Human Genetic Polymorphisms in T1R1 and T1R3 Taste Receptor Subunits Affect Their Function
Umami is the typical taste induced by monosodium glutamate (MSG), which is thought to be detected by the heterodimeric G protein-coupled receptor, T1R1 and T1R3. Previously, we showed that MSG detection thresholds differ substantially between individuals and we further showed that nontaster and hypo...
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| Veröffentlicht in: | Chemical senses 2011-07, Vol.36 (6), p.527-537 |
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| creator | Raliou, Mariam Grauso, Marta Hoffmann, Brice Schlegel-Le-Poupon, Claire Nespoulous, Claude Débat, Hélène Belloir, Christine Wiencis, Anna Sigoillot, Maud Preet Bano, Singh Trotier, Didier Pernollet, Jean-Claude Montmayeur, Jean-Pierre Faurion, Annick Briand, Loïc |
| description | Umami is the typical taste induced by monosodium glutamate (MSG), which is thought to be detected by the heterodimeric G protein-coupled receptor, T1R1 and T1R3. Previously, we showed that MSG detection thresholds differ substantially between individuals and we further showed that nontaster and hypotaster subjects are associated with nonsynonymous single polymorphisms occurring in the T1R1 and T1R3 genes. Here, we show using functional expression that both amino acid substitutions (A110V and R507Q) in the N-terminal ligand-binding domain of T1R1 and the 2 other ones (F749S and R757C), located in the transmembrane domain of T1R3, severely impair in vitro T1R1/T1R3 response to MSG. A molecular model of the ligand-binding region of T1R1/T1R3 provides a mechanistic explanation supporting functional expression data. The data presented here support causal relations between the genotype and previous in vivo psychophysical studies in human evaluating sensitivity to MSG. |
| doi_str_mv | 10.1093/chemse/bjr014 |
| format | Article |
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Previously, we showed that MSG detection thresholds differ substantially between individuals and we further showed that nontaster and hypotaster subjects are associated with nonsynonymous single polymorphisms occurring in the T1R1 and T1R3 genes. Here, we show using functional expression that both amino acid substitutions (A110V and R507Q) in the N-terminal ligand-binding domain of T1R1 and the 2 other ones (F749S and R757C), located in the transmembrane domain of T1R3, severely impair in vitro T1R1/T1R3 response to MSG. A molecular model of the ligand-binding region of T1R1/T1R3 provides a mechanistic explanation supporting functional expression data. The data presented here support causal relations between the genotype and previous in vivo psychophysical studies in human evaluating sensitivity to MSG.</description><identifier>ISSN: 0379-864X</identifier><identifier>EISSN: 1464-3553</identifier><identifier>DOI: 10.1093/chemse/bjr014</identifier><identifier>PMID: 21422378</identifier><language>eng</language><publisher>England: Oxford University Press</publisher><subject>Amino Acid Substitution ; Blotting, Western ; Cells, Cultured ; Data processing ; G protein-coupled receptors ; Gene polymorphism ; Genetics ; Human genetics ; Humans ; Immunohistochemistry ; Life Sciences ; Models, Molecular ; Molecular modelling ; Monosodium glutamate ; Neurobiology ; Neurons and Cognition ; Polymorphism, Genetic ; Psychophysics ; Receptors, G-Protein-Coupled ; Receptors, G-Protein-Coupled - genetics ; Receptors, G-Protein-Coupled - physiology ; Sodium Glutamate ; Sodium Glutamate - metabolism ; Taste receptors ; Taste Threshold ; Taste Threshold - genetics ; Transmembrane domains ; Umami</subject><ispartof>Chemical senses, 2011-07, Vol.36 (6), p.527-537</ispartof><rights>The Author 2011. Published by Oxford University Press. All rights reserved. For permissions, please e-mail: journals.permissions@oup.com 2011</rights><rights>The Author 2011. Published by Oxford University Press. All rights reserved.