Current Biology
Volume 15, Issue 21, 8 November 2005, Pages 1948-1952
Journal home page for Current Biology

Report
Distinct Contributions of T1R2 and T1R3 Taste Receptor Subunits to the Detection of Sweet Stimuli

https://doi.org/10.1016/j.cub.2005.09.037Get rights and content
Under an Elsevier user license
open archive

Summary

Animals utilize hundreds of distinct G protein-coupled receptor (GPCR)-type chemosensory receptors to detect a diverse array of chemical signals in their environment, including odors, pheromones, and tastants [1]. However, the molecular mechanisms by which these receptors selectively interact with their cognate ligands remain poorly understood. There is growing evidence that many chemosensory receptors exist in multimeric complexes [2, 3, 4], though little is known about the relative contributions of individual subunits to receptor functions. Here, we report that each of the two subunits in the heteromeric T1R2:T1R3 sweet taste receptor [2, 5, 6, 7, 8, 9, 10] binds sweet stimuli though with distinct affinities and conformational changes. Furthermore, ligand affinities for T1R3 are drastically reduced by the introduction of a single amino acid change associated with decreased sweet taste sensitivity in behaving mice [11]. Thus, individual T1R subunits increase the receptive range of the sweet taste receptor, offering a functional mechanism for phenotypic variations in sweet taste.

Cited by (0)

3

These authors contributed equally to this work.

4

Present address: Department of Physiology, MRL 6220, University of California, Los Angeles, 675 Charles Young Drive South, Los Angeles, California 90095.