ArticleThe Biochemical journal2004
Functional features and genomic organization of mouse NaCT, a sodium-coupled transporter for tricarboxylic acid cycle intermediates.
Article in The Biochemical journal, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.
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52 citing papers in PubMed, 86 citations in OpenAlex.
- Review
- Structures of the human sodium-citrate cotransporter NaCT with and without substrates.Structure (London, England : 1993) · 2026Article
- Structures of the human sodium-citrate cotransporter NaCT with and without substrates.bioRxiv : the preprint server for biology · 2026Article
- Discovery and Characterization of a Nonacidic Small-Molecule Inhibitor of the Sodium-Coupled Dicarboxylate Transporter NaCT.Journal of medicinal chemistry · 2026Article
- Citrate Transporter Expression and Localization: TheInternational journal of molecular sciences · 2025Article
- Cryo-EM structures reveal the HLife science alliance · 2025Article
- Structural basis for the reaction cycle and transport mechanism of human NaScience advances · 2024Article
- Targeting Solute Carrier Transporters (SLCs) as a Therapeutic Target in Different Cancers.Diseases (Basel, Switzerland) · 2024Review
- Metabolic basis of solute carrier transporters in treatment of type 2 diabetes mellitus.Acta pharmaceutica Sinica. B · 2024Review
- Targeting Longevity GeneMetabolites · 2023Article
- Prognostic 7-SLC-Gene Signature Identified via Weighted Gene Co-Expression Network Analysis for Patients with Hepatocellular Carcinoma.Journal of oncology · 2023Article
- Review
- Binding of Citrate-FeInternational journal of molecular sciences · 2022Article
- Untargeted Metabolomics of Slc13a5 Deficiency Reveal Critical Liver-Brain Axis for Lipid Homeostasis.Metabolites · 2022Article
- Metabolic Alterations in Cellular Senescence: The Role of Citrate in Ageing and Age-Related Disease.International journal of molecular sciences · 2022Review
- The ups and downs of elevator-type di-/tricarboxylate membrane transporters.The FEBS journal · 2022Article
- Phenobarbital Induces SLC13A5 Expression through Activation of PXR but Not CAR in Human Primary Hepatocytes.Cells · 2021Article
- Thermostability-based binding assays reveal complex interplay of cation, substrate and lipid binding in the bacterial DASS transporter, VcINDY.The Biochemical journal · 2021Article
- Review
- Molecular Mechanisms of the SLC13A5 Gene Transcription.Metabolites · 2021Review
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6 authors at 1 institution in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
In the present study, we report on the molecular cloning and functional characterization of mouse NaCT (Na+-coupled citrate transporter), the mouse orthologue of Drosophila Indy. Mouse NaCT consists of 572 amino acids and is highly similar to rat and human NaCTs in primary sequence. The mouse nact gene coding for the transporter is approx. 23 kb long and consists of 12 exons. When expressed in mammalian cells, the cloned transporter mediates the Na+-coupled transport of citrate and succinate. Competition experiments reveal that mouse NaCT also recognizes other tricarboxylic acid cycle intermediates such as malate, fumarate and 2-oxo-glutarate as excellent substrates. The Michaelis-Menten constant for the transport process is 38+/-5 mM for citrate and 37+/-6 mM for succinate at pH 7.5. The transport process is electrogenic and exhibits an obligatory requirement for Na+. Na+-activation kinetics indicates that multiple Na+ ions are involved in the activation process. Extracellular pH has a differential effect on the transport function of mouse NaCT depending on whether the transported substrate is citrate or succinate. The Michaelis-Menten constants for these substrates are also influenced markedly by pH. When examined in the Xenopus laevis oocyte expression system with the two-microelectrode voltage-clamp technique, the transport process mediated by mouse NaCT is electrogenic. The charge-to-substrate ratio is 1 for citrate and 2 for succinate. The most probable transport mechanism predicted by these studies involves the transport of citrate as a tervalent anion and succinate as a bivalent anion with a fixed Na+/substrate stoichiometry of 4:1. The present study provides the first unequivocal evidence for the electrogenic nature of mammalian NaCT.
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