ArticleJournal of cell science2016
Vulnerability of newly synthesized proteins to proteostasis stress.
Article in Journal of cell science, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
23 citing papers in PubMed, 37 citations in OpenAlex.
- Transient ER stress cell-autonomously promotes beta cell cycling in mice.Diabetologia · 2026Article
- Native Fold Delay and its implications for co-translational chaperone binding and protein aggregation.Nature communications · 2025Article
- Limiting 20S proteasome assembly leads to unbalanced nucleo-cytoplasmic distribution of 26S/30S proteasomes and chronic proteotoxicity.iScience · 2024Article
- An adaptive biomolecular condensation response is conserved across environmentally divergent species.Nature communications · 2024Article
- Chaperone regulation of biomolecular condensates.Frontiers in biophysics · 2024Article
- The generation of detergent-insoluble clipped fragments from an ERAD substrate in mammalian cells.Scientific reports · 2023Article
- Proteostasis is differentially modulated by inhibition of translation initiation or elongation.eLife · 2023Article
- An adaptive biomolecular condensation response is conserved across environmentally divergent species.bioRxiv : the preprint server for biology · 2023Article
- Transcriptional lockdown during acute proteotoxic stress.Trends in biochemical sciences · 2022Review
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- Neonatal Maternal Separation Modifies Proteostasis Marker Expression in the Adult Hippocampus.Frontiers in molecular neuroscience · 2021Article
- Diversity in Aβ deposit morphology and secondary proteome insolubility across models of Alzheimer-type amyloidosis.Acta neuropathologica communications · 2020Article
- Functional Modules of the Proteostasis Network.Cold Spring Harbor perspectives in biology · 2020Review
- Emerging Evidence Highlighting the Importance of Redox Dysregulation in the Pathogenesis of Amyotrophic Lateral Sclerosis (ALS).Frontiers in cellular neuroscience · 2020Article
- Quantitative proteomics identifies proteins that resist translational repression and become dysregulated in ALS-FUS.Human molecular genetics · 2019Article
- Folding and Misfolding of Human Membrane Proteins in Health and Disease: From Single Molecules to Cellular Proteostasis.Chemical reviews · 2019Article
- Intrinsically aggregation-prone proteins form amyloid-like aggregates and contribute to tissue aging ineLife · 2019Article
- Nascent-protein ubiquitination is required for heat shock-induced gene downregulation in human cells.Nature structural & molecular biology · 2019Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
The capacity of the cell to produce, fold and degrade proteins relies on components of the proteostasis network. Multiple types of insults can impose a burden on this network, causing protein misfolding. Using thermal stress, a classic example of acute proteostatic stress, we demonstrate that ∼5-10% of the soluble cytosolic and nuclear proteome in human HEK293 cells is vulnerable to misfolding when proteostatic function is overwhelmed. Inhibiting new protein synthesis for 30 min prior to heat-shock dramatically reduced the amount of heat-stress induced polyubiquitylation, and reduced the misfolding of proteins identified as vulnerable to thermal stress. Following prior studies in C. elegans in which mutant huntingtin (Q103) expression was shown to cause the secondary misfolding of cytosolic proteins, we also demonstrate that mutant huntingtin causes similar 'secondary' misfolding in human cells. Similar to thermal stress, inhibiting new protein synthesis reduced the impact of mutant huntingtin on proteostatic function. These findings suggest that newly made proteins are vulnerable to misfolding when proteostasis is disrupted by insults such as thermal stress and mutant protein aggregation.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.