Structural mechanism of a Rag GTPase activation checkpoint by the lysosomal folliculin complex
What this study shows
Structure reveals the FLCN complex as a Rag-GTPase activation checkpoint gating mTORC1.
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 | Science |
| Year | 2019 |
| Peer reviewed | Yes |
| Record last updated | 2026-10-01 |
| Source | DOI 10.1126/science.aax0364 · PMID 31672913 · Free full text (PMC6945816) |
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 (FLCN complex) |
| Target | FLCN–FNIP2 / RagC / mTORC1 |
| Model | Structure; cells |
| Effect | The lysosomal folliculin complex acts as a GAP for RagC, a checkpoint in nutrient-dependent mTORC1 activation |
In the Atlas
Links in the pathway map
- Supports FLCN / FNIP1/2 activates Rag GTPases
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