ArticleThe EMBO journal2007
The morphology proteins Mdm12/Mmm1 function in the major beta-barrel assembly pathway of mitochondria.
Article in The EMBO journal, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 62 papers.
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Who cites it
62 citing papers in PubMed.
- Biogenesis of mitochondrial β-barrel membrane proteins.FEBS open bio · 2024Review
- Modular Assembly of Mitochondrial β-Barrel Proteins.Methods in molecular biology (Clifton, N.J.) · 2024Article
- The Name Is Barrel, β-Barrel.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
- Mitochondria-associated endoplasmic reticulum membrane: Overview and inextricable link with cancer.Journal of cellular and molecular medicine · 2023Review
- Crosstalk between Mitochondrial Protein Import and Lipids.International journal of molecular sciences · 2022Review
- Building Better Barrels - β-barrel Biogenesis and Insertion in Bacteria and Mitochondria.Journal of molecular biology · 2021Review
- Insertion of plastidic β-barrel proteins into the outer envelopes of plastids involves an intermembrane space intermediate formed with Toc75-V/OEP80.The Plant cell · 2021Article
- Article
- Emr1 regulates the number of foci of the endoplasmic reticulum-mitochondria encounter structure complex.Nature communications · 2021Article
- Mechanisms of Non-Vesicular Exchange of Lipids at Membrane Contact Sites: Of Shuttles, Tunnels and, Funnels.Frontiers in cell and developmental biology · 2021Review
- Solid-phase inclusion as a mechanism for regulating unfolded proteins in the mitochondrial matrix.Science advances · 2020Article
- Article
- Transcriptional responses ofNPJ biofilms and microbiomes · 2020Article
- Mitochondria-Associated Membranes (MAMs) are involved in Bax mitochondrial localization and cytochrome c release.Microbial cell (Graz, Austria) · 2019Article
- Article
- Crystal structures of Mmm1 and Mdm12-Mmm1 reveal mechanistic insight into phospholipid trafficking at ER-mitochondria contact sites.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Endoplasmic reticulum-mitochondria junction is required for iron homeostasis.The Journal of biological chemistry · 2017Article
- Revisiting trends on mitochondrial mega-channels for the import of proteins and nucleic acids.Journal of bioenergetics and biomembranes · 2017Review
- Crystal structure of Mdm12 reveals the architecture and dynamic organization of the ERMES complex.EMBO reports · 2016Article
2 more citing papers are in PubMed but not listed here.
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Authors and funding
12 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The beta-barrel proteins of mitochondria are synthesized on cytosolic ribosomes. The proteins are imported by the translocase of the outer membrane (TOM) and the sorting and assembly machinery (SAM). It has been assumed that the SAM(core) complex with the subunits Sam35, Sam37 and Sam50 represents the last import stage common to all beta-barrel proteins, followed by splitting in a Tom40-specific route and a route for other beta-barrel proteins. We have identified new components of the beta-barrel assembly machinery and show that the major beta-barrel pathway extends beyond SAM(core). Mdm12/Mmm1 function after SAM(core) yet before splitting of the major pathway. Mdm12/Mmm1 have been known for their role in maintenance of mitochondrial morphology but we reveal assembly of beta-barrel proteins as their primary function. Moreover, Mdm10, which functions in the Tom40-specific route, can associate with SAM(core) as well as Mdm12/Mmm1 to form distinct assembly complexes, indicating a dynamic exchange between the machineries governing mitochondrial beta-barrel assembly. We conclude that assembly of mitochondrial beta-barrel proteins represents a major function of the morphology proteins Mdm12/Mmm1.
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