Amino Acid-Dependent mTORC1 Regulation by the Lysosomal Membrane Protein SLC38A9
What this study shows
SLC38A9, a lysosomal membrane protein, mediates amino-acid-dependent mTORC1 activation.
At a glance
| Evidence type | M Molecular — cells, biochemistry, structure Marked M because it is molecular or in-vitro work (model: Mammalian 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 | Mammalian cells |
| Journal | Molecular and cellular biology |
| Year | 2015 |
| Peer reviewed | Yes |
| Record last updated | 2026-10-01 |
| Source | DOI 10.1128/MCB.00125-15 · PMID 25963655 · Free full text (PMC4475919) |
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 | Biochemical/genetic (SLC38A9) |
| Target | SLC38A9 / Rag-Ragulator / mTORC1 |
| Model | Mammalian cells |
| Effect | SLC38A9 is a lysosomal component of the Rag-Ragulator that mediates amino-acid-dependent mTORC1 activation |
In the Atlas
Related topics
Links in the pathway map
- Supports SLC38A9 activates Rag GTPases
More studies on this topic
- Lysosomal cholesterol activates mTORC1 via an SLC38A9-Niemann-Pick C1 signaling complex (2017)
- 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)
- Ragulator and SLC38A9 activate the Rag GTPases through noncanonical GEF mechanisms (2018)
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