Essential amino acid sensed by two separate routes: cytosolic arginine binds CASTOR1, and lysosomal arginine is read by the transporter-like protein SLC38A9.
| Tier | What it means | Studies |
|---|---|---|
| D | Mechanistic / in vitro / review | 5 |
No direct human evidence in the Atlas for this entity yet — everything below rests on animal or mechanistic work.
| Study | Year | Tier | Finding |
|---|---|---|---|
| LEI2018 | 2018 | D | Crystal structure of arginine-bound SLC38A9 reveals the basis of lysosomal arginine sensing. |
| CHA2016 | 2016 | D | 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 th |
| SAX2016 | 2016 | D | CASTOR1 is a direct arginine sensor upstream of mTORC1; structure reveals the arginine-binding mechanism. |
| REB2015 | 2015 | D | SLC38A9 is a component of the lysosomal amino-acid sensing machinery controlling mTORC1. |
| WAN2015 | 2015 | D | The lysosomal transporter SLC38A9 signals arginine sufficiency to mTORC1. |