ArticleProceedings of the National Academy of Sciences of the United States of America2007
The yeast mitochondrial ADP/ATP carrier functions as a monomer in mitochondrial membranes.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.
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Who cites it
47 citing papers in PubMed, 96 citations in OpenAlex.
- Evolutionary history and recombination in the mitochondrial carrier SLC25 superfamily analyzed by similarities in the exon and transmembrane α-helix sequences.Protein science : a publication of the Protein Society · 2026Article
- Biogenesis and function of the mitochondrial solute carrier (SLC25) family in yeast.Biological chemistry · 2025Review
- The peculiar properties of mitochondrial carriers of the SLC25 family.The Biochemical journal · 2025Review
- Membrane potential stimulates ADP import and ATP export by the mitochondrial ADP/ATP carrier due to its positively charged binding site.Science advances · 2024Article
- Human mitochondrial carriers of the SLC25 family function as monomers exchanging substrates with a ping-pong kinetic mechanism.The EMBO journal · 2024Article
- Human mitochondrial ADP/ATP carrier SLC25A4 operates with a ping-pong kinetic mechanism.EMBO reports · 2023Article
- Bacterial over-expression of functionally active human CT2 (SLC22A16) carnitine transporter.Molecular biology reports · 2022Article
- Substrate binding in the mitochondrial ADP/ATP carrier is a step-wise process guiding the structural changes in the transport cycle.Nature communications · 2022Article
- Engineering artificial photosynthetic life-forms through endosymbiosis.Nature communications · 2022Article
- Review
- Peroxisomal ATP Uptake Is Provided by Two Adenine Nucleotide Transporters and the ABCD Transporters.Frontiers in cell and developmental biology · 2021Article
- A Single Cysteine Residue in the Translocation Pathway of the Mitosomal ADP/ATP Carrier fromInternational journal of molecular sciences · 2020Article
- The SLC25 Carrier Family: Important Transport Proteins in Mitochondrial Physiology and Pathology.Physiology (Bethesda, Md.) · 2020Review
- The mitochondrial ADP/ATP carrier exists and functions as a monomer.Biochemical Society transactions · 2020Review
- Cardiolipin, conformation, and respiratory complex-dependent oligomerization of the major mitochondrial ADP/ATP carrier in yeast.Science advances · 2020Article
- On the Detection and Functional Significance of the Protein-Protein Interactions of Mitochondrial Transport Proteins.Biomolecules · 2020Review
- A 20/20 view of ANT function in mitochondrial biology and necrotic cell death.Journal of molecular and cellular cardiology · 2020Review
- Article
- Emerging Roles in the Biogenesis of CytochromeFrontiers in cell and developmental biology · 2019Review
- Identification and quantification of proteinThe Journal of biological chemistry · 2017Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 3 countries.
Funding
Abstract
Mitochondrial carriers are believed widely to be dimers both in structure and function. However, the structural fold is a barrel of six transmembrane alpha-helices without an obvious dimerisation interface. Here, we show by negative dominance studies that the yeast mitochondrial ADP/ATP carrier 2 from Saccharomyces cerevisiae (AAC2) is functional as a monomer in the mitochondrial membrane. Adenine nucleotide transport by wild-type AAC2 is inhibited by the sulfhydryl reagent 2-sulfonatoethyl-methanethiosulfonate (MTSES), whereas the activity of a mutant AAC2, devoid of cysteines, is unaffected. Wild-type and cysteine-less AAC2 were coexpressed in different molar ratios in yeast mitochondrial membranes. After addition of MTSES the residual transport activity correlated linearly with the fraction of cysteine-less carrier present in the membranes, and so the two versions functioned independently of each other. Also, the cysteine-less and wild-type carriers were purified separately, mixed in defined ratios and reconstituted into liposomes. Again, the residual transport activity in the presence of MTSES depended linearly on the amount of cysteine-less carrier. Thus, the entire transport cycle for ADP/ATP exchange is carried out by the monomer.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.