Phosphorylation and regulation of Akt/PKB by the rictor-mTOR complex
What this study shows
The rictor-mTOR complex (mTORC2) directly phosphorylates Akt/PKB on Ser473, regulating cell survival.
At a glance
| Evidence type | M Molecular — cells, biochemistry, structure Marked M because it is molecular or in-vitro work (model: Human cells; Drosophila) 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 | Human cells; Drosophila |
| Journal | Science |
| Year | 2005 |
| Peer reviewed | Yes |
| Record last updated | 2026-08-22 |
| Source | DOI 10.1126/science.1106148 · PMID 15718470 |
Extracted findings
| Intervention | Genetic/biochemical (rictor-mTOR) |
| Target | mTORC2 (rictor) / Akt Ser473 |
| Model | Human cells; Drosophila |
| Effect | The rictor-mTOR complex (mTORC2) phosphorylates Akt/PKB at Ser473 |
In the Atlas
Related topics
More studies on this topic
- Active-site inhibitors of mTOR target rapamycin-resistant outputs of mTORC1 and mTORC2 (2009)
- Ablation in mice of the mTORC components raptor, rictor, or mLST8 reveals that mTORC2 is required for signaling to Akt-FOXO and PKCalpha, but not S6K1 (2006)
- DEPTOR is an mTOR inhibitor frequently overexpressed in multiple myeloma cells and required for their survival (2009)
- Rictor, a novel binding partner of mTOR, defines a rapamycin-insensitive and raptor-independent pathway that regulates the cytoskeleton (2004)
Learn the biology
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