Targeting the VCP-binding motif of ataxin-3 improves phenotypes in Drosophila models of Spinocerebellar Ataxia Type 3.

AAA ATPase Ataxia Ataxin-3 Deubiquitinase Drosophila Machado-Joseph Disease Neurodegeneration Polyglutamine Spinocerebellar Ataxia Type 3 VCP/p97

Journal

Neurobiology of disease
ISSN: 1095-953X
Titre abrégé: Neurobiol Dis
Pays: United States
ID NLM: 9500169

Informations de publication

Date de publication:
12 2021
Historique:
received: 30 06 2021
revised: 23 08 2021
accepted: 21 09 2021
pubmed: 27 9 2021
medline: 29 3 2022
entrez: 26 9 2021
Statut: ppublish

Résumé

Of the family of polyglutamine (polyQ) neurodegenerative diseases, Spinocerebellar Ataxia Type 3 (SCA3) is the most common. Like other polyQ diseases, SCA3 stems from abnormal expansions in the CAG triplet repeat of its disease gene resulting in elongated polyQ repeats within its protein, ataxin-3. Various ataxin-3 protein domains contribute to its toxicity, including the valosin-containing protein (VCP)-binding motif (VBM). We previously reported that VCP, a homo-hexameric protein, enhances pathogenic ataxin-3 aggregation and exacerbates its toxicity. These findings led us to explore the impact of targeting the SCA3 protein by utilizing a decoy protein comprising the N-terminus of VCP (N-VCP) that binds ataxin-3's VBM. The notion was that N-VCP would reduce binding of ataxin-3 to VCP, decreasing its aggregation and toxicity. We found that expression of N-VCP in Drosophila melanogaster models of SCA3 ameliorated various phenotypes, coincident with reduced ataxin-3 aggregation. This protective effect was specific to pathogenic ataxin-3 and depended on its VBM. Increasing the amount of N-VCP resulted in further phenotype improvement. Our work highlights the protective potential of targeting the VCP-ataxin-3 interaction in SCA3, a key finding in the search for therapeutic opportunities for this incurable disorder.

Identifiants

pubmed: 34563642
pii: S0969-9961(21)00265-5
doi: 10.1016/j.nbd.2021.105516
pmc: PMC8693084
mid: NIHMS1762179
pii:
doi:

Substances chimiques

Ataxin-3 EC 3.4.19.12
Valosin Containing Protein EC 3.6.4.6

Types de publication

Journal Article Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

105516

Subventions

Organisme : NINDS NIH HHS
ID : R01 NS086778
Pays : United States

Informations de copyright

Copyright © 2021 The Authors. Published by Elsevier Inc. All rights reserved.

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Auteurs

Sean L Johnson (SL)

Department of Pharmacology, Wayne State University School of Medicine, Detroit, MI 48201, USA.

Kozeta Libohova (K)

Department of Pharmacology, Wayne State University School of Medicine, Detroit, MI 48201, USA.

Jessica R Blount (JR)

Department of Pharmacology, Wayne State University School of Medicine, Detroit, MI 48201, USA.

Alyson L Sujkowski (AL)

Department of Pharmacology, Wayne State University School of Medicine, Detroit, MI 48201, USA; Department of Physiology, Wayne State University School of Medicine, Detroit, MI 48201, USA.

Matthew V Prifti (MV)

Department of Pharmacology, Wayne State University School of Medicine, Detroit, MI 48201, USA.

Wei-Ling Tsou (WL)

Department of Pharmacology, Wayne State University School of Medicine, Detroit, MI 48201, USA.

Sokol V Todi (SV)

Department of Pharmacology, Wayne State University School of Medicine, Detroit, MI 48201, USA; Department of Neurology, Wayne State University School of Medicine, Detroit, MI 48201, USA. Electronic address: stodi@wayne.edu.

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