RAFT1: a mammalian protein that binds to FKBP12 in a rapamycin-dependent fashion and is homologous to yeast TORs
What this study shows
Discovery of the protein RAFT1 (today's mTOR) as the direct target of the FKBP12-rapamycin complex; one of three 1994 reports (with Brown et al. and Chiu et al.) that identified mammalian TOR, three years after TOR was found in yeast.
At a glance
| Evidence type | M Molecular — cells, biochemistry, structure Marked M because it is molecular or in-vitro work (model: Rat brain (protein purification)) 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 | Rat brain (protein purification) |
| Journal | Cell |
| Year | 1994 |
| Peer reviewed | Yes |
| Record last updated | 2026-10-01 |
| Source | DOI 10.1016/0092-8674(94)90570-3 · PMID 7518356 |
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 (FKBP12-rapamycin affinity purification) |
| Target | RAFT1 (mTOR/FRAP) / FKBP12 |
| Model | Rat brain tissue (biochemical purification) |
| Effect | Identifies RAFT1 (mammalian TOR) as the FKBP12-rapamycin target, homologous to yeast TORs |
In the Atlas
Related topics
Links in the pathway map
- Supports FKBP12 binds mTORC1
- Supports Rapamycin inhibits mTORC1
Learn the biology
Want to understand the biology behind this study? → What is mTOR?
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