ArticleProceedings of the National Academy of Sciences of the United States of America2021
Interface mobility between monomers in dimeric bovine ATP synthase participates in the ultrastructure of inner mitochondrial membranes.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed, 44 citations in OpenAlex.
- Article
- Assembly of the catalytic module and the rotor of human ATP synthase.The EMBO journal · 2026Article
- A planar dimer of bovine ATP synthase.Cell death and differentiation · 2026Article
- An atypical F-type ATPase is necessary for the function of the antibody cleavage system MIB-MIP in mycoplasmas.PLoS pathogens · 2026Article
- Unconventional model organisms bend our view on mitochondrial cristae.Journal of cell science · 2026Review
- Dominant negative ATP5F1A variants disrupt oxidative phosphorylation causing neurological disorders.EMBO molecular medicine · 2025Article
- Molecular machineries shaping the mitochondrial inner membrane.Nature reviews. Molecular cell biology · 2025Review
- Cardiolipin acyl chain composition tailors the conformation of mammalian ATP synthase dimers.Communications chemistry · 2025Article
- Rare Evolutionary Events Support the Phylogenetic Placement of Orthonectida Within Annelida.International journal of molecular sciences · 2025Article
- Article
- Variants in Human ATP Synthase Mitochondrial Genes: Biochemical Dysfunctions, Associated Diseases, and Therapies.International journal of molecular sciences · 2024Review
- The consequence of ATP synthase dimer angle on mitochondrial morphology studied by cryo-electron tomography.The Biochemical journal · 2024Article
- Mitochondrial Cristae Morphology Reflecting Metabolism, Superoxide Formation, Redox Homeostasis, and Pathology.Antioxidants & redox signaling · 2023Review
- ATP synthase interactome analysis identifies a new subunit l as a modulator of permeability transition pore in yeast.Scientific reports · 2023Article
- The mitochondrial permeability transition: Recent progress and open questions.The FEBS journal · 2022Review
- An ancestral interaction module promotes oligomerization in divergent mitochondrial ATP synthases.Nature communications · 2022Article
- Melatonin: Regulation of Viral Phase Separation and Epitranscriptomics in Post-Acute Sequelae of COVID-19.International journal of molecular sciences · 2022Review
- Eraldo Antonini Lectures, 1983-2019.Biology direct · 2022Article
- Threshold of heteroplasmic truncating MT-ATP6 mutation in reprogramming, Notch hyperactivation and motor neuron metabolism.Human molecular genetics · 2022Article
- ATP synthase FCellular and molecular life sciences : CMLS · 2022Review
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Authors and funding
3 authors at 1 institution in 1 country.
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Abstract
The ATP synthase complexes in mitochondria make the ATP required to sustain life by a rotary mechanism. Their membrane domains are embedded in the inner membranes of the organelle, and they dimerize via interactions between their membrane domains. The dimers form extensive chains along the tips of the cristae with the two rows of monomeric catalytic domains extending into the mitochondrial matrix at an angle to each other. Disruption of the interface between dimers by mutation affects the morphology of the cristae severely. By analysis of particles of purified dimeric bovine ATP synthase by cryo-electron microscopy, we have shown that the angle between the central rotatory axes of the monomeric complexes varies between ca. 76 and 95°. These particles represent active dimeric ATP synthase. Some angular variations arise directly from the catalytic mechanism of the enzyme, and others are independent of catalysis. The monomer-monomer interaction is mediated mainly by j subunits attached to the surface of wedge-shaped protein-lipid structures in the membrane domain of the complex, and the angular variation arises from rotational and translational changes in this interaction, and combinations of both. The structures also suggest how the dimeric ATP synthases might be interacting with each other to form the characteristic rows along the tips of the cristae via other interwedge contacts, molding themselves to the range of oligomeric arrangements observed by tomography of mitochondrial membranes, and at the same time allowing the ATP synthase to operate under the range of physiological conditions that influence the structure of the cristae.
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