ArticleBiochimica et biophysica acta2015
Calcium-induced conformational changes in the regulatory domain of the human mitochondrial ATP-Mg/Pi carrier.
Article in Biochimica et biophysica acta, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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24 citing papers in PubMed, 44 citations in OpenAlex.
- 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
- My path to citrin deficiency.Journal of inherited metabolic disease · 2025Review
- Human mitochondrial carriers of the SLC25 family function as monomers exchanging substrates with a ping-pong kinetic mechanism.The EMBO journal · 2024Article
- Lactiplantibacillus plantarum as a novel platform for production and purification of integral membrane proteins using RseP as the benchmark.Scientific reports · 2023Article
- Organelle transporters and inter-organelle communication as drivers of metabolic regulation and cellular homeostasis.Molecular metabolism · 2022Review
- Tumor bud-derived CCL5 recruits fibroblasts and promotes colorectal cancer progression via CCR5-SLC25A24 signaling.Journal of experimental & clinical cancer research : CR · 2022Article
- Review
- AGC1 Deficiency: Pathology and Molecular and Cellular Mechanisms of the Disease.International journal of molecular sciences · 2022Review
- Exome sequencing identifies a disease variant of the mitochondrial ATP-Mg/Pi carrier SLC25A25 in two families with kidney stones.Molecular genetics & genomic medicine · 2021Article
- Metabolic implications of non-electrogenic ATP/ADP exchange in cancer cells: A mechanistic basis for the Warburg effect.Biochimica et biophysica acta. Bioenergetics · 2021Review
- 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
- Mitochondrial SLC25 Carriers: Novel Targets for Cancer Therapy.Molecules (Basel, Switzerland) · 2020Review
- Diseases Caused by Mutations in Mitochondrial Carrier GenesBiomolecules · 2020Review
- The SLC25 Mitochondrial Carrier Family: Structure and Mechanism.Trends in biochemical sciences · 2020Review
- Structural changes in the transport cycle of the mitochondrial ADP/ATP carrier.Current opinion in structural biology · 2019Review
- Calcium-regulated mitochondrial ATP-Mg/PIUBMB life · 2018Review
- The mitochondrial transporter SLC25A25 links ciliary TRPP2 signaling and cellular metabolism.PLoS biology · 2018Article
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Authors and funding
3 authors at 2 institutions in 1 country.
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Abstract
The mitochondrial ATP-Mg/Pi carrier imports adenine nucleotides from the cytosol into the mitochondrial matrix and exports phosphate. The carrier is regulated by the concentration of cytosolic calcium, altering the size of the adenine nucleotide pool in the mitochondrial matrix in response to energetic demands. The protein consists of three domains; (i) the N-terminal regulatory domain, which is formed of two pairs of fused calcium-binding EF-hands, (ii) the C-terminal mitochondrial carrier domain, which is involved in transport, and (iii) a linker region with an amphipathic α-helix of unknown function. The mechanism by which calcium binding to the regulatory domain modulates substrate transport in the carrier domain has not been resolved. Here, we present two new crystal structures of the regulatory domain of the human isoform 1. Careful analysis by SEC confirmed that although the regulatory domain crystallised as dimers, full-length ATP-Mg/Pi carrier is monomeric. Therefore, the ATP-Mg/Pi carrier must have a different mechanism of calcium regulation than the architecturally related aspartate/glutamate carrier, which is dimeric. The structure showed that an amphipathic α-helix is bound to the regulatory domain in a hydrophobic cleft of EF-hand 3/4. Detailed bioinformatics analyses of different EF-hand states indicate that upon release of calcium, EF-hands close, meaning that the regulatory domain would release the amphipathic α-helix. We propose a mechanism for ATP-Mg/Pi carriers in which the amphipathic α-helix becomes mobile upon release of calcium and could block the transport of substrates across the mitochondrial inner membrane.
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