ArticleProceedings of the National Academy of Sciences of the United States of America2016
Helical arrays of U-shaped ATP synthase dimers form tubular cristae in ciliate mitochondria.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.
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Who cites it
45 citing papers in PubMed, 73 citations in OpenAlex.
- Article
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- Electron tomography reveals mitochondrial network and cristae remodelling during cell differentiation in the human placenta.Nature communications · 2026Article
- Mitochondrial super complexes in the colorless chlorophycean alga Polytomella parva.Journal of bioenergetics and biomembranes · 2026Article
- High-Resolution Imaging Reveals Mitochondrial Protein Imbalance in Sperm of Oligoasthenospermic Men.Molecular reproduction and development · 2026Article
- Proteolytic processing of the unique FScientific reports · 2026Article
- Microscopy in mitochondrial research - a comprehensive review.Journal of cell science · 2026Review
- Targeting mitochondrial translation and OXPHOS in high-grade serous ovarian carcinoma eliminates stem-like cells.Cell death & disease · 2025Article
- Molecular machineries shaping the mitochondrial inner membrane.Nature reviews. Molecular cell biology · 2025Review
- Article
- Mitochondria structurally remodel near synapses to fuel the sustained energy demands of plasticity.bioRxiv : the preprint server for biology · 2025Article
- Implications of mitochondrial membrane potential gradients on signaling and ATP production analyzed by correlative multi-parameter microscopy.Scientific reports · 2024Article
- The consequence of ATP synthase dimer angle on mitochondrial morphology studied by cryo-electron tomography.The Biochemical journal · 2024Article
- Structures of Tetrahymena thermophila respiratory megacomplexes on the tubular mitochondrial cristae.Nature communications · 2023Article
- Article
- The mystery of massive mitochondrial complexes: the apicomplexan respiratory chain.Trends in parasitology · 2022Review
- Mitochondria: intracellular sentinels of infections.Medical microbiology and immunology · 2022Review
- Structures ofScience (New York, N.Y.) · 2022Article
- Article
- Forty years in cryoEM of membrane proteins.Microscopy (Oxford, England) · 2022Article
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
F1Fo-ATP synthases are universal energy-converting membrane protein complexes that synthesize ATP from ADP and inorganic phosphate. In mitochondria of yeast and mammals, the ATP synthase forms V-shaped dimers, which assemble into rows along the highly curved ridges of lamellar cristae. Using electron cryotomography and subtomogram averaging, we have determined the in situ structure and organization of the mitochondrial ATP synthase dimer of the ciliate Paramecium tetraurelia. The ATP synthase forms U-shaped dimers with parallel monomers. Each complex has a prominent intracrista domain, which links the c-ring of one monomer to the peripheral stalk of the other. Close interaction of intracrista domains in adjacent dimers results in the formation of helical ATP synthase dimer arrays, which differ from the loose dimer rows in all other organisms observed so far. The parameters of the helical arrays match those of the cristae tubes, suggesting the unique features of the P. tetraurelia ATP synthase are directly responsible for generating the helical tubular cristae. We conclude that despite major structural differences between ATP synthase dimers of ciliates and other eukaryotes, the formation of ATP synthase dimer rows is a universal feature of mitochondria and a fundamental determinant of cristae morphology.
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