title: Amino acid regulation of autophagy through the GPCR TAS1R1-TAS1R3.
abstract: 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.affiliation: Department of Pharmacology, University of Texas Southwestern Medical Center at Dallas, Dallas, TX, USA.
authors.forename: Eric M
authors.initials: EM
authors.lastname: Wauson
authors.forename: Elma
authors.initials: E
authors.lastname: Zaganjor
authors.forename: Melanie H
authors.initials: MH
authors.lastname: Cobb
mesh_terms: D000596:Amino Acids / Q000378:metabolism*; D000818:Animals; D001343:Autophagy / Q000502:physiology*; D005786:Gene Expression Regulation; D006706:Homeostasis; D000076222:Mechanistic Target of Rapamycin Complex 1; D051379:Mice; D008822:Mice, Transgenic; D046912:Multiprotein Complexes; D011506:Proteins / Q000378:metabolism; D043562:Receptors, G-Protein-Coupled / Q000378:metabolism*; D015398:Signal Transduction; D058570:TOR Serine-Threonine Kinases
chemical_list: D000596:Amino Acids; D046912:Multiprotein Complexes; D011506:Proteins; D043562:Receptors, G-Protein-Coupled; C431926:taste receptors, type 1; D000076222:Mechanistic Target of Rapamycin Complex 1; D058570:TOR Serine-Threonine Kinases