Hybrid Structure of the RagA/C-Ragulator mTORC1 Activation Complex
What this study shows
Hybrid structural model of the RagA/C-Ragulator mTORC1 activation complex.
At a glance
| Evidence type | M Molecular — cells, biochemistry, structure Marked M because it is molecular or in-vitro work (model: Hybrid structure) 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 | Hybrid structure |
| Journal | Molecular cell |
| Year | 2017 |
| Peer reviewed | Yes |
| Record last updated | 2026-10-01 |
| Source | DOI 10.1016/j.molcel.2017.10.016 · PMID 29107538 · Free full text (PMC5722659) |
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/hybrid) |
| Target | Rag GTPases / Ragulator (Lamtor1-5) / mTORC1 |
| Model | Hybrid structure |
| Effect | Structure of the RagA/C-Ragulator activation complex; Lamtor1 wraps the subunits to form the Rag-binding platform |
In the Atlas
Related topics
More studies on this topic
- Structure of the lysosomal mTORC1-TFEB-Rag-Ragulator megacomplex (2023)
- Structural basis for mTORC1 activation on the lysosomal membrane (2025)
- A Rag GTPase dimer code defines the regulation of mTORC1 by amino acids (2022)
- Structural basis for the docking of mTORC1 on the lysosomal surface (2019)
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