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 | 2026-10-01 |
| Source | DOI 10.1126/science.1106148 · PMID 15718470 |
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 | 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
- Lysosomal mTORC2/PHLPP1/Akt regulate chaperone-mediated autophagy (2015)
- A dynamic network model of mTOR signaling reveals TSC-independent mTORC2 regulation (2012)
- The mammalian target of rapamycin complex 2 controls folding and stability of Akt and protein kinase C (2008)
- Active-site inhibitors of mTOR target rapamycin-resistant outputs of mTORC1 and mTORC2 (2009)
Learn the biology
Want to understand the biology behind this study? → Growth Factor Signalling
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