Evidence map›Paper›PMID 42562736›Full record

ArticleNeurotherapeutics : the journal of the American Society for Experimental NeuroTherapeutics2026

Wild-type C9orf72 drives proteasomal dysfunction and mutant aggregates via a Stat1-Isg15 axis in Huntington's disease.

Siew Chin Chan, Chih-Wei Tung, Chih-Yi Chang, Ching-Chun Su, Yi-Ching Chen, Po-Ming Wu, Chia-Yu Tung, Shih-Feng Chen, Hsiao-Ying Kuo, Pei-Hsun Cheng and 2 more

Abstract read
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Article in Neurotherapeutics : the journal of the American Society for Experimental NeuroTherapeutics, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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1 · What the graph read from it

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2 · The registry

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3 · Its place in the literature

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4 · The record

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5 · Who and what money

Authors and funding

12 authors.

Siew Chin ChanDepartment of Physiology, College of Medicine, National Cheng Kung University, Tainan, 70101, Taiwan; Institute of Basic Medical Sciences, College of Medicine, National Cheng Kung University, Tainan, 70101, Taiwan.
Chih-Wei TungDepartment of Physiology, College of Medicine, National Cheng Kung University, Tainan, 70101, Taiwan; Department of Animal Science and Biotechnology, College of Agriculture and Health, Tunghai University, Taichung, 407224, Taiwan.
Chih-Yi ChangDepartment of Physiology, College of Medicine, National Cheng Kung University, Tainan, 70101, Taiwan.
Ching-Chun SuDepartment of Physiology, College of Medicine, National Cheng Kung University, Tainan, 70101, Taiwan.
Yi-Ching ChenDepartment of Physiology, College of Medicine, National Cheng Kung University, Tainan, 70101, Taiwan.
Po-Ming WuDepartment of Pediatrics, National Cheng Kung University Hospital, College of Medicine, National Cheng Kung University, Tainan, 70101, Taiwan.
Chia-Yu TungDepartment of Physiology, College of Medicine, National Cheng Kung University, Tainan, 70101, Taiwan.
Shih-Feng ChenDepartment of Physiology, College of Medicine, National Cheng Kung University, Tainan, 70101, Taiwan.
Hsiao-Ying KuoDepartment of Physiology, College of Medicine, National Cheng Kung University, Tainan, 70101, Taiwan.
Pei-Hsun ChengDepartment of Physiology, College of Medicine, National Cheng Kung University, Tainan, 70101, Taiwan.
Chuan-Mu ChenDepartment of Life Sciences, College of Life Sciences, National Chung Hsing University, Taichung, 40227, Taiwan.
Shang-Hsun YangDepartment of Physiology, College of Medicine, National Cheng Kung University, Tainan, 70101, Taiwan; Institute of Basic Medical Sciences, College of Medicine, National Cheng Kung University, Tainan, 70101, Taiwan. Electronic address: syang@mail.ncku.edu.tw.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Mutant C9orf72 has been extensively studied as a major genetic cause of amyotrophic lateral sclerosis and frontotemporal dementia, and is also known to generate Huntington's disease (HD)-like phenocopies. However, despite this strong disease association, the role of wild-type C9orf72 (wt-C9orf72) in neurodegeneration remains largely unexplored. HD is a neurodegenerative disease, and characterized by the accumulation of misfolded mutant Huntingtin (mHTT) and impaired proteostasis, yet the upstream mechanisms driving ubiquitin-proteasome system (UPS) dysfunction are not fully understood. Here, we identify a previously unrecognized modulatory role of wt-C9orf72 in regulating mHTT aggregation in experimental HD models. Analysis of public transcriptomic datasets reveal context-dependent C9ORF72 expression changes across HD-related human datasets, while C9orf72 levels are increased in R6/2 mouse brain lysates. Functional analyses reveal that overexpression of wt-C9orf72 increases mHTT aggregation and is accompanied by increased apoptotic signaling and reduced cell viability. Unbiased proteomic profiling identifies Stat1 as a key downstream effector. Mechanistically, wt-C9orf72 promotes Stat1 activation and nuclear translocation, leading to transcriptional upregulation of Isg15, a ubiquitin-like modifier. Elevated Isg15 disrupts UPS function, resulting in accumulation of polyubiquitinated proteins and impaired proteasomal degradation. Importantly, genetic suppression of Stat1 or Isg15 significantly attenuates C9orf72-associated mHTT aggregation, supporting a functional C9orf72-Stat1-Isg15 axis. Consistent with these cell-based findings, Stat1, phosphorylated Stat1 and Isg15 levels are elevated in the cortex and striatum of R6/2 HD mouse brains. Collectively, our findings identify a novel wt-C9orf72-Stat1-Isg15 axis that promotes proteasomal dysfunction and mHTT aggregation, providing new insights into wt-C9orf72-associated protein homeostasis.

Indexed as

C9orf72 ProteinCytokinesHuntington DiseaseProteasome Endopeptidase ComplexSTAT1 Transcription FactorUbiquitinsAnimalsBrainHumansHuntingtin ProteinMiceMice, TransgenicMutationProteotoxic StressSignal TransductionC9orf72 ProteinC9orf72 protein, humanCytokinesHuntingtin ProteinISG15 protein, humanProteasome Endopeptidase ComplexSTAT1 protein, humanStat1 protein, mouseSTAT1 Transcription FactorUbiquitinsHuntington’s diseaseIsg15Stat1Ubiquitin-proteasome systemWild-type C9orf72

Identifiers

PMID42562736
PMCPMC13615721

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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.