Sigma-1R–Pom121 axis preserves nuclear transport and integrity in poly-PR-induced C9orf72 ALS

Nucleocytoplasmic transport disruption contributes to the pathogenesis of C9orf72-associated amyotrophic lateral sclerosis (ALS) and frontotemporal dementia. Among the dipeptide repeat proteins translated from G4C2-repeat RNA, poly-PR is particularly toxic, compromising nuclear envelope integrity an...

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Main Authors: Chun-Yu Lin, Hsuan-Cheng Wu, Ru-Huei Fu, Eddie Feng-Ju Weng, Wen-Chi Hsieh, Tsung-Ping Su, Hsiang-En Wu, Shao-Ming Wang
Format: Article
Language:English
Published: Elsevier 2025-08-01
Series:Neurobiology of Disease
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Online Access:http://www.sciencedirect.com/science/article/pii/S0969996125002086
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author Chun-Yu Lin
Hsuan-Cheng Wu
Ru-Huei Fu
Eddie Feng-Ju Weng
Wen-Chi Hsieh
Tsung-Ping Su
Hsiang-En Wu
Shao-Ming Wang
author_facet Chun-Yu Lin
Hsuan-Cheng Wu
Ru-Huei Fu
Eddie Feng-Ju Weng
Wen-Chi Hsieh
Tsung-Ping Su
Hsiang-En Wu
Shao-Ming Wang
author_sort Chun-Yu Lin
collection DOAJ
description Nucleocytoplasmic transport disruption contributes to the pathogenesis of C9orf72-associated amyotrophic lateral sclerosis (ALS) and frontotemporal dementia. Among the dipeptide repeat proteins translated from G4C2-repeat RNA, poly-PR is particularly toxic, compromising nuclear envelope integrity and transport. Here, we revealed that poly-PR reduced expression of the nucleoporin Pom121 in NSC-34 cells and in an AAV-mediated poly-PR42 mouse model, resulting in cytoplasmic mislocalization of the neuroprotective transcription factor ATF3 and nuclear envelope damage. Pom121 overexpression restored nuclear ATF3 localization and alleviated poly-PR-induced toxicity. We further identified Sigma-1 receptor (Sigma-1R) as a stabilizer of Pom121 that preserved nuclear integrity and ATF3 function under oxidative stress. Overexpression of Sigma-1R, Pom121, or ATF3 rescued poly-PR-induced cytotoxicity. Our findings defined a protective Sigma-1R/Pom121/ATF3 axis and suggested this pathway as a therapeutic target in C9orf72-linked ALS.
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institution OA Journals
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publishDate 2025-08-01
publisher Elsevier
record_format Article
series Neurobiology of Disease
spelling doaj-art-bd44bd76aaef40c1bf1a167ae3aff04a2025-08-20T02:35:44ZengElsevierNeurobiology of Disease1095-953X2025-08-0121210699210.1016/j.nbd.2025.106992Sigma-1R–Pom121 axis preserves nuclear transport and integrity in poly-PR-induced C9orf72 ALSChun-Yu Lin0Hsuan-Cheng Wu1Ru-Huei Fu2Eddie Feng-Ju Weng3Wen-Chi Hsieh4Tsung-Ping Su5Hsiang-En Wu6Shao-Ming Wang7Neuroscience and Brain Disease Center, China Medical University, Taichung 404328, Taiwan; School of Medicine, College of Medicine, China Medical University, Taichung 404328, TaiwanNeuroscience and Brain Disease Center, China Medical University, Taichung 404328, Taiwan; Graduate Institute of Biomedical Sciences, College of Medicine, China Medical University, Taichung 404328, TaiwanGraduate Institute of Biomedical Sciences, College of Medicine, China Medical University, Taichung 404328, Taiwan; Ph.D. Program for Aging, China Medical University, Taichung 404328, Taiwan; Translational Medicine Research Center, China Medical University Hospital, Taichung 40447, TaiwanNeuroscience and Brain Disease Center, China Medical