Abstract
Detection of tastes is critical for animals. Sweet, umami and bitter taste are mediated by G-protein-coupled receptors that are expressed in the taste receptor cells. TAS1Rs which belong to class C G-protein-coupled receptors form heterodimeric complexes to function as sweet (TAS1R2 + TAS1R3) or umami (TAS1R1 + TAS1R3) taste receptors. Umami taste is also considered to be mediated by mGluRs. TAS2Rs belong to class A G-protein-coupled receptors and are responsible for bitter taste. After activation of these receptors, their second messenger pathways lead to depolarization and intracellular calcium increase in taste receptor cells. Then, transmitter is released from taste receptor cells leading to activation of taste nerve fibers and taste information is sent to the central nervous system. Recent studies on heterologous expression system and molecular modeling lead to better understanding of binding site of TAS1Rs and TAS2Rs and molecular mechanisms for interaction between taste substances and these receptors. TAS1Rs and TAS2Rs have multiple and single binding sites for structurally diverse ligands, respectively. Sensitivities of these receptors are known to differ among individuals, strains, and species. In addition, some species abolish these receptors and signaling molecules. Here we focus on structure, function, signaling, polymorphism, and molecular evolution of the taste G-protein-coupled receptors.
Keywords: Bitter taste, G-protein-coupled receptors, molecular evolution, molecular modeling, signal transduction, sweet taste, TAS1Rs, TAS2Rs, umami taste.
Current Pharmaceutical Biotechnology
Title:Structure, Function, and Signaling of Taste G-Protein-Coupled Receptors
Volume: 15 Issue: 10
Author(s): Keisuke Sanematsu, Ryusuke Yoshida, Noriatsu Shigemura and Yuzo Ninomiya
Affiliation:
Keywords: Bitter taste, G-protein-coupled receptors, molecular evolution, molecular modeling, signal transduction, sweet taste, TAS1Rs, TAS2Rs, umami taste.
Abstract: Detection of tastes is critical for animals. Sweet, umami and bitter taste are mediated by G-protein-coupled receptors that are expressed in the taste receptor cells. TAS1Rs which belong to class C G-protein-coupled receptors form heterodimeric complexes to function as sweet (TAS1R2 + TAS1R3) or umami (TAS1R1 + TAS1R3) taste receptors. Umami taste is also considered to be mediated by mGluRs. TAS2Rs belong to class A G-protein-coupled receptors and are responsible for bitter taste. After activation of these receptors, their second messenger pathways lead to depolarization and intracellular calcium increase in taste receptor cells. Then, transmitter is released from taste receptor cells leading to activation of taste nerve fibers and taste information is sent to the central nervous system. Recent studies on heterologous expression system and molecular modeling lead to better understanding of binding site of TAS1Rs and TAS2Rs and molecular mechanisms for interaction between taste substances and these receptors. TAS1Rs and TAS2Rs have multiple and single binding sites for structurally diverse ligands, respectively. Sensitivities of these receptors are known to differ among individuals, strains, and species. In addition, some species abolish these receptors and signaling molecules. Here we focus on structure, function, signaling, polymorphism, and molecular evolution of the taste G-protein-coupled receptors.
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Cite this article as:
Sanematsu Keisuke, Yoshida Ryusuke, Shigemura Noriatsu and Ninomiya Yuzo, Structure, Function, and Signaling of Taste G-Protein-Coupled Receptors, Current Pharmaceutical Biotechnology 2014; 15 (10) . https://dx.doi.org/10.2174/1389201015666140922105911
DOI https://dx.doi.org/10.2174/1389201015666140922105911 |
Print ISSN 1389-2010 |
Publisher Name Bentham Science Publisher |
Online ISSN 1873-4316 |
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