{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nTAS1R3 is a central component of mammalian taste reception, where it partners with either TAS1R2 to form the canonical sweet taste receptor or with TAS1R1 to detect umami‐tasting L‐amino acids. In gustatory cells, TAS1R3 contributes to a receptor complex that is broadly tuned for a variety of ligands—from natural sugars and artificial sweeteners to sweet proteins and amino acids—by employing multiple ligand–binding sites located in both its large extracellular Venus flytrap domain and its transmembrane region. Structure–function studies using mutagenesis, heterologous expression, and molecular dynamics simulations have identified key residues in the extracellular and transmembrane domains that determine ligand selectivity, allosteric modulation (for example by inhibitors such as lactisole and cyclamate), and species‐dependent sensitivity. Genetic variants upstream of TAS1R3 that affect promoter activity further contribute to the marked interindividual differences in sweet perception."}, {"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": "\nBeyond its well‐defined role in oral chemosensation, TAS1R3 is also expressed in several extra‐oral tissues where it appears to modulate diverse physiological processes. For example, TAS1R3–containing receptors in the gastrointestinal tract contribute to the regulation of nutrient‐dependent hormone secretion, influencing the release of incretin and satiation peptides. Expression in non‐gustatory tissues—including in the liver, pancreas, adipocytes, and even in sperm and retinal and immune cells—suggests an additional role in monitoring luminal chemical composition, mediating cellular metabolism and barrier functions, and possibly modulating inflammatory responses. Such extra‐oral functions indicate that TAS1R3 serves as an integrative sensor linking nutritional cues to systemic metabolic and cellular signaling pathways."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "18", "end_ref": "26"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nRecent molecular and genetic studies have further refined our understanding of TAS1R3’s regulatory mechanisms and structure. Advanced techniques—including high-resolution structural modeling, saturation transfer difference NMR spectroscopy, and comprehensive site-directed mutagenesis—have delineated the specific contributions of TAS1R3’s extracellular, cysteine-rich, and transmembrane domains in ligand binding, receptor activation, and intracellular signaling. In parallel, genetic association studies and single nucleotide polymorphism analyses have linked variations in TAS1R3 (and in its partner subunits) with altered taste perception, dietary habits, and even broader phenotypic outcomes such as dental caries and metabolic traits. Moreover, investigations into membrane trafficking have revealed that proper surface expression and dimerization of TAS1R3 are crucial for functional receptor assembly. Together, these studies offer an atomistic framework that not only explains TAS1R3’s pivotal role in chemosensory perception but also its emerging functions in systemic physiology."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "27", "end_ref": "41"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Greg Nelson, Jayaram Chandrashekar, Mark A Hoon, et al. 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"}, {"type": "b", "children": [{"type": "t", "text": "The cysteine-rich region of T1R3 determines responses to intensely sweet proteins."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biol Chem (2004)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/jbc.M406779200"}], "href": "https://doi.org/10.1074/jbc.M406779200"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "15299024"}], "href": "https://pubmed.ncbi.nlm.nih.gov/15299024"}]}, {"type": "r", "ref": 3, "children": [{"type": "t", "text": "Hong Xu, Lena Staszewski, Huixian Tang, et al. 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