ArticleNature communications2016
Separating mitochondrial protein assembly and endoplasmic reticulum tethering by selective coupling of Mdm10.
Article in Nature communications, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.
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Who cites it
49 citing papers in PubMed.
- Mitochondrially tethered Mmm1 can function as a sole lipid transporter at ER-mitochondria contacts.The Journal of cell biology · 2026Article
- The TOM Complex in the Outer Membrane of Mitochondria: A Supramolecular Assembly for Protein Import.Advances in experimental medicine and biology · 2026Review
- Functional role ofVirulence · 2025Article
- Molecular machineries and pathways of mitochondrial protein transport.Nature reviews. Molecular cell biology · 2025Review
- Mitochondria-plasma membrane contact sites regulate the ER-mitochondria encounter structure.Journal of cell science · 2025Article
- Review
- New insights into the structure and dynamics of the TOM complex in mitochondria.Biochemical Society transactions · 2024Review
- The ER-SURF pathway uses ER-mitochondria contact sites for protein targeting to mitochondria.EMBO reports · 2024Article
- Modular Assembly of Mitochondrial β-Barrel Proteins.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Multiple tethers of organelle contact sites are involved in α-synuclein toxicity in yeast.Molecular biology of the cell · 2023Article
- Article
- Article
- A multipoint guidance mechanism for β-barrel folding on the SAM complex.Nature structural & molecular biology · 2023Article
- The metabolite-controlled ubiquitin conjugase Ubc8 promotes mitochondrial protein import.Life science alliance · 2023Article
- Mechanistic insights into fungal mitochondrial outer membrane protein biogenesis.Current opinion in structural biology · 2022Review
- Crosstalk between Mitochondrial Protein Import and Lipids.International journal of molecular sciences · 2022Review
- Mitochondrial protein translocation machinery: From TOM structural biogenesis to functional regulation.The Journal of biological chemistry · 2022Review
- ER-misfolded proteins become sequestered with mitochondria and impair mitochondrial function.Communications biology · 2021Article
- Subunit exchange among endolysosomal tethering complexes is linked to contact site formation at the vacuole.Molecular biology of the cell · 2021Article
- Cnm1 mediates nucleus-mitochondria contact site formation in response to phospholipid levels.The Journal of cell biology · 2021Article
Corrections and comments
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Authors and funding
16 authors.
Funding
Abstract
The endoplasmic reticulum-mitochondria encounter structure (ERMES) connects the mitochondrial outer membrane with the ER. Multiple functions have been linked to ERMES, including maintenance of mitochondrial morphology, protein assembly and phospholipid homeostasis. Since the mitochondrial distribution and morphology protein Mdm10 is present in both ERMES and the mitochondrial sorting and assembly machinery (SAM), it is unknown how the ERMES functions are connected on a molecular level. Here we report that conserved surface areas on opposite sides of the Mdm10 β-barrel interact with SAM and ERMES, respectively. We generated point mutants to separate protein assembly (SAM) from morphology and phospholipid homeostasis (ERMES). Our study reveals that the β-barrel channel of Mdm10 serves different functions. Mdm10 promotes the biogenesis of α-helical and β-barrel proteins at SAM and functions as integral membrane anchor of ERMES, demonstrating that SAM-mediated protein assembly is distinct from ER-mitochondria contact sites.
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