ArticleThe Journal of cell biology2022
The multi-factor modulated biogenesis of the mitochondrial multi-span protein Om14.
Article in The Journal of cell biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- Molecular machineries and pathways of mitochondrial protein transport.Nature reviews. Molecular cell biology · 2025Review
- The mammalian protein MTCH1 can function as an insertase.Journal of cell science · 2025Article
- Mpf1 affects the dual distribution of tail-anchored proteins between mitochondria and peroxisomes.EMBO reports · 2025Article
- Protein insertion into the inner membrane of mitochondria: routes and mechanisms.FEBS open bio · 2024Review
- Jatonik polyherbal mixture induced rat liver MMPT pore opening in normal Wistar rat:Chinese herbal medicines · 2024Article
- Nascent mitochondrial proteins initiate the localized condensation of cytosolic protein aggregates on the mitochondrial surface.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Crosstalk between Mitochondrial Protein Import and Lipids.International journal of molecular sciences · 2022Review
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Authors and funding
4 authors.
Funding
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Abstract
The mitochondrial outer membrane (MOM) harbors proteins that traverse the membrane via several helical segments and are called multi-span proteins. To obtain new insights into the biogenesis of these proteins, we utilized yeast mitochondria and the multi-span protein Om14. Testing different truncation variants, we show that while only the full-length protein contains all the information that assures perfect targeting specificity, shorter variants are targeted to mitochondria with compromised fidelity. Employing a specific insertion assay and various deletion strains, we show that proteins exposed to the cytosol do not contribute significantly to the biogenesis process. We further demonstrate that Mim1 and Porin support optimal membrane integration of Om14 but none of them are absolutely required. Unfolding of newly synthesized Om14, its optimal hydrophobicity, and higher fluidity of the membrane enhanced the import capacity of Om14. Collectively, these findings suggest that MOM multi-span proteins follow different biogenesis pathways in which proteinaceous elements and membrane behavior contribute to a variable extent to the combined efficiency.
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