ArticleProtein science : a publication of the Protein Society2025
Ancestral sequence reconstruction of the Mic60 Mitofilin domain reveals residues supporting respiration in yeast.
Article in Protein science : a publication of the Protein Society, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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4 citing papers in PubMed.
- The molecular mechanisms of crista formation: how mitochondria give themselves breathing room.Biochemical Society transactions · 2026Review
- MICOS and MIMAS, multifunctional assemblies linking mitochondrial biogenesis, architecture, and function.Protein science : a publication of the Protein Society · 2026Review
- The Core MICOS Complex Subunit mic60 has Been Substituted by Two Cryptic Mitofilin-containing Proteins in Euglenozoa.Molecular biology and evolution · 2025Article
- Ancestral sequence reconstruction of the Mic60 Mitofilin domain reveals residues supporting respiration in yeast.Protein science : a publication of the Protein Society · 2025Article
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12 authors.
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Abstract
In eukaryotes, cellular respiration takes place in the cristae of mitochondria. The mitochondrial inner membrane protein Mic60, a core component of the mitochondrial contact site and cristae organizing system, is crucial for the organization and stabilization of crista junctions and its associated functions. While the C-terminal Mitofilin domain of Mic60 is necessary for cellular respiration, the sequence determinants for this function have remained unclear. Here, we used ancestral sequence reconstruction to generate Mitofilin ancestors up to and including the last opisthokont common ancestor (LOCA). We found that yeast-lineage derived Mitofilin ancestors as far back as the LOCA rescue respiration. By comparing Mitofilin ancestors, we identified four residues sufficient to explain the respiratory difference between yeast- and animal-derived Mitofilin ancestors. Our results provide a foundation for investigating the conservation of Mic60-mediated cristae junction interactions.
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