Document Detail


An amino-acid taste receptor.
MedLine Citation:
PMID:  11894099     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The sense of taste provides animals with valuable information about the nature and quality of food. Mammals can recognize and respond to a diverse repertoire of chemical entities, including sugars, salts, acids and a wide range of toxic substances. Several amino acids taste sweet or delicious (umami) to humans, and are attractive to rodents and other animals. This is noteworthy because L-amino acids function as the building blocks of proteins, as biosynthetic precursors of many biologically relevant small molecules, and as metabolic fuel. Thus, having a taste pathway dedicated to their detection probably had significant evolutionary implications. Here we identify and characterize a mammalian amino-acid taste receptor. This receptor, T1R1+3, is a heteromer of the taste-specific T1R1 and T1R3 G-protein-coupled receptors. We demonstrate that T1R1 and T1R3 combine to function as a broadly tuned L-amino-acid sensor responding to most of the 20 standard amino acids, but not to their D-enantiomers or other compounds. We also show that sequence differences in T1R receptors within and between species (human and mouse) can significantly influence the selectivity and specificity of taste responses.
Authors:
Greg Nelson; Jayaram Chandrashekar; Mark A Hoon; Luxin Feng; Grace Zhao; Nicholas J P Ryba; Charles S Zuker
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Publication Detail:
Type:  Journal Article; Research Support, U.S. Gov't, P.H.S.     Date:  2002-02-24
Journal Detail:
Title:  Nature     Volume:  416     ISSN:  0028-0836     ISO Abbreviation:  Nature     Publication Date:  2002 Mar 
Date Detail:
Created Date:  2002-03-14     Completed Date:  2002-04-10     Revised Date:  2009-11-19    
Medline Journal Info:
Nlm Unique ID:  0410462     Medline TA:  Nature     Country:  England    
Other Details:
Languages:  eng     Pagination:  199-202     Citation Subset:  IM    
Affiliation:
Howard Hughes Medical Institute and Departments of Biology and Neurosciences, University of California at San Diego, La Jolla, California, 92093-0649, USA.
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MeSH Terms
Descriptor/Qualifier:
Alleles
Amino Acids / chemistry,  metabolism*,  pharmacology
Animals
Calcium Signaling / drug effects
Cell Line
Chorda Tympani Nerve / drug effects,  physiology
Dose-Response Relationship, Drug
Heterotrimeric GTP-Binding Proteins / metabolism
Humans
Inosine Monophosphate / metabolism,  pharmacology
Mice
Mutation / genetics
Polymorphism, Genetic / genetics
Protein Subunits
Receptors, Cell Surface / chemistry,  genetics,  metabolism*
Receptors, G-Protein-Coupled*
Stereoisomerism
Structure-Activity Relationship
Substrate Specificity
Taste / genetics,  physiology
Taste Buds / chemistry
Transfection
Chemical
Reg. No./Substance:
0/Amino Acids; 0/Protein Subunits; 0/Receptors, Cell Surface; 0/Receptors, G-Protein-Coupled; 0/taste receptors, type 1; 131-99-7/Inosine Monophosphate; EC 3.6.5.1/Heterotrimeric GTP-Binding Proteins
Comments/Corrections
Comment In:
Nature. 2002 Mar 14;416(6877):136   [PMID:  11894081 ]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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