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Article

TDP-43 nuclear loss in FTD/ALS causes widespread alternative polyadenylation changes.

Nature neuroscience - 1 Nov 2025

Zeng Yi, Lovchykova Anastasiia, Akiyama Tetsuya, Rayner Stephanie L, Maheswari Jawahar Vidhya, Liu Chang, Sianto Odilia, Guo Caiwei, Calliari Anna, Prudencio Mercedes, Dickson Dennis W, Petrucelli Leonard, Gitler Aaron D

Abstract excerpt

In frontotemporal dementia and amyotrophic lateral sclerosis, the RNA-binding protein TDP-43 is depleted from the nucleus of neurons in the brain and spinal cord. A key function of TDP-43 has emerged as a repressor of cryptic exon inclusion during pre-mRNA splicing, but a role for TDP-43 in other RNA-processing events remains unresolved. Here we show that loss of TDP-43 from neuronal nuclei of human brain and...

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Source

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Identifiers

PMID: 41120750
DOI: 10.1038/s41593-025-02049-3
PMCID: PMC12586192

Genes

NEFL
SFPQ
TMEM106B

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026.

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TDP-43 nuclear loss in FTD/ALS causes widespread alternative polyadenylation changes.PMID 41120750Read ↗

TDP-43 nuclear loss in FTD/ALS causes widespread alternative polyadenylation changesSemantic proximity Read ↗

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TDP-43 loss induces extensive cryptic polyadenylation in ALS/FTDSemantic proximity Read ↗

Pathogenic Mutation of TDP-43 Impairs RNA Processing in a Cell Type-Specific Manner: Implications for the Pathogenesis of ALS/FTLD.Semantic proximity Read ↗

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