C9ORF72 poly-PR induces TDP-43 nuclear condensation via NEAT1 and is modulated by HSP70 activity

Summary: The toxicity of C9ORF72-encoded polyproline-arginine (poly-PR) dipeptide is associated with its ability to disrupt the liquid-liquid phase separation of intrinsically disordered proteins participating in the formation of membraneless organelles, such as the nucleolus and paraspeckles. Amyot...

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Main Authors: Diksha Agnihotri, Chi-Chang Lee, Po-Chao Lu, Ruei-Yu He, Yung-An Huang, Hung-Chih Kuo, Joseph Jen-Tse Huang
Format: Article
Language:English
Published: Elsevier 2025-01-01
Series:Cell Reports
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Online Access:http://www.sciencedirect.com/science/article/pii/S2211124724015249
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author Diksha Agnihotri
Chi-Chang Lee
Po-Chao Lu
Ruei-Yu He
Yung-An Huang
Hung-Chih Kuo
Joseph Jen-Tse Huang
author_facet Diksha Agnihotri
Chi-Chang Lee
Po-Chao Lu
Ruei-Yu He
Yung-An Huang
Hung-Chih Kuo
Joseph Jen-Tse Huang
author_sort Diksha Agnihotri
collection DOAJ
description Summary: The toxicity of C9ORF72-encoded polyproline-arginine (poly-PR) dipeptide is associated with its ability to disrupt the liquid-liquid phase separation of intrinsically disordered proteins participating in the formation of membraneless organelles, such as the nucleolus and paraspeckles. Amyotrophic lateral sclerosis (ALS)-related TAR DNA-binding protein 43 (TDP-43) also undergoes phase separation to form nuclear condensates (NCs) in response to stress. However, whether poly-PR alters the nuclear condensation of TDP-43 in ALS remains unclear. In this study, we find that the poly-PR dipeptide enhances the formation of TDP-43 NCs with decreased fluidity. While the non-coding RNA, nuclear-enriched abundant transcript 1 (NEAT1), is essential for the formation of TDP-43 NCs, heat shock protein 70 (HSP70) chaperone maintains their fluidity. Under prolonged poly-PR stress, HSP70 delocalizes from TDP-43 NCs, leading to the oligomerization of TDP-43 within these condensates. This phenomenon is accompanied with TDP-43 mislocalization and increasing cytotoxicity. Our study demonstrates the role of NEAT1 and HSP70 in the aberrant phase transition of TDP-43 NCs under poly-PR stress.
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issn 2211-1247
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publishDate 2025-01-01
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spelling doaj-art-b41e9a2f419e482da5cb104efdd2add52025-08-20T02:40:40ZengElsevierCell Reports2211-12472025-01-0144111517310.1016/j.celrep.2024.115173C9ORF72 poly-PR induces TDP-43 nuclear condensation via NEAT1 and is modulated by HSP70 activityDiksha Agnihotri0Chi-Chang Lee1Po-Chao Lu2Ruei-Yu He3Yung-An Huang4Hung-Chih Kuo5Joseph Jen-Tse Huang6Institute of Chemistry, Academia Sinica, Taipei 115, Taiwan; Taiwan International Graduate Program in Interdisciplinary Neuroscience, National Taiwan University and Academia Sinica, Taipei, Taiwan; National Taiwan University, Taipei 100, TaiwanInstitute of Chemistry, Academia Sinica, Taipei 115, TaiwanInstitute of Chemistry, Academia Sinica, Taipei 115, Taiwan; Chemical Biology and Molecular Biophysics, Taiwan International Graduate Program, Academia Sinica, Taipei 115, Taiwan; Department and Graduate Institute of Pharmacology, National Taiwan University, Taipei 100, TaiwanInstitute of Chemistry, Academia Sinica, Taipei 115, TaiwanInstitute of Chemistry, Academia Sinica, Taipei 115, TaiwanNeuroscience Program of Academia Sinica, Academia Sinica, Taipei 115, Taiwan; Institute of Cellular and Organismic Biology, Academia Sinica, No. 128, Sec. 2, Academia Road, Nankang, Taipei 11529, Taiwan; Graduate Institute of Medical Genomics and Proteomics, College of Medicine, National Taiwan University, Taipei, TaiwanInstitute of Chemistry, Academia Sinica, Taipei 115, Taiwan; Sustainable Chemical Science and Technology, Taiwan International Graduate Program, Academia Sinica, Taipei 115, Taiwan; Department of Applied Chemistry, National Chiayi University, Chiayi City 600, Taiwan; Neuroscience Program of Academia Sinica, Academia Sinica, Taipei 115, Taiwan; Corresponding authorSummary: The toxicity of C9ORF72-encoded polyproline-arginine (poly-PR) dipeptide is associated with its ability to disrupt the liquid-liquid phase separation of intrinsically disordered proteins participating in the formation of membraneless organelles, such as the nucleolus and paraspeckles. Amyotrophic lateral sclerosis (ALS)-related TAR DNA-binding protein 43 (TDP-43) also undergoes phase separation to form nuclear condensates (NCs) in response to stress. However, whether poly-PR alters the nuclear condensation of TDP-43 in ALS remains unclear. In this study, we find that the poly-PR dipeptide enhances the formation of TDP-43 NCs with decreased fluidity. While the non-coding RNA, nuclear-enriched abundant transcript 1 (NEAT1), is essential for the formation of TDP-43 NCs, heat shock protein 70 (HSP70) chaperone maintains their fluidity. Under prolonged poly-PR stress, HSP70 delocalizes from TDP-43 NCs, leading to the oligomerization of TDP-43 within these condensates. This phenomenon is accompanied with TDP-43 mislocalization and increasing cytotoxicity. Our study demonstrates the role of NEAT1 and HSP70 in the aberrant phase transition of TDP-43 NCs under poly-PR stress.http://www.sciencedirect.com/science/article/pii/S2211124724015249CP: Cell biology
spellingShingle Diksha Agnihotri
Chi-Chang Lee
Po-Chao Lu
Ruei-Yu He
Yung-An Huang
Hung-Chih Kuo
Joseph Jen-Tse Huang
C9ORF72 poly-PR induces TDP-43 nuclear condensation via NEAT1 and is modulated by HSP70 activity
Cell Reports
CP: Cell biology
title C9ORF72 poly-PR induces TDP-43 nuclear condensation via NEAT1 and is modulated by HSP70 activity
title_full C9ORF72 poly-PR induces TDP-43 nuclear condensation via NEAT1 and is modulated by HSP70 activity
title_fullStr C9ORF72 poly-PR induces TDP-43 nuclear condensation via NEAT1 and is modulated by HSP70 activity
title_full_unstemmed C9ORF72 poly-PR induces TDP-43 nuclear condensation via NEAT1 and is modulated by HSP70 activity
title_short C9ORF72 poly-PR induces TDP-43 nuclear condensation via NEAT1 and is modulated by HSP70 activity
title_sort c9orf72 poly pr induces tdp 43 nuclear condensation via neat1 and is modulated by hsp70 activity
topic CP: Cell biology
url http://www.sciencedirect.com/science/article/pii/S2211124724015249
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