Lysosomal amino-acid transporter and signaling component; acts as an arginine sensor on the lysosomal membrane. Works together with v-ATPase and Ragulator to relay luminal arginine availability to the Rag GTPases and thereby recruit mTORC1. Loss of SLC38A9 impairs arginine-dependent mTORC1 activation.
| 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. |
| WYA2017 | 2017 | D | SLC38A9 effluxes essential amino acids (e.g. leucine) from lysosomes to activate mTORC1. |
| JUN2015 | 2015 | D | SLC38A9, a lysosomal membrane protein, mediates amino-acid-dependent mTORC1 activation. |
| 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. |