ArticleThe Journal of cell biology2018
Cytosolic Hsp70 and Hsp40 chaperones enable the biogenesis of mitochondrial β-barrel proteins.
Article in The Journal of cell biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.
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Who cites it
54 citing papers in PubMed, 115 citations in OpenAlex.
- A multilayered stress-response circuit: The mammalian mitochondrial UPR.The FEBS journal · 2026Review
- Dynamic disorder is crucial for mitochondrial protein import.Protein science : a publication of the Protein Society · 2026Review
- The role of the nucleus in the control of mitochondrial precursor proteins in yeast.Protein science : a publication of the Protein Society · 2026Review
- Functions of J-domain proteins in mitochondrial protein biogenesis.Protein science : a publication of the Protein Society · 2026Review
- The IQ-compete assay for measuring mitochondrial protein import efficiencies in living yeast cells.FEBS letters · 2026Article
- Molecular machineries and pathways of mitochondrial protein transport.Nature reviews. Molecular cell biology · 2025Review
- Navigating the landscape of protein folding and proteostasis: from molecular chaperones to therapeutic innovations.Signal transduction and targeted therapy · 2025Review
- Mpf1 affects the dual distribution of tail-anchored proteins between mitochondria and peroxisomes.EMBO reports · 2025Article
- Review
- Chaperone-mediated insertion of mitochondrial import receptor TOM70 protects against diet-induced obesity.Nature cell biology · 2025Article
- Oxidative protein folding in the intermembrane space of human mitochondria.FEBS open bio · 2024Review
- Biogenesis of mitochondrial β-barrel membrane proteins.FEBS open bio · 2024Review
- Gonococcal OMV-delivered PorB induces epithelial cell mitophagy.Nature communications · 2024Article
- J-domain proteins: From molecular mechanisms to diseases.Cell stress & chaperones · 2024Article
- Dynamic stability of Sgt2 enables selective and privileged client handover in a chaperone triad.Nature communications · 2024Article
- Modular Assembly of Mitochondrial β-Barrel Proteins.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Independent organelle and organelle-organelle interactions: essential mechanisms for malignant gynecological cancer cell survival.Frontiers in immunology · 2024Review
- Prefoldin 2 contributes to mitochondrial morphology and function.BMC biology · 2023Article
- MitoStores: chaperone-controlled protein granules store mitochondrial precursors in the cytosol.The EMBO journal · 2023Article
- Analysis of the Interactome of theProteomes · 2023Article
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Authors and funding
11 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Mitochondrial β-barrel proteins are encoded in the nucleus, translated by cytosolic ribosomes, and then imported into the organelle. Recently, a detailed understanding of the intramitochondrial import pathway of β-barrel proteins was obtained. In contrast, it is still completely unclear how newly synthesized β-barrel proteins reach the mitochondrial surface in an import-competent conformation. In this study, we show that cytosolic Hsp70 chaperones and their Hsp40 cochaperones Ydj1 and Sis1 interact with newly synthesized β-barrel proteins. These interactions are highly relevant for proper biogenesis, as inhibiting the activity of the cytosolic Hsp70, preventing its docking to the mitochondrial receptor Tom70, or depleting both Ydj1 and Sis1 resulted in a significant reduction in the import of such substrates into mitochondria. Further experiments demonstrate that the interactions between β-barrel proteins and Hsp70 chaperones and their importance are conserved also in mammalian cells. Collectively, this study outlines a novel mechanism in the early events of the biogenesis of mitochondrial outer membrane β-barrel proteins.
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