ArticleThe Journal of biological chemistry2014
Determinants of substrate and cation transport in the human Na+/dicarboxylate cotransporter NaDC3.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 35 citations in OpenAlex.
- Focally administered succinate improves cerebral metabolism in traumatic brain injury patients with mitochondrial dysfunction.Journal of cerebral blood flow and metabolism : official journal of the International Society of Cerebral Blood Flow and Metabolism · 2022Trial
- Functional role of a structural water in the elevator domain of dicarboxylate transporter VcINDY.PNAS nexus · 2026Article
- Liver-specific SLC13A3 modulation alleviates MASLD by regulating NADMolecular and cellular biochemistry · 2026Article
- Metabolic Symbiosis Between Cancer Cells and Endothelial Cells: A Key Driver of Tumor Angiogenesis.Advances in experimental medicine and biology · 2026Review
- Emerging roles of the metabolite succinate in bone-related diseases.Journal of Zhejiang University. Science. B · 2025Review
- Substrate translocation and inhibition in human dicarboxylate transporter NaDC3.Nature structural & molecular biology · 2025Article
- The metabolic-epigenetic interface: lysine succinylation orchestrates bidirectional crosstalk in neurodegenerative disorders.Frontiers in neurology · 2025Review
- The impact of solute carrier proteins on disrupting substance regulation in metabolic disorders: insights and clinical applications.Frontiers in pharmacology · 2024Review
- The pathogenesis of, and pharmacological treatment for, Canavan disease.Drug discovery today · 2022Review
- Thermostability-based binding assays reveal complex interplay of cation, substrate and lipid binding in the bacterial DASS transporter, VcINDY.The Biochemical journal · 2021Article
- Article
- Human neurons from Christianson syndrome iPSCs reveal mutation-specific responses to rescue strategies.Science translational medicine · 2021Article
- INDY-From Flies to Worms, Mice, Rats, Non-Human Primates, and Humans.Frontiers in aging · 2021Review
- Solvent accessibility changes in a NaThe Journal of biological chemistry · 2020Article
- Proteome sequencing and analysis of Ophiocordyceps sinensis at different culture periods.BMC genomics · 2020Article
- Discovery of Potent Inhibitors for the Large Neutral Amino Acid Transporter 1 (LAT1) by Structure-Based Methods.International journal of molecular sciences · 2018Article
- Analysis of naturally occurring mutations in the human uptake transporter NaCT important for bone and brain development and energy metabolism.Scientific reports · 2018Article
- The effect of succinate on brain NADH/NADScientific reports · 2018Article
- Focally perfused succinate potentiates brain metabolism in head injury patients.Journal of cerebral blood flow and metabolism : official journal of the International Society of Cerebral Blood Flow and Metabolism · 2017Article
- Structure and function of the divalent anion/NaNature communications · 2017Article
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Metabolic intermediates, such as succinate and citrate, regulate important processes ranging from energy metabolism to fatty acid synthesis. Cytosolic concentrations of these metabolites are controlled, in part, by members of the SLC13 gene family. The molecular mechanism underlying Na(+)-coupled di- and tricarboxylate transport by this family is understood poorly. The human Na(+)/dicarboxylate cotransporter NaDC3 (SLC13A3) is found in various tissues, including the kidney, liver, and brain. In addition to citric acid cycle intermediates such as α-ketoglutarate and succinate, NaDC3 transports other compounds into cells, including N-acetyl aspartate, mercaptosuccinate, and glutathione, in keeping with its dual roles in cell nutrition and detoxification. In this study, we construct a homology structural model of NaDC3 on the basis of the structure of the Vibrio cholerae homolog vcINDY. Our computations are followed by experimental testing of the predicted NaDC3 structure and mode of interaction with various substrates. The results of this study show that the substrate and cation binding domains of NaDC3 are composed of residues in the opposing hairpin loops and unwound portions of adjacent helices. Furthermore, these results provide a possible explanation for the differential substrate specificity among dicarboxylate transporters that underpin their diverse biological roles in metabolism and detoxification. The structural model of NaDC3 provides a framework for understanding substrate selectivity and the Na(+)-coupled anion transport mechanism by the human SLC13 family and other key solute carrier transporters.
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