ArticleCell2014
Organelle-based aggregation and retention of damaged proteins in asymmetrically dividing cells.
Article in Cell, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 133 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
133 citing papers in PubMed, 249 citations in OpenAlex.
- Mitochondria-lysosome coupling contributes to lysosome acidification and aging.Molecular cell · 2026Article
- Next-Generation Bionic Sensors for Small Molecule Detection: Integrating Synthetic Biology, Nanomaterials, and Artificial Intelligence.Micromachines · 2026Review
- Nascent protein retention at polysomes reduces kinetic barriers to self-assembly.bioRxiv : the preprint server for biology · 2026Article
- ER stress induced mitochondrial dysfunction drives Treg instability in coronary artery disease.EMBO molecular medicine · 2025Article
- Hydroxyurea induces an oxidative stress response that triggers ER expansion and cytoplasmic protein aggregation.PLoS biology · 2025Article
- Cell membrane asymmetries and cellular aging.The Biochemical journal · 2025Review
- Transcriptome-wide mRNP condensation precedes stress granule formation and excludes new mRNAs.bioRxiv : the preprint server for biology · 2025Article
- Article
- Remodeling, compartmentalization, and degradation: a trifecta for organelle quality control during gametogenesis.Current opinion in genetics & development · 2025Review
- Crosstalk Between Phase-Separated Membraneless Condensates and Membrane-Bound Organelles in Cellular Function and Disease.Advances in experimental medicine and biology · 2025Review
- TDP43 aggregation at ER-exit sites impairs ER-to-Golgi transport.Nature communications · 2024Article
- Mitochondria-Associated Membranes in Aging and Senescence.Aging and disease · 2024Review
- StaufenC facilitates utilization of the ERAD pathway to transport dsRNA through the endoplasmic reticulum to the cytosol.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Premature aging in aneuploid yeast is caused in part by aneuploidy-induced defects in Ribosome Quality Control.bioRxiv : the preprint server for biology · 2024Article
- Enhancing mitochondrial proteolysis alleviates alpha-synuclein-mediated cellular toxicity.NPJ Parkinson's disease · 2024Article
- Article
- Elimination of virus-like particles reduces protein aggregation and extends replicative lifespan inProceedings of the National Academy of Sciences of the United States of America · 2024Article
- The ER-SURF pathway uses ER-mitochondria contact sites for protein targeting to mitochondria.EMBO reports · 2024Article
- GPI-anchored Gas1 protein regulates cytosolic proteostasis in budding yeast.G3 (Bethesda, Md.) · 2024Article
- Fission-independent compartmentalization of mitochondria during budding yeast cell division.The Journal of cell biology · 2024Article
73 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
10 authors at 2 institutions in 1 country.
Funding
Abstract
Aggregation of damaged or misfolded proteins is a protective mechanism against proteotoxic stress, abnormalities of which underlie many aging-related diseases. Here, we show that in asymmetrically dividing yeast cells, aggregation of cytosolic misfolded proteins does not occur spontaneously but requires new polypeptide synthesis and is restricted to the surface of ER, which harbors the majority of active translation sites. Protein aggregates formed on ER are frequently also associated with or are later captured by mitochondria, greatly constraining aggregate mobility. During mitosis, aggregates are tethered to well-anchored maternal mitochondria, whereas mitochondria acquired by the bud are largely free of aggregates. Disruption of aggregate-mitochondria association resulted in increased mobility and leakage of mother-accumulated aggregates into the bud. Cells with advanced replicative age exhibit gradual decline of aggregates-mitochondria association, likely contributing to their diminished ability to rejuvenate through asymmetric cell division.
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What OpenQuestion holds
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.