Cited by 932Heat shock proteins researchAutophagy in Disease and TherapyGenetic Neurodegenerative Diseases

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Misfolded proteins partition between two distinct quality control compartments

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Kaganovich, Daniel, Kopito, Ron, Frydman, Judith·2008·Nature

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Abstract

The accumulation of misfolded proteins in intracellular amyloid inclusions, typical of many neurodegenerative disorders including Huntington's and prion disease, is thought to occur after failure of the cellular protein quality control mechanisms. Here we examine the formation of misfolded protein inclusions in the eukaryotic cytosol of yeast and mammalian cell culture models. We identify two intracellular compartments for the sequestration of misfolded cytosolic proteins. Partition of quality control substrates to either compartment seems to depend on their ubiquitination status and aggregation state. Soluble ubiquitinated misfolded proteins accumulate in a juxtanuclear compartment where proteasomes are concentrated. In contrast, terminally aggregated proteins are sequestered in a perivacuolar inclusion. Notably, disease-associated Huntingtin and prion proteins are preferentially directed to the perivacuolar compartment. Enhancing ubiquitination of a prion protein suffices to promote its delivery to the juxtanuclear inclusion. Our findings provide a framework for understanding the preferential accumulation of amyloidogenic proteins in inclusions linked to human disease.

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1 retracted

RETRACTED ARTICLE: A specific amyloid-β protein assembly in the brain impairs memory
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Authors: Kaganovich, D., Kopito, R., & Frydman, J.
Affiliations: Stanford University (US)
Corresponding author: Frydman, Judith
ORCID: Kaganovich, Daniel
Kopito, Ron
Frydman, Judith
Venue: Nature
Publisher: Springer Science and Business Media LLC
Published: 2008-08
Volume: 454
Issue: 7208
Pages: 1088-1095
ISSN: 0028-0836 (ISSN-L)
1476-4687
DOI: 10.1038/nature07195
PMC: PMC2746971
OpenAlex: W1967025628
Cited by: 932
References: 57
Citations by year: 2026: 24 · 2025: 29 · 2024: 41 · 2023: 47 · 2022: 40 · 2021: 52 · 2020: 55 · 2019: 53 · 2018: 54 · 2017: 76 · 2016: 74 · 2015: 65 · 2014: 71 · 2013: 59 · 2012: 58
FWCI: 18.36
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Licence: www.springer.com/tdm (tdm)
Locations: Nature (publishedVersion)
PubMed (publishedVersion)
PubMed Central (acceptedVersion)
RePEc: Research Papers in Economics (submittedVersion)
ePrints Soton (University of Southampton) (submittedVersion)
Funders: National Institutes of Health
National Institute of General Medical Sciences (R01GM056433)
National Institute of Neurological Disorders and Stroke (R01NS042842)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Genetic Neurodegenerative Diseases
Keywords: protein misfolding, protein quality control, ubiquitination, proteasome, protein aggregation, huntingtin, prion protein, autophagy, neurodegenerative diseases, yeast, mammalian cells
MeSH terms: Ubiquitin-Conjugating Enzyme UBC9, Cytosol, HeLa Cells, Humans, Prions, Proteins, Saccharomyces cerevisiae, Solubility, Protein Folding, Ubiquitin-Conjugating Enzymes, Proteasome Endopeptidase Complex, Von Hippel-Lindau Tumor Suppressor Protein, Ubiquitination

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Misfolded proteins partition between two distinct quality control compartments

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