Critically evaluating sweet taste receptor expression and signaling through a molecular pharmacology lens

The class C G protein-coupled sweet taste receptor (STR) is responsible for the perception of sweet-tasting molecules. Considered an obligate heterodimer, it consists 1 2 and 3 subunits. Interest in STR has steadily grown, especially since its discovery extraoral tissues hints at a metabolic role receptor. It now known that many pharmacologically exploitable binding sites exist across extracellular transmembrane regions both subunits STR, indicative potential amenability to pharmacotherapeutic modulation. In this review, we briefly describe structural characteristics functional relevance STR. Then, from molecular pharmacology perspective, dissect research surrounding regulation surface expression signal transduction, oral tissues, discuss exploitation biased agonists We find despite 20 years into target remains frustratingly enigmatic. Not only are mechanisms controlling regulating unclear, but also full repertoire signaling partners present inconclusive. Critically, influence polymorphisms (including those associated with sugar consumption) on hitherto unexplored. Finally, provide recommendations reporting reference sequence identification numbers avoid incorrect attribution wild-type these biologically significant polymorphisms, which argue may have led some inconsistencies field.