Isolation of a protein target of the FKBP12-rapamycin complex in mammalian cells
What this study shows
Isolated mTOR as the FKBP12-rapamycin-associated protein controlling G1-S progression.
At a glance
| Evidence type | M Molecular — cells, biochemistry, structure Marked M because it is molecular or in-vitro work (model: Rat/mouse cells; in vitro) 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/mouse cells; in vitro |
| Journal | The Journal of biological chemistry |
| Year | 1995 |
| Peer reviewed | Yes |
| Record last updated | 2026-10-01 |
| Source | DOI 10.1074/jbc.270.2.815 · PMID 7822316 |
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) |
| Target | mTOR (FRAP/RAFT1) / FKBP12 |
| Model | Rat/mouse cells; in vitro |
| Effect | Isolation of the mammalian FKBP12-rapamycin target protein (mTOR) |
In the Atlas
Links in the pathway map
- Supports FKBP12 binds mTORC1
- Supports Rapamycin binds FKBP12
- Supports Rapamycin inhibits mTORC1
Learn the biology
Want to understand the biology behind this study? → Challenge 02: Why rapamycin does not switch mTORC1 off
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