Cited by 643Genetic Neurodegenerative DiseasesHeat shock proteins researchPrion Diseases and Protein Misfolding

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Progressive Disruption of Cellular Protein Folding in Models of Polyglutamine Diseases

Gidalevitz, Tali, Ben-Zvi, Anat, Ho, Kim H., Brignull, Heather R., Morimoto, Richard I.·2006·Science

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Abstract

Numerous human diseases are associated with the chronic expression of misfolded and aggregation-prone proteins. The expansion of polyglutamine residues in unrelated proteins is associated with the early onset of neurodegenerative disease. To understand how the presence of misfolded proteins leads to cellular dysfunction, we employed Caenorhabditis elegans polyglutamine aggregation models. Here, we find that polyglutamine expansions disrupted the global balance of protein folding quality control, resulting in the loss of function of diverse metastable proteins with destabilizing temperature-sensitive mutations. In turn, these proteins, although innocuous under normal physiological conditions, enhanced the aggregation of polyglutamine proteins. Thus, weak folding mutations throughout the genome can function as modifiers of polyglutamine phenotypes and toxicity.

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Authors: Gidalevitz, T., Ben-Zvi, A., Ho, K. H., Brignull, H. R., & Morimoto, R. I.
Affiliations: Northwestern University (US)
Department of Biochemistry, Molecular Biology, and Cell Biology, Rice Institute for Biomedical Research, Northwestern University, Evanston, IL 60208, USA.
Corresponding author: Gidalevitz, Tali
Morimoto, Richard I.
ORCID: Gidalevitz, Tali
Morimoto, Richard I.
Venue: Science
Publisher: American Association for the Advancement of Science (AAAS)
Published: 2006-03-10
Volume: 311
Issue: 5766
Pages: 1471-1474
ISSN: 0036-8075 (ISSN-L)
1095-9203
DOI: 10.1126/science.1124514
OpenAlex: W2025851491
Cited by: 643
References: 30
Citations by year: 2026: 13 · 2025: 15 · 2024: 15 · 2023: 22 · 2022: 26 · 2021: 24 · 2020: 28 · 2019: 38 · 2018: 28 · 2017: 28 · 2016: 29 · 2015: 28 · 2014: 46 · 2013: 40 · 2012: 41
FWCI: 16.20
Type: journal article
Language: en
Open access: closed
Locations: Science (publishedVersion)
PubMed (publishedVersion)
Funders: National Institutes of Health (5f32gm075583-02)
National Institute on Aging (R37AG026647)
National Heart, Lung, and Blood Institute (T32HL076139)
National Institute of General Medical Sciences (T32 GM 08061, F32 GM075583-01, T32GM008061)
Topics: Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Genetic Neurodegenerative Diseases
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Prion Diseases and Protein Misfolding
Keywords: polyglutamine diseases, protein folding, protein aggregation, protein quality control, temperature-sensitive mutation, genetic modifiers, neurodegenerative diseases, Caenorhabditis elegans, protein misfolding
MeSH terms: Animals, Disease Models, Animal, Glutamine, Humans, Mutation, Peptides, Temperature, Tropomyosin, Caenorhabditis elegans, Protein Folding, Neurodegenerative Diseases, Caenorhabditis elegans Proteins, Dynamin I

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Progressive Disruption of Cellular Protein Folding in Models of Polyglutamine Diseases

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