University, Taichung 404328, Taiwan; Graduate Institute of Biomedical Sciences, College of Medicine, China Medical University, Taichung 404328, TaiwanNeuroscience and Brain Disease Center, China Medical University, Taichung 404328, Taiwan; Graduate Institute of Biomedical Sciences, College of Medicine, China Medical University, Taichung 404328, TaiwanCellular Pathobiology Section, Integrative Neuroscience Research Branch, Intramural Research Program, National Institute on Drug Abuse, National Institutes of Health, DHHS, 333 Cassell Drive, Baltimore, MD 21224, USACellular Pathobiology Section, Integrative Neuroscience Research Branch, Intramural Research Program, National Institute on Drug Abuse, National Institutes of Health, DHHS, 333 Cassell Drive, Baltimore, MD 21224, USANeuroscience and Brain Disease Center, China Medical University, Taichung 404328, Taiwan; Graduate Institute of Biomedical Sciences, College of Medicine, China Medical University, Taichung 404328, Taiwan; Corresponding author at: Graduate Institute of Biomedical Sciences, College of Medicine, China Medical University, Taichung 404328, Taiwan.Nucleocytoplasmic transport disruption contributes to the pathogenesis of C9orf72-associated amyotrophic lateral sclerosis (ALS) and frontotemporal dementia. Among the dipeptide repeat proteins translated from G4C2-repeat RNA, poly-PR is particularly toxic, compromising nuclear envelope integrity and transport. Here, we revealed that poly-PR reduced expression of the nucleoporin Pom121 in NSC-34 cells and in an AAV-mediated poly-PR42 mouse model, resulting in cytoplasmic mislocalization of the neuroprotective transcription factor ATF3 and nuclear envelope damage. Pom121 overexpression restored nuclear ATF3 localization and alleviated poly-PR-induced toxicity. We further identified Sigma-1 receptor (Sigma-1R) as a stabilizer of Pom121 that preserved nuclear integrity and ATF3 function under oxidative stress. Overexpression of Sigma-1R, Pom121, or ATF3 rescued poly-PR-induced cytotoxicity. Our findings defined a protective Sigma-1R/Pom121/ATF3 axis and suggested this pathway as a therapeutic target in C9orf72-linked ALS.http://www.sciencedirect.com/science/article/pii/S0969996125002086Poly-PRC9orf72 ALSPom121Sigma-1RNucleocytoplasmic transportNuclear envelope integrity
spellingShingle Chun-Yu Lin
Hsuan-Cheng Wu
Ru-Huei Fu
Eddie Feng-Ju Weng
Wen-Chi Hsieh
Tsung-Ping Su
Hsiang-En Wu
Shao-Ming Wang
Sigma-1R–Pom121 axis preserves nuclear transport and integrity in poly-PR-induced C9orf72 ALS
Neurobiology of Disease
Poly-PR
C9orf72 ALS
Pom121
Sigma-1R
Nucleocytoplasmic transport
Nuclear envelope integrity
title Sigma-1R–Pom121 axis preserves nuclear transport and integrity in poly-PR-induced C9orf72 ALS
title_full Sigma-1R–Pom121 axis preserves nuclear transport and integrity in poly-PR-induced C9orf72 ALS
title_fullStr Sigma-1R–Pom121 axis preserves nuclear transport and integrity in poly-PR-induced C9orf72 ALS
title_full_unstemmed Sigma-1R–Pom121 axis preserves nuclear transport and integrity in poly-PR-induced C9orf72 ALS
title_short Sigma-1R–Pom121 axis preserves nuclear transport and integrity in poly-PR-induced C9orf72 ALS
title_sort sigma 1r pom121 axis preserves nuclear transport and integrity in poly pr induced c9orf72 als
topic Poly-PR
C9orf72 ALS
Pom121
Sigma-1R
Nucleocytoplasmic transport
Nuclear envelope integrity
url http://www.sciencedirect.com/science/article/pii/S0969996125002086
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