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; founding paper of the entire mTOR field.
At a glance
| Evidence type | M Molecular — cells, biochemistry, structure Marked M because it is molecular or in-vitro work (model: Mammalian cell culture) 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 cell culture |
| Journal | Cell |
| Year | 1994 |
| Peer reviewed | Yes |
| Record last updated | 2026-08-22 |
| Source | DOI 10.1016/0092-8674(94)90570-3 · PMID 7518356 |
Extracted findings
| Intervention | Biochemical (FKBP12-rapamycin affinity purification) |
| Target | RAFT1 (mTOR/FRAP) / FKBP12 |
| Model | Mammalian cell culture |
| Effect | Identifies RAFT1 (mammalian TOR) as the FKBP12-rapamycin target, homologous to yeast TORs |
In the Atlas
Related topics
More studies on this topic
- Rapamycin-induced fatty liver in mice is attenuated by chloroquine co-treatment in an ERRα-dependent manner (2026)
- Transient rapamycin treatment can increase lifespan and healthspan in middle-aged mice (2016)
- Mechanisms of life span extension by rapamycin in the fruit fly Drosophila melanogaster (2010)
- Molecular interplay between mTOR, amyloid-beta, and Tau: effects on cognitive impairments (2010)
Learn the biology
Want to understand the biology behind this study? → What is mTOR?