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Article

YTHDC1 functions as a molecular chaperone to suppress ALS-linked hnRNPA1 mutants from aggregation.

Nature communications - 21 Aug 2026

Ren Kang, Cheng Mingjie, Luo Qiudan, Zhang Boxin, Zhang Haosheng, Li Zhe, Liu Yuxin, Wang Yujie, Kang Ting, Dai Xiaoming, Chen Jiong, Cheng Yuanming, Huang Liangqian

Abstract excerpt

Proteostasis failure drives multiple neurodegenerative disorders (NDs), and ATP-independent chaperone pathways that support neuronal proteostasis remain poorly defined. Here, we identify the N6-methyladenosine (m6A)-binding protein YTHDC1 as an ATP-independent molecular chaperone, whose activity is mediated by a highly acidic polyaspartate/glutamate (polyD/E) segment. YTHDC1 prevents protein misfolding and...

Read the complete abstract on PubMed

Topics

Amyotrophic Lateral Sclerosis
Heterogeneous Nuclear Ribonucleoprotein A1
Humans
Molecular Chaperones
Animals

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Mutation

Protein Aggregates

Protein Folding

Protein Aggregation, Pathological

Nerve Tissue Proteins

Neurons

Source

Open in PubMed Open full text

Identifiers

PMID: 42680774
DOI: 10.1038/s41467-026-77016-y
PMCID: PMC13534550

Genes

YTHDC1

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 25 Oct 2026.

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