Mechanism of arginine sensing by CASTOR1 upstream of mTORC1
What this study shows
CASTOR1 is a direct arginine sensor upstream of mTORC1; structure reveals the arginine-binding mechanism.
At a glance
| Evidence type | M Molecular — cells, biochemistry, structure Marked M because it is molecular or in-vitro work (model: Structure; 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 | Structure; cells |
| Journal | Nature |
| Year | 2016 |
| Peer reviewed | Yes |
| Record last updated | 2026-10-01 |
| Source | DOI 10.1038/nature19079 · PMID 27487210 · Free full text (PMC4988899) |
Extracted findings
These fields were extracted from the paper with AI assistance and have not been checked against the source. Read them as a pointer into the paper, not as curated claims; where they disagree with the curated summary above, the curated summary stands.
| Intervention | Structural/biochemical (CASTOR1) |
| Target | CASTOR1 / GATOR2 / mTORC1 (arginine) |
| Model | Structure; cells |
| Effect | CASTOR1 is a direct arginine sensor upstream of mTORC1; structure reveals the arginine-binding mechanism |
In the Atlas
Related topics
Links in the pathway map
- Supports Arginine inhibits CASTOR1
- Supports CASTOR1 inhibits GATOR2
More studies on this topic
- The CASTOR Proteins Are Arginine Sensors for the mTORC1 Pathway (2016)
- L-Arginine Modulates T Cell Metabolism and Enhances Survival and Anti-tumor Activity (2016)
- 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)
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