Sweet taste receptor (TAS1R2–TAS1R3 heterodimer) (T1R2–T1R3)

The sweet taste receptor is a heterodimer composed of the T1R2 and T1R3 subunits, both belonging to the class C GPCR family[6][2][4][3]. This complex is responsible for detecting a wide range of sweet-tasting compounds, including natural sugars and artificial sweeteners. The receptor is expressed primarily in gustatory tissues but is also found in other tissues. Structural studies reveal that T1R2 provides the main ligand-binding site, while T1R3 can modulate ligand specificity and acts as the common subunit for both sweet and umami taste heterodimers[1][3]. When sweet compounds bind to the receptor, it activates intracellular signaling pathways through G protein coupling, leading to taste perception[6][2][4][1]. The receptor exhibits broad chemical recognition, which allows it to detect diverse sweet substances with specificity[3][5]. Its function and ligand selectivity show species-specific differences, influencing how different animals respond to sweet compounds[4]. Artificial and natural sweeteners interact with distinct domains of the receptor, informing rational design of future sweeteners[1][5]. There are no major intrinsic safety concerns, although the physiological impact of widespread artificial sweetener use remains ongoing research[4].

Other names

Sweet taste receptorT1R2–T1R3TAS1R2–TAS1R3 heterodimerType 1 taste receptor (sweet subtype)

Ligand binding to receptor subunits triggers conformational change and downstream G protein-coupled signaling, perceived as sweetness. Allosteric modulation (certain ligands bind to distinct sites and modulate receptor function).