Crystal structure of arginine-bound lysosomal transporter SLC38A9 in the cytosol-open state
What this study shows
Crystal structure of arginine-bound SLC38A9 reveals the basis of lysosomal arginine sensing.
At a glance
| Evidence type | M Molecular — cells, biochemistry, structure Marked M because it is molecular or in-vitro work (model: Structure; in vitro) 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; in vitro |
| Journal | Nature structural & molecular biology |
| Year | 2018 |
| Peer reviewed | Yes |
| Record last updated | 2026-10-01 |
| Source | DOI 10.1038/s41594-018-0072-2 · PMID 29872228 · Free full text (PMC7346717) |
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 (crystal structure of SLC38A9) |
| Target | SLC38A9 / arginine / mTORC1 |
| Model | Structure; in vitro (Danio rerio) |
| Effect | First crystal structure of arginine-bound SLC38A9 (cytosol-open state), the lysosomal amino-acid transporter/sensor for mTORC1 |
In the Atlas
Related topics
More studies on this topic
- SLC38A9 is a component of the lysosomal amino acid sensing machinery that controls mTORC1 (2015)
- Ragulator and SLC38A9 activate the Rag GTPases through noncanonical GEF mechanisms (2018)
- Metabolism. Lysosomal amino acid transporter SLC38A9 signals arginine sufficiency to mTORC1 (2015)
- The CASTOR Proteins Are Arginine Sensors for the mTORC1 Pathway (2016)
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