ArticleScientific reports2017
Identification of Key Residues for Urate Specific Transport in Human Glucose Transporter 9 (hSLC2A9).
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 10 citations in OpenAlex.
- SLC2A9-Mediated Uric Acid Homeostasis Modulates Apoptosis in TNBC.Breast cancer (Dove Medical Press) · 2026Article
- Structural basis of disease mutation and substrate recognition by the human SLC2A9 transporter.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Fatty Acid-Rich Extract fromMolecules (Basel, Switzerland) · 2023Article
- Potentially Functional Genetic Variants in the NRF2 Signaling Pathway Genes are Associated With HBV-related Hepatocellular Carcinoma Survival.Journal of Cancer · 2023Article
- Urate transport capacity of glucose transporter 9 and urate transporter 1 in cartilage chondrocytes.Molecular medicine reports · 2019Article
- Overexpression of Uric Acid Transporter SLC2A9 Inhibits Proliferation of Hepatocellular Carcinoma Cells.Oncology research · 2019Article
- Large-scale whole-exome sequencing association studies identify rare functional variants influencing serum urate levels.Nature communications · 2018Article
- Human Mutations in SLC2A9 (Glut9) Affect Transport Capacity for Urate.Frontiers in physiology · 2018Article
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Authors and funding
8 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Human glucose transporter 9 (hSLC2A9) is critical in human urate homeostasis, for which very small deviations can lead to chronic or acute metabolic disorders. Human SLC2A9 is unique in that it transports hexoses as well as the organic anion, urate. This ability is in contrast to other homologous sugar transporters such as glucose transporters 1 and 5 (SLC2A1 &SLC2A5) and the xylose transporter (XylE), despite the fact that these transporters have similar protein structures. Our in silico substrate docking study has revealed that urate and fructose bind within the same binding pocket in hSLC2A9, yet with distinct orientations, and allowed us to identify novel residues for urate binding. Our functional studies confirmed that N429 is a key residue for both urate binding and transport. We have shown that cysteine residues, C181, C301 and C459 in hSLC2A9 are also essential elements for mediating urate transport. Additional data from chimæric protein analysis illustrated that transmembrane helix 7 of hSLC2A9 is necessary for urate transport but not sufficient to allow urate transport to be induced in glucose transporter 5 (hSLC2A5). These data indicate that urate transport in hSLC2A9 involves several structural elements rather than just a unique substrate binding pocket.
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