scholarly journals Sweet Taste Receptor Activation in the Gut Is of Limited Importance for Glucose-Stimulated GLP-1 and GIP Secretion

Nutrients ◽  
2017 ◽  
Vol 9 (4) ◽  
pp. 418 ◽  
Author(s):  
Monika Saltiel ◽  
Rune Kuhre ◽  
Charlotte Christiansen ◽  
Rasmus Eliasen ◽  
Kilian Conde-Frieboes ◽  
...  
Keyword(s):  
Taste Receptor ◽  
Receptor Activation ◽  
Sweet Taste ◽  
Sweet Taste Receptor

scholarly journals Conserved Residues Control the T1R3-Specific Allosteric Signaling Pathway of the Mammalian Sweet-Taste Receptor

2019 ◽  
Vol 44 (5) ◽  
pp. 303-310 ◽  
Author(s):  
Jean-Baptiste Chéron ◽  
Amanda Soohoo ◽  
Yi Wang ◽  
Jérôme Golebiowski ◽  
Serge Antonczak ◽  
...  
Keyword(s):  
Transmembrane Domain ◽  
Taste Receptor ◽  
Receptor Activation ◽  
Sweet Taste ◽  
Site Directed Mutagenesis ◽  
Activation Mechanism ◽  
Structural Basis ◽  
Directed Mutagenesis ◽  
Conserved Residues ◽  
Sweet Taste Receptor

Abstract Mammalian sensory systems detect sweet taste through the activation of a single heteromeric T1R2/T1R3 receptor belonging to class C G-protein-coupled receptors. Allosteric ligands are known to interact within the transmembrane domain, yet a complete view of receptor activation remains elusive. By combining site-directed mutagenesis with computational modeling, we investigate the structure and dynamics of the allosteric binding pocket of the T1R3 sweet-taste receptor in its apo form, and in the presence of an allosteric ligand, cyclamate. A novel positively charged residue at the extracellular loop 2 is shown to interact with the ligand. Molecular dynamics simulations capture significant differences in the behavior of a network of conserved residues with and without cyclamate, although they do not directly interact with the allosteric ligand. Structural models show that they adopt alternate conformations, associated with a conformational change in the transmembrane region. Site-directed mutagenesis confirms that these residues are unequivocally involved in the receptor function and the allosteric signaling mechanism of the sweet-taste receptor. Similar to a large portion of the transmembrane domain, they are highly conserved among mammals, suggesting an activation mechanism that is evolutionarily conserved. This work provides a structural basis for describing the dynamics of the receptor, and for the rational design of new sweet-taste modulators.

A novel functional screening assay to monitor sweet taste receptor activation in vitro

2017 ◽  
Vol 33 (2) ◽  
pp. 173-183 ◽  
Author(s):  
Shanna Bastiaan-Net ◽  
Dianne B.P.M. van den Berg-Somhorst ◽  
Renata M.C. Ariëns ◽  
Marcel Paques ◽  
Jurriaan J. Mes
Keyword(s):  
Taste Receptor ◽  
Receptor Activation ◽  
Sweet Taste ◽  
Functional Screening ◽  
Screening Assay ◽  
Sweet Taste Receptor

Interaction of suosan with the sweet taste receptor

1982 ◽  
Vol 175 (4) ◽  
pp. 266-268 ◽  
Author(s):  
Jean-Marie Tinti ◽  
Claude Nofre ◽  
Anne-Marie Peytavi
Keyword(s):  
Taste Receptor ◽  
Sweet Taste ◽  
Sweet Taste Receptor
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