ArticleProceedings of the National Academy of Sciences of the United States of America2014
Structures of yeast mitochondrial ADP/ATP carriers support a domain-based alternating-access transport mechanism.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 140 papers.
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140 citing papers in PubMed, 222 citations in OpenAlex.
- Molecular mechanisms of mitochondrial uncoupling: focus on 2,4-dinitrophenol.European biophysics journal : EBJ · 2026Review
- The SLC-ome of membrane transport: from molecular discovery to physiology and clinical applications.Physiological reviews · 2026Review
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- Higher-order structural organization of mitochondrial metabolism.The Journal of biological chemistry · 2026Review
- Structural evolution of the MTCH family of mitochondrial insertases.Science advances · 2026Article
- A Structural Context for the Mechanisms of Uncoupling Protein 1 in Brown Fat Thermogenesis.Acta physiologica (Oxford, England) · 2026Review
- Structural evolution of the MTCH family of mitochondrial insertases.bioRxiv : the preprint server for biology · 2026Article
- From the cytosol to the inner membrane: biogenesis of the mitochondrial carrier family.Protein science : a publication of the Protein Society · 2026Review
- Natural Product Driven Activation of UCP1 and Tumor Metabolic Suppression: Integrating Thermogenic Nutrient Competition with Cancer Metabolic Reprogramming.Biomolecules · 2026Review
- Detecting the body's reproductive hormonal brake against tissue overgrowth: Micrin/SgII-70.PloS one · 2026Article
- SLC25A mitochondrial carriers as biomarkers and therapeutic targets of spaceflight-induced dysfunction: the ADP/ATP carrier (AAC3) as a structural case study.Journal of translational medicine · 2025Article
- Biogenesis and function of the mitochondrial solute carrier (SLC25) family in yeast.Biological chemistry · 2025Review
- Mitochondrial NADScience advances · 2025Article
- SLC25A45 is required for mitochondrial uptake of methylated amino acids and de novo carnitine biosynthesis.Molecular cell · 2025Article
- Discovery of therapeutic AGC2 modulators by combining docking, binding, and vesicle-based transport assays.Journal of translational medicine · 2025Article
- Selective loss of ATP carriers in favour of SLC25A43 orthologues in metamonad mitochondria adapted to anaerobiosis.Open biology · 2025Article
- The peculiar properties of mitochondrial carriers of the SLC25 family.The Biochemical journal · 2025Review
- Proton conductance by human uncoupling protein 1 is inhibited by purine and pyrimidine nucleotides.The EMBO journal · 2025Article
- Current Understanding of Pathogenic Mechanisms and Disease Models of Citrin Deficiency.Journal of inherited metabolic disease · 2025Review
- My path to citrin deficiency.Journal of inherited metabolic disease · 2025Review
80 more citing papers are in PubMed but not listed here.
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
Abstract
The mitochondrial ADP/ATP carrier imports ADP from the cytosol and exports ATP from the mitochondrial matrix. The carrier cycles by an unresolved mechanism between the cytoplasmic state, in which the carrier accepts ADP from the cytoplasm, and the matrix state, in which it accepts ATP from the mitochondrial matrix. Here we present the structures of the yeast ADP/ATP carriers Aac2p and Aac3p in the cytoplasmic state. The carriers have three domains and are closed at the matrix side by three interdomain salt-bridge interactions, one of which is braced by a glutamine residue. Glutamine braces are conserved in mitochondrial carriers and contribute to an energy barrier, preventing the conversion to the matrix state unless substrate binding occurs. At the cytoplasmic side a second salt-bridge network forms during the transport cycle, as demonstrated by functional analysis of mutants with charge-reversed networks. Analyses of the domain structures and properties of the interdomain interfaces indicate that interconversion between states involves movement of the even-numbered α-helices across the surfaces of the odd-numbered α-helices by rotation of the domains. The odd-numbered α-helices have an L-shape, with proline or serine residues at the kinks, which functions as a lever-arm, coupling the substrate-induced disruption of the matrix network to the formation of the cytoplasmic network. The simultaneous movement of three domains around a central translocation pathway constitutes a unique mechanism among transport proteins. These findings provide a structural description of transport by mitochondrial carrier proteins, consistent with an alternating-access mechanism.
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