SLC38A9 is a component of the lysosomal amino acid sensing machinery that controls mTORC1
What this study shows
SLC38A9 is a component of the lysosomal amino-acid sensing machinery controlling mTORC1.
At a glance
| Evidence type | M Molecular — cells, biochemistry, structure Marked M because it is molecular or in-vitro work (model: Mammalian cells) rather than a whole-organism health-outcome study. That is often exactly where causal biology gets established -- the code says which system the finding was shown in, and nothing about how good the work is. |
| Study type | 5 - Mechanistic / In Vitro |
| Model system | Mammalian cells |
| Journal | Nature |
| Year | 2015 |
| Peer reviewed | Yes |
| Record last updated | 2026-08-22 |
| Source | DOI 10.1038/nature14107 · PMID 25561175 · Free full text (PMC4376665) |
Extracted findings
| Intervention | Biochemical/genetic (SLC38A9) |
| Target | SLC38A9 / Rag-Ragulator / mTORC1 |
| Model | Mammalian cells |
| Effect | SLC38A9 is a lysosomal amino-acid (arginine) transporter/sensor component that controls mTORC1 |
In the Atlas
Related topics
More studies on this topic
- Crystal structure of arginine-bound lysosomal transporter SLC38A9 in the cytosol-open state (2018)
- Metabolism. Lysosomal amino acid transporter SLC38A9 signals arginine sufficiency to mTORC1 (2015)
- The CASTOR Proteins Are Arginine Sensors for the mTORC1 Pathway (2016)
- Amino Acid-Dependent mTORC1 Regulation by the Lysosomal Membrane Protein SLC38A9 (2015)
Learn the biology
Want to understand the biology behind this study? → Nutrient Sensing