The CASTOR Proteins Are Arginine Sensors for the mTORC1 Pathway
What this study shows
Identified CASTOR1 as the direct arginine sensor: when arginine binds CASTOR1, it lets go of GATOR2, switching mTORC1 on. Together with Sestrin2 (leucine) this built the picture of mTORC1 as a cell that literally tastes individual amino acids.
At a glance
| Evidence type | M Molecular — cells, biochemistry, structure Marked M because it is molecular or in-vitro work (model: Human cells (biochemistry)) 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 | Human cells (biochemistry) |
| Journal | Cell |
| Year | 2016 |
| Peer reviewed | Yes |
| Record last updated | 2026-08-22 |
| Source | DOI 10.1016/j.cell.2016.02.035 · PMID 26972053 · Free full text (PMC4808398) |
Extracted findings
| Intervention | Biochemical/genetic (CASTOR1/2) |
| Target | CASTOR / GATOR2 / mTORC1 (arginine) |
| Model | Human cells (biochemistry) |
| Effect | The CASTOR proteins are direct arginine sensors for the mTORC1 pathway |
In the Atlas
Related topics
More studies on this topic
- A Tumor suppressor complex with GAP activity for the Rag GTPases that signal amino acid sufficiency to mTORC1 (2013)
- CASTOR1 regulates humoral immune responses and contributes to the pathogenesis of systemic lupus erythematosus (2026)
- Crystal structure of arginine-bound lysosomal transporter SLC38A9 in the cytosol-open state (2018)
- SLC38A9 is a component of the lysosomal amino acid sensing machinery that controls mTORC1 (2015)
Learn the biology
Want to understand the biology behind this study? → Nutrient Sensing