Evidence map›Paper›PMID 42420559›Full record

ArticleNature neuroscience2026

Microglial TDP-43 mediates myelin refinement and represses Tyrobp cryptic exon inclusion in mice.

Anne-Claire Compagnion, Andranik Ivanov, Anil Rana, Felipe Espinoza, Thomas Sandmann, Fanny S Martineau, Katia Monsorno, Roberta Facchinetti, Alessandro Matera, Lionel Rougé and 14 more

Abstract read
In one paragraph

Article in Nature neuroscience, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

24 authors.

Anne-Claire CompagnionDepartment of Biomedical Sciences, University of Lausanne, Lausanne, Switzerland.
Andranik Ivanov *Core Unit Bioinformatics, Berlin Institute of Health, Charité-Universitätsmedizin Berlin, Berlin, Germany.ORCID http://orcid.org/0000-0002-4824-1925
Anil Rana *Denali Therapeutics, South San Francisco, CA, USA.
Felipe Espinoza *Department of Biomedical Sciences, University of Lausanne, Lausanne, Switzerland.
Thomas SandmannDenali Therapeutics, South San Francisco, CA, USA.ORCID http://orcid.org/0000-0002-6601-8890
Fanny S MartineauDepartment of Biomedical Sciences, University of Lausanne, Lausanne, Switzerland.
Katia MonsornoDepartment of Biomedical Sciences, University of Lausanne, Lausanne, Switzerland.ORCID http://orcid.org/0000-0002-3701-5930
Roberta FacchinettiDepartment of Life Sciences, Health and Health Professions, Link Campus University, Rome, Italy.
Alessandro MateraDepartment of Biomedical Sciences, University of Lausanne, Lausanne, Switzerland.
Lionel RougéDenali Therapeutics, South San Francisco, CA, USA.
Fernando González IbáñezDépartement de Médecine Moléculaire, Faculté de Médecine, Université Laval, Quebec City, Quebec, Canada.ORCID http://orcid.org/0000-0003-3330-437X
Clarissa CataleInstitut de Biologie de l'Ecole Normale Supérieure (IBENS), Ecole Normale Supérieure, CNRS, INSERM, Université PSL, Team Brain Development and Plasticity, Paris, France.
Matteo BizzottoIRCCS Humanitas Research Hospital, Rozzano, Italy.ORCID http://orcid.org/0000-0003-1622-9371
Sonia GarelInstitut de Biologie de l'Ecole Normale Supérieure (IBENS), Ecole Normale Supérieure, CNRS, INSERM, Université PSL, Team Brain Development and Plasticity, Paris, France.ORCID http://orcid.org/0000-0003-2984-3645
Michela MatteoliIRCCS Humanitas Research Hospital, Rozzano, Italy.ORCID http://orcid.org/0000-0002-3569-7843
Yutaro KashiwagiDepartment of Cellular Neurobiology, Graduate School of Medicine, The University of Tokyo, Tokyo, Japan.ORCID http://orcid.org/0000-0002-8034-3729
Ryuta KoyamaDepartment of Translational Neurobiology, National Institute of Neuroscience, National Center of Neurology and Psychiatry, Tokyo, Japan.ORCID http://orcid.org/0000-0001-7108-174X
Christian HaassBiomedical Center (BMC), Department of Anatomy and Cell Biology, Faculty of Medicine, Ludwig-Maximilians-Universität München, Planegg-Martinsried, Germany.ORCID http://orcid.org/0000-0002-4869-1627
Marie-Eve TremblaySchool of Medical Sciences, University of Victoria, Victoria, British Columbia, Canada.ORCID http://orcid.org/0000-0003-2863-9626
Dieter BeuleCore Unit Bioinformatics, Berlin Institute of Health, Charité-Universitätsmedizin Berlin, Berlin, Germany.
Ileana JelescuDepartment of Radiology, Lausanne University Hospital, Lausanne, Switzerland.ORCID http://orcid.org/0000-0002-3664-0195
Valerio ZerbiDepartment of Psychiatry, Faculty of Medicine, University of Geneva, Geneva, Switzerland.ORCID http://orcid.org/0000-0001-7984-9565
Gilbert Di PaoloDenali Therapeutics, South San Francisco, CA, USA.ORCID http://orcid.org/0000-0003-1032-1265
Rosa C PaolicelliDepartment of Biomedical Sciences, University of Lausanne, Lausanne, Switzerland. rosachiara.paolicelli@unil.ch.ORCID http://orcid.org/0000-0001-6851-0849

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

TDP-43 proteinopathy is a hallmark of neurodegenerative disorders such as amyotrophic lateral sclerosis and frontotemporal dementia where mislocalization of TDP-43 has been observed in neurons and glial cells. However, the role of TDP-43 in microglia and the consequences of its loss of function remain unexplored. Combining magnetic resonance imaging, and confocal, and electron microscopy, we uncovered structural changes and myelin abnormalities in the early postnatal brain of mice lacking microglial TDP-43. Spatial transcriptomics further revealed an enriched interferon-responsive signature associated with oligodendrocyte dysfunction. Early depletion of microglial TDP-43 led to motor deficits in adult mice. Mechanistically, knocking out TDP-43 impaired microglial ability to engulf and degrade myelin. It also led to cryptic exon inclusion in the Tyrobp mRNA, resulting in truncated DAP12 protein, thus causing defective TREM2 signaling. Our findings reveal a role for TDP-43 in regulating the TREM2-DAP12 axis in mice, highlighting a previously unrecognized mechanism through which TDP-43 controls microglial function.

Indexed as

Adaptor Proteins, Signal TransducingDNA-Binding ProteinsMembrane ProteinsMicrogliaMyelin SheathAnimalsBrainExonsMembrane GlycoproteinsMiceMice, Inbred C57BLMice, KnockoutReceptors, ImmunologicAdaptor Proteins, Signal TransducingDNA-Binding ProteinsMembrane GlycoproteinsMembrane ProteinsReceptors, ImmunologicTardbp protein, mouseTrem2 protein, mouseTyrobp protein, mouse

Identifiers

PMID42420559
PMCPMC13433257

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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.