{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nSLC2A9, also known as GLUT9, is a multifunctional protein of the facilitative glucose transporter family that has emerged as a high‐capacity urate transporter. Initial genome‐wide association studies and linkage analyses demonstrated that common genetic variants in SLC2A9 contribute significantly to the inter‐individual variation observed in serum urate levels and predispose to hyperuricemia and gout, with these variants affecting renal urate handling and excretion."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "10"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn the kidney, SLC2A9 is critical for urate homeostasis. It is predominantly expressed in the proximal tubule, where it functions as an efflux transporter to move urate from renal epithelial cells into the bloodstream—a role substantiated by functional experiments using Xenopus laevis oocytes that reveal its robust, electrogenic urate transport activity. Moreover, distinct loss‐of‐function mutations and alternative splicing generating isoforms with different N‐terminal domains (such as GLUT9a and GLUT9b) have been linked to severe renal hypouricemia, nephrolithiasis, and exercise‐induced acute renal failure, underscoring its indispensable role in reabsorption mechanisms."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "11", "end_ref": "17"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond its renal function, SLC2A9 is expressed in a variety of tissues—including the liver, placenta, articular cartilage, and pancreatic beta‐cells—implying broader roles in metabolism beyond urate handling. Alternative splicing produces isoforms with differential subcellular localization, a feature that may tailor its function to specific cellular contexts. Notably, recent investigations have revealed a connection between SLC2A9 and cellular antioxidant defense—whereby p53‐dependent regulation of SLC2A9 expression helps modulate reactive oxygen species—and its capacity to transport not only urate but also hexose sugars underscores its dual roles in sugar flux and urate balance."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "18", "end_ref": "32"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nAdditional studies have expanded the clinical and therapeutic implications of SLC2A9. Its genetic variants have been associated not only with urate-related disorders such as gout but also with broader cardiometabolic conditions including hypertension, coronary heart disease, and even Parkinson’s disease through effects on serum urate levels. Furthermore, its role in placental glucose and urate transport suggests implications for fetal growth in diabetic pregnancies, while its substrate specificity—including the transport of adenine—may contribute to diverse metabolic processes. These multifaceted aspects position SLC2A9 as a promising molecular target for pharmacological intervention in hyperuricemia and its related complications."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "33", "end_ref": "40"}, {"type": "fg_f", "ref": "10"}, {"type": "fg_f", "ref": "41"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Veronique Vitart, Igor Rudan, Caroline Hayward, et al. 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