AMPK and mTOR regulate autophagy through direct phosphorylation of Ulk1
What this study shows
Revealed the tug-of-war over ULK1: the energy sensor AMPK phosphorylates ULK1 at activating sites to turn autophagy ON when energy is low, while mTORC1 phosphorylates a different site (Ser757) to keep it OFF and even blocks AMPK from reaching ULK1. Two opposing kinases wired to the same switch.
At a glance
| Evidence type | M Molecular — cells, biochemistry, structure Marked M because it is molecular or in-vitro work (model: Human/mouse 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 | Human/mouse cells |
| Journal | Nature Cell Biology |
| Year | 2011 |
| Peer reviewed | Yes |
| Record last updated | 2026-08-22 |
| Source | DOI 10.1038/ncb2152 · PMID 21258367 · Free full text (PMC3987946) |
Extracted findings
| Intervention | Genetic/biochemical (AMPK, mTOR, ULK1) |
| Target | AMPK / mTOR / ULK1 |
| Model | Human/mouse cells |
| Effect | AMPK and mTOR reciprocally phosphorