Insulin signalling to mTOR mediated by the Akt/PKB substrate PRAS40
What this study shows
Insulin signals to mTORC1 through Akt phosphorylation of the inhibitor PRAS40.
At a glance
| Evidence type | M Molecular — cells, biochemistry, structure Marked M because it is molecular or in-vitro work (model: Mammalian 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 | Mammalian cells |
| Journal | Nature cell biology |
| Year | 2007 |
| Peer reviewed | Yes |
| Record last updated | 2026-10-01 |
| Source | DOI 10.1038/ncb1547 · PMID 17277771 |
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/genetic (PRAS40/Akt) |
| Target | mTORC1 / PRAS40 / Akt |
| Model | Mammalian cells |
| Effect | Insulin signals to mTOR via Akt phosphorylation of PRAS40, relieving its inhibition of mTORC1 |
In the Atlas
Related topics
Links in the pathway map
- Supports Akt/PKB inhibits PRAS40
More studies on this topic
- The proline-rich Akt substrate of 40 kDa (PRAS40) is a physiological substrate of mammalian target of rapamycin complex 1 (2007)
- PRAS40 is an insulin-regulated inhibitor of the mTORC1 protein kinase (2007)
- Mechanisms of mTORC1 activation by RHEB and inhibition by PRAS40 (2017)
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