</rights><rights>Distributed under a Creative Commons Attribution 4.0 International License</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c430t-3b67a931ea46ffa90574b8ec9671f06ad1e30338d1c5cef07d9622cd2d0e1c2f3</citedby><cites>FETCH-LOGICAL-c430t-3b67a931ea46ffa90574b8ec9671f06ad1e30338d1c5cef07d9622cd2d0e1c2f3</cites><orcidid>0000-0002-8175-5936 ; 0000-0002-3828-1421 ; 0000-0003-0413-9950 ; 0000-0002-2991-141X</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>230,314,780,784,885,1584,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/21422378$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://hal.science/hal-00641823$$DView record in HAL$$Hfree_for_read</backlink></links><search><creatorcontrib>Raliou, Mariam</creatorcontrib><creatorcontrib>Grauso, Marta</creatorcontrib><creatorcontrib>Hoffmann, Brice</creatorcontrib><creatorcontrib>Schlegel-Le-Poupon, Claire</creatorcontrib><creatorcontrib>Nespoulous, Claude</creatorcontrib><creatorcontrib>Débat, Hélène</creatorcontrib><creatorcontrib>Belloir, Christine</creatorcontrib><creatorcontrib>Wiencis, Anna</creatorcontrib><creatorcontrib>Sigoillot, Maud</creatorcontrib><creatorcontrib>Preet Bano, Singh</creatorcontrib><creatorcontrib>Trotier, Didier</creatorcontrib><creatorcontrib>Pernollet, Jean-Claude</creatorcontrib><creatorcontrib>Montmayeur, Jean-Pierre</creatorcontrib><creatorcontrib>Faurion, Annick</creatorcontrib><creatorcontrib>Briand, Loïc</creatorcontrib><title>Human Genetic Polymorphisms in T1R1 and T1R3 Taste Receptor Subunits Affect Their Function</title><title>Chemical senses</title><addtitle>Chem Senses</addtitle><description>Umami is the typical taste induced by monosodium glutamate (MSG), which is thought to be detected by the heterodimeric G protein-coupled receptor, T1R1 and T1R3. Previously, we showed that MSG detection thresholds differ substantially between individuals and we further showed that nontaster and hypotaster subjects are associated with nonsynonymous single polymorphisms occurring in the T1R1 and T1R3 genes. Here, we show using functional expression that both amino acid substitutions (A110V and R507Q) in the N-terminal ligand-binding domain of T1R1 and the 2 other ones (F749S and R757C), located in the transmembrane domain of T1R3, severely impair in vitro T1R1/T1R3 response to MSG. A molecular model of the ligand-binding region of T1R1/T1R3 provides a mechanistic explanation supporting functional expression data. The data presented here support causal relations between the genotype and previous in vivo psychophysical studies in human evaluating sensitivity to MSG.</description><subject>Amino Acid Substitution</subject><subject>Blotting, Western</subject><subject>Cells, Cultured</subject><subject>Data processing</subject><subject>G protein-coupled receptors</subject><subject>Gene polymorphism</subject><subject>Genetics</subject><subject>Human genetics</subject><subject>Humans</subject><subject>Immunohistochemistry</subject><subject>Life Sciences</subject><subject>Models, Molecular</subject><subject>Molecular modelling</subject><subject>Monosodium glutamate</subject><subject>Neurobiology</subject><subject>Neurons and Cognition</subject><subject>Polymorphism, Genetic</subject><subject>Psychophysics</subject><subject>Receptors, G-Protein-Coupled</subject><subject>Receptors, G-Protein-Coupled - genetics</subject><subject>Receptors, G-Protein-Coupled - physiology</subject><subject>Sodium Glutamate</subject><subject>Sodium Glutamate - metabolism</subject><subject>Taste receptors</subject><subject>Taste Threshold</subject><subject>Taste Threshold - genetics</subject><subject>Transmembrane domains</subject><subject>Umami</subject><issn>0379-864X</issn><issn>1464-3553</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2011</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqF0c1LwzAYBvAgipsfR6-Sm3qoy1e_jmOoEwbKnCBeQpq-YZG2qUkr-N_bUd3VU17Cj4eX90HogpJbSnI-01uoA8yKD0-oOEBTKhIR8Tjmh2hKeJpHWSLeJugkhA8yCM6yYzRhVDDG02yK3pd9rRr8AA10VuNnV33XzrdbG-qAbYM3dE2xasrdwPFGhQ7wGjS0nfP4pS_6xnYBz40B3eHNFqzH932jO-uaM3RkVBXg_Pc9Ra_3d5vFMlo9PTwu5qtIC066iBdJqnJOQYnEGJWTOBVFBjpPUmpIokoKnHCelVTHGgxJyzxhTJesJEA1M_wU3Yy5W1XJ1tta-W_plJXL-Uru_ghJBM0Y_6KDvRpt691nD6GTtQ0aqko14PogczKcJWax-FdmKeVZnDIyyGiU2rsQPJj9EpTIXUdy7EiOHQ3-8je5L2oo9_qvlAFcj8D17T9ZP9gJmqs</recordid><startdate>20110701</startdate><enddate>20110701</enddate><creator>Raliou, Mariam</creator><creator>Grauso, Marta</creator><creator>Hoffmann, Brice</creator><creator>Schlegel-Le-Poupon, Claire</creator><creator>Nespoulous, Claude</creator><creator>Débat, Hélène</creator><creator>Belloir, Christine</creator><creator>Wiencis, Anna</creator><creator>Sigoillot, Maud</creator><creator>Preet Bano, Singh</creator><creator>Trotier, Didier</creator><creator>Pernollet, Jean-Claude</creator><creator>Montmayeur, Jean-Pierre</creator><creator>Faurion, Annick</creator><creator>Briand, Loïc</creator><general>Oxford University Press</general><general>Oxford University Press (OUP)</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope><scope>7QR</scope><scope>7TK</scope><scope>8FD</scope><scope>FR3</scope><scope>P64</scope><scope>1XC</scope><scope>VOOES</scope><orcidid>https://orcid.org/0000-0002-8175-5936</orcidid><orcidid>https://orcid.org/0000-0002-3828-1421</orcidid><orcidid>https://orcid.org/0000-0003-0413-9950</orcidid><orcidid>https://orcid.org/0000-0002-2991-141X</orcidid></search><sort><creationdate>20110701</creationdate><title>Human Genetic Polymorphisms in T1R1 and T1R3 Taste Receptor Subunits Affect Their Function</title><author>Raliou, Mariam ; 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Previously, we showed that MSG detection thresholds differ substantially between individuals and we further showed that nontaster and hypotaster subjects are associated with nonsynonymous single polymorphisms occurring in the T1R1 and T1R3 genes. Here, we show using functional expression that both amino acid substitutions (A110V and R507Q) in the N-terminal ligand-binding domain of T1R1 and the 2 other ones (F749S and R757C), located in the transmembrane domain of T1R3, severely impair in vitro T1R1/T1R3 response to MSG. A molecular model of the ligand-binding region of T1R1/T1R3 provides a mechanistic explanation supporting functional expression data. 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| ispartof | Chemical senses, 2011-07, Vol.36 (6), p.527-537 |
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| subjects | Amino Acid Substitution Blotting, Western Cells, Cultured Data processing G protein-coupled receptors Gene polymorphism Genetics Human genetics Humans Immunohistochemistry Life Sciences Models, Molecular Molecular modelling Monosodium glutamate Neurobiology Neurons and Cognition Polymorphism, Genetic Psychophysics Receptors, G-Protein-Coupled Receptors, G-Protein-Coupled - genetics Receptors, G-Protein-Coupled - physiology Sodium Glutamate Sodium Glutamate - metabolism Taste receptors Taste Threshold Taste Threshold - genetics Transmembrane domains Umami |
| title | Human Genetic Polymorphisms in T1R1 and T1R3 Taste Receptor Subunits Affect Their Function |
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