Document Detail


Amino acid regulation of autophagy through the GPCR TAS1R1-TAS1R3.
MedLine Citation:
PMID:  23222068     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Cells require the ability to rapidly detect decreases in concentrations of free amino acids so that homeostatic mechanisms, including autophagy, can be engaged to replenish amino acids. Amino acids are transported into cells where it is generally accepted that they are detected by an intracellular sensor. We now show that the cell surface G protein coupled receptor (GPCR) TAS1R1-TAS1R3 (T1R1-T1R3) can sense extracellular amino acids, activate MTORC1, and inhibit autophagy. This receptor is expressed in most tissues and fasted TAS1R3 (-/-) mice have increased autophagy in the heart, skeletal muscle and liver.
Authors:
Eric M Wauson; Elma Zaganjor; Melanie H Cobb
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Publication Detail:
Type:  Journal Article     Date:  2012-12-07
Journal Detail:
Title:  Autophagy     Volume:  9     ISSN:  1554-8635     ISO Abbreviation:  Autophagy     Publication Date:  2013 Mar 
Date Detail:
Created Date:  2013-02-21     Completed Date:  2013-09-23     Revised Date:  2014-03-03    
Medline Journal Info:
Nlm Unique ID:  101265188     Medline TA:  Autophagy     Country:  United States    
Other Details:
Languages:  eng     Pagination:  418-9     Citation Subset:  IM    
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MeSH Terms
Descriptor/Qualifier:
Amino Acids / metabolism*
Animals
Autophagy / physiology*
Gene Expression Regulation*
Homeostasis
Mice
Mice, Transgenic
Multiprotein Complexes
Proteins / metabolism
Receptors, G-Protein-Coupled / metabolism*
Signal Transduction
TOR Serine-Threonine Kinases
Chemical
Reg. No./Substance:
0/Amino Acids; 0/Multiprotein Complexes; 0/Proteins; 0/Receptors, G-Protein-Coupled; 0/mechanistic target of rapamycin complex 1; 0/taste receptors, type 1; EC 2.7.1.1/TOR Serine-Threonine Kinases

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


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