ArticleScience advances2020
Solid-phase inclusion as a mechanism for regulating unfolded proteins in the mitochondrial matrix.
Article in Science advances, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 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
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Who cites it
12 citing papers in PubMed, 26 citations in OpenAlex.
- Fluorescent TAPY-bodipy dyads as tools for imaging fungal mitochondria by confocal microscopy and flow cytometry.Analytical and bioanalytical chemistry · 2026Article
- When mitochondria lose their fold: matrix proteostasis and stress signaling.Frontiers in physiology · 2026Review
- Mitochondrial dysfunction in the regulation of aging and aging-related diseases.Cell communication and signaling : CCS · 2025Review
- Remodeling, compartmentalization, and degradation: a trifecta for organelle quality control during gametogenesis.Current opinion in genetics & development · 2025Review
- Spatial analysis of mitochondrial gene expression reveals dynamic translation hubs and remodeling in stress.Science advances · 2025Article
- Idiopathic Pulmonary Fibrosis Caused by Damaged Mitochondria and Imbalanced Protein Homeostasis in Alveolar Epithelial Type II Cell.Advanced biology · 2025Review
- A spatial atlas of mitochondrial gene expression reveals dynamic translation hubs and remodeling in stress.bioRxiv : the preprint server for biology · 2024Article
- Article
- Gene dosage adaptations to mtDNA depletion and mitochondrial protein stress in budding yeast.G3 (Bethesda, Md.) · 2024Article
- Biased placement of Mitochondria fission facilitates asymmetric inheritance of protein aggregates during yeast cell division.PLoS computational biology · 2023Article
- Newly imported proteins in mitochondria are particularly sensitive to aggregation.Acta physiologica (Oxford, England) · 2023Article
- Comprehensive characterization of the Hsp70 interactome reveals novel client proteins and interactions mediated by posttranslational modifications.PLoS biology · 2022Article
Corrections and comments
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Authors and funding
10 authors at 1 institution in 2 countries.
Funding
Abstract
Proteostasis declines with age, characterized by the accumulation of unfolded or damaged proteins. Recent studies suggest that proteins constituting pathological inclusions in neurodegenerative diseases also enter and accumulate in mitochondria. How unfolded proteins are managed within mitochondria remains unclear. Here, we found that excessive unfolded proteins in the mitochondrial matrix of yeast cells are consolidated into solid-phase inclusions, which we term deposits of unfolded mitochondrial proteins (DUMP). Formation of DUMP occurs in mitochondria near endoplasmic reticulum-mitochondria contact sites and is regulated by mitochondrial proteins controlling the production of cytidine 5'-diphosphate-diacylglycerol. DUMP formation is age dependent but accelerated by exogenous unfolded proteins. Many enzymes of the tricarboxylic acid cycle were enriched in DUMP. During yeast cell division, DUMP formation is necessary for asymmetric inheritance of damaged mitochondrial proteins between mother and daughter cells. We provide evidence that DUMP-like structures may be induced by excessive unfolded proteins in human cells.
Identifiers
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.