Review: intracellular amino-acid transporters mark the site of mTORC1 activation.
| Evidence tier | D Mechanistic / in vitro / review |
| Study type | Narrative Review |
| Model system | Review |
| Journal | Cell metabolism |
| Year | 2016 |
| Peer reviewed | Yes |
| Source | DOI 10.1016/j.cmet.2016.03.013 · PMID 27076075 · Free full text (PMC5067300) |
Cell metabolism and growth are matched to nutrient availability via the amino-acid-regulated mechanistic target of rapamycin complex 1 (mTORC1). Transporters have emerged as important amino acid sensors controlling mTOR recruitment and activation at the surface of multiple intracellular compartments. Classically, this has involved late endosomes and lysosomes, but now, in a recent twist, also the Golgi apparatus. Here we propose a model in which specific amino acids in assorted compartments activate different mTORC1 complexes, which may have distinct drug sensitivities and functions. We will discuss the implications of this for mTORC1 function in health and disease.
| Intervention | Not applicable (review) |
| Target | mTORC1 / amino-acid transporters |
| Model | Review |
| Effect | Reviews how intracellular amino-acid transporters mark the sites (lysosome, Golgi) of mTORC1 activation |