ArticleThe Journal of cell biology2024
Mitochondrial-derived compartments remove surplus proteins from the outer mitochondrial membrane.
Article in The Journal of cell biology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
What it found
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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
11 citing papers in PubMed.
- Mitochondrial-derived compartments buffer outer membrane protein load during acute mitochondrial adaptation.bioRxiv : the preprint server for biology · 2026Article
- Novel therapeutic strategies targeting mitochondrial quality control for metabolic dysfunction-associated steatotic liver disease.Frontiers in physiology · 2026Review
- The tumor suppressor LACTB remodels mitochondria to promote cytochrome c release and apoptosis.Science advances · 2025Article
- Alterations in lipid saturation trigger remodeling of the outer mitochondrial membrane.Molecular biology of the cell · 2025Article
- Mitochondrial quality control in diabetes mellitus and complications: molecular mechanisms and therapeutic strategies.Cell death & disease · 2025Review
- Mitochondrial fission - changing perspectives for future progress.Journal of cell science · 2025Review
- Mitochondrial protein import stress.Nature cell biology · 2025Review
- Mitochondrial-derived compartments are multilamellar domains that encase membrane cargo and cytosol.The Journal of cell biology · 2024Article
- Amino acids trigger MDC-dependent mitochondrial remodeling by altering mitochondrial function.bioRxiv : the preprint server for biology · 2024Article
- The phospholipids cardiolipin and phosphatidylethanolamine differentially regulate MDC biogenesis.The Journal of cell biology · 2024Article
- Mitochondrial-Derived Compartments are Multilamellar Domains that Encase Membrane Cargo and Cytosol.bioRxiv : the preprint server for biology · 2023Article
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
The outer mitochondrial membrane (OMM) creates a boundary that imports most of the mitochondrial proteome while removing extraneous or damaged proteins. How the OMM senses aberrant proteins and remodels to maintain OMM integrity remains unresolved. Previously, we identified a mitochondrial remodeling mechanism called the mitochondrial-derived compartment (MDC) that removes a subset of the mitochondrial proteome. Here, we show that MDCs specifically sequester proteins localized only at the OMM, providing an explanation for how select mitochondrial proteins are incorporated into MDCs. Remarkably, selective sorting into MDCs also occurs within the OMM, as subunits of the translocase of the outer membrane (TOM) complex are excluded from MDCs unless assembly of the TOM complex is impaired. Considering that overloading the OMM with mitochondrial membrane proteins or mistargeted tail-anchored membrane proteins induces MDCs to form and sequester these proteins, we propose that one functional role of MDCs is to create an OMM-enriched trap that segregates and sequesters excess proteins from the mitochondrial surface.
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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 Socratic graph.