBMF, Helmholtzstr. 8/1, Ulm, 89081, Germany. axel.freischmidt@uni-ulm.de.ORCID http://orcid.org/0000-0003-1216-3790

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Members of the fragile X protein (FXP) family (FMR1, FXR1 and FXR2) are differentially expressed in most types of cancer and major neurodegenerative diseases. While increased expression of FXR1 in cancer has been linked to senescence evasion and consequently tumor initiation and progression, decreased expression of FXPs in neurodegeneration may contribute to pathogenic protein aggregation and death of vulnerable neurons. However, due the causal role in fragile x syndrome, most data are available about loss of FMR1 in neurons while functions of FXR1 and especially FXR2 remain largely unexplored. To address this knowledge gap, and to directly compare functions of the FXPs, we used proteomics of CRISPR/Cas9 edited HAP1 cells carrying knockouts of the individual FXPs for identification of cellular mechanisms associated with these proteins. Further exploration of proteomic findings suggests roles of the FXPs in ribosome biogenesis, autophagy and mitochondrial health linked to organismal aging, and cellular senescence. Validation of FXP induced defects relevant for neurodegenerative diseases in neuroblastoma cell line SH-SY5Y upon FXP knockdown revealed high cell type specificity of individual FXP functions. Overall, we provide a comprehensive overview and comparison of cellular mechanisms related to the individual FXPs, as well as starting points for further studying this protein family in respective cell types of FXP associated diseases, and in aging in general.

Indexed as

AgingCellular SenescenceFragile X Messenger Ribonucleoprotein 1RNA-Binding ProteinsAutophagyCell Line, TumorCRISPR-Cas SystemsFragile X SyndromeHumansMitochondriaNeurodegenerative DiseasesProteomicsFMR1 protein, humanFragile X Messenger Ribonucleoprotein 1FXR1 protein, humanRNA-Binding ProteinsAlzheimer’s diseaseAmyotrophic lateral sclerosisFragile x syndromeParkinson’s diseaseProtein aggregation

Identifiers

PMID41117937
PMCPMC12540212

What Socratic holds

Textmetadata
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.