{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nHuman concentrative nucleoside transporter 3 (hCNT3), encoded by SLC28A3, is a high‐affinity, broadly selective, sodium‐ and proton‐coupled transporter that mediates the cellular uptake of a wide spectrum of natural nucleosides—including both ribo‐ and deoxyribonucleosides—and many anticancer and antiviral nucleoside analogues. Detailed functional studies using electrophysiology, rapid kinetic measurements, and substituted cysteine accessibility methods have established that hCNT3 operates with distinct cation coupling stoichiometries (e.g. a 2:1 Na⁺/nucleoside stoichiometry in the presence of Na⁺ versus a 1:1 stoichiometry when H⁺ is the driving ion), and that key residues (such as conserved cysteines and glutamates) in its transmembrane domains critically determine ligand recognition and transport efficiency. Furthermore, high‐resolution cryo‐electron microscopy and molecular simulation studies have elucidated its trimeric organization, detailed translocation pathway, and the conformational changes of its mobile transport domain relative to a more static scaffold domain, thereby providing a mechanistic basis for its “elevator‐type” transport mechanism."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "17"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn addition to its core transport function, hCNT3 expression and localization are subject to sophisticated regulatory mechanisms. Multiple studies have documented its prominent expression in epithelial tissues such as kidney proximal tubules and pancreatic as well as hepatic tumors, where its apical insertion facilitates effective nucleoside reabsorption and drug uptake. Protein–protein interactions and post‐translational modifications critically influence hCNT3 trafficking—for example, interactions with regulatory factors like galectins or TGF‐β–dependent signaling cascades promote its relocation to the plasma membrane, thereby modulating transport activity in response to cellular differentiation or extracellular cues. These regulatory insights have been further bolstered by comparative expression analyses showing that hCNT3, often in tandem with other nucleoside transporters such as hENT1, underlies the salvaging of nucleosides in both normal physiology and in neoplastic tissues."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "18", "end_ref": "24"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nClinically, SLC28A3 has emerged as a key pharmacogenomic biomarker, with genetic variations and expression levels of hCNT3 influencing response to nucleoside analog–based chemotherapies. Elevated transporter expression has been associated with increased drug uptake and augmented cytotoxicity in treatments for pancreatic adenocarcinoma, acute myeloid leukemia, and chronic lymphocytic leukemia, while certain single‐nucleotide polymorphisms in SLC28A3 have been linked to altered drug disposition and even cardiotoxicity with anthracycline regimens. These findings highlight the dual importance of hCNT3 in not only maintaining nucleoside homeostasis but also modulating chemotherapy efficacy and toxicity profiles, thereby supporting its potential as a target for therapeutic intervention as well as for patient stratification in precision medicine."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "25", "end_ref": "31"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Shuy-Vang Toan, Kenneth K W To, George P H Leung, et al. 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