Cited by 321Heat shock proteins researchEndoplasmic Reticulum Stress and DiseaseGenetics, Aging, and Longevity in Model Organisms

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Spatial sequestration of misfolded proteins by a dynamic chaperone pathway enhances cellular fitness during stress

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Escusa-Toret, Stéphanie, Vonk, Willianne I. M., Frydman, Judith·2013·Nature Cell Biology

DOI 10.1038/ncb2838PMC PMC4121856

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Abstract

The extensive links between proteotoxic stress, protein aggregation and pathologies ranging from ageing to neurodegeneration underscore the importance of understanding how cells manage protein misfolding. Using live-cell imaging, we determine the fate of stress-induced misfolded proteins from their initial appearance until their elimination. Upon denaturation, misfolded proteins are sequestered from the bulk cytoplasm into dynamic endoplasmic reticulum (ER)-associated puncta that move and coalesce into larger structures in an energy-dependent but cytoskeleton-independent manner. These puncta, which we name Q-bodies, concentrate different misfolded and stress-denatured proteins en route to degradation, but do not contain amyloid aggregates, which localize instead to the insoluble protein deposit compartment. Q-body formation and clearance depends on an intact cortical ER and a complex chaperone network that is affected by rapamycin and impaired during chronological ageing. Importantly, Q-body formation enhances cellular fitness during stress. We conclude that spatial sequestration of misfolded proteins in Q-bodies is an early quality control strategy occurring synchronously with degradation to clear the cytoplasm of potentially toxic species.

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Authors: Escusa-Toret, S., Vonk, W. I. M., & Frydman, J.
Affiliations: Stanford University (US)
Corresponding author: Frydman, Judith
ORCID: Vonk, Willianne I. M.
Frydman, Judith
Venue: Nature Cell Biology
Publisher: Springer Science and Business Media LLC
Published: 2013-09-15
Volume: 15
Issue: 10
Pages: 1231-1243
ISSN: 1465-7392 (ISSN-L)
1476-4679
DOI: 10.1038/ncb2838
PMC: PMC4121856
OpenAlex: W2092986760
Cited by: 321
References: 65
Citations by year: 2026: 6 · 2025: 15 · 2024: 26 · 2023: 30 · 2022: 16 · 2021: 30 · 2020: 35 · 2019: 27 · 2018: 29 · 2017: 24 · 2016: 20 · 2015: 36 · 2014: 23 · 2013: 4
FWCI: 12.38
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Licence: www.springer.com/tdm (tdm)
Locations: Nature Cell Biology (publishedVersion)
PubMed (publishedVersion)
Europe PMC (PubMed Central) (acceptedVersion)
PubMed Central (acceptedVersion)
Funders: National Eye Institute (PN2EY016525)
National Institute of General Medical Sciences (R37GM056433, R01GM056433)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Endoplasmic Reticulum Stress and Disease
Life Sciences › Biochemistry, Genetics and Molecular Biology › Aging › Genetics, Aging, and Longevity in Model Organisms
Keywords: protein misfolding, ER-associated degradation, chaperone network, proteotoxic stress, protein aggregation, endoplasmic reticulum, proteasome, chronological aging, rapamycin, cell fitness, protein quality control, amyloid aggregates, inclusion bodies
MeSH terms: Ethanol, Azetidinecarboxylic Acid, Endoplasmic Reticulum, Hot Temperature, Saccharomyces cerevisiae, Stress, Physiological, Signal Transduction, Protein Folding, Molecular Chaperones, Protein Transport, Cellular Microenvironment

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Spatial sequestration of misfolded proteins by a dynamic chaperone pathway enhances cellular fitness during stress

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