Distinct contributions of T1R2 and T1R3 taste receptor subunits to the detection of sweet stimuli

Yiling Nie, Stephan Vigues, Jeanette R. Hobbs, Graeme L. Conn, Steven D. Munger

    Research output: Contribution to journalArticlepeer-review

    Abstract

    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 [2-4], 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, 5-10] 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. ©2005 Elsevier Ltd All rights reserved.
    Original languageEnglish
    Pages (from-to)1948-1952
    Number of pages4
    JournalCurrent Biology
    Volume15
    Issue number21
    DOIs
    Publication statusPublished - 8 Nov 2005

    Fingerprint

    Dive into the research topics of 'Distinct contributions of T1R2 and T1R3 taste receptor subunits to the detection of sweet stimuli'. Together they form a unique fingerprint.

    Cite this