Title: | Distinct contributions of T1R2 and T1R3 taste receptor subunits to the detection of sweet stimuli |
Author(s): | Nie Y; Vigues S; Hobbs JR; Conn GL; Munger SD; |
Address: | "Department of Anatomy and Neurobiology, University of Maryland School of Medicine, Baltimore, Maryland 21201, USA" |
DOI: | 10.1016/j.cub.2005.09.037 |
ISSN/ISBN: | 0960-9822 (Print) 0960-9822 (Linking) |
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. 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, 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 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. Thus, individual T1R subunits increase the receptive range of the sweet taste receptor, offering a functional mechanism for phenotypic variations in sweet taste" |
Keywords: | "Animals Chromatography, Affinity DNA Primers Electrophoresis, Polyacrylamide Gel Genetic Vectors/genetics Ligands Mice Mutagenesis, Site-Directed Polymorphism, Single Nucleotide/genetics Protein Structure, Tertiary/genetics Protein Subunits/genetics/*meta;" |
Notes: | "MedlineNie, Yiling Vigues, Stephan Hobbs, Jeanette R Conn, Graeme L Munger, Steven D eng Wellcome Trust/United Kingdom Comparative Study Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't England 2005/11/08 Curr Biol. 2005 Nov 8; 15(21):1948-52. doi: 10.1016/j.cub.2005.09.037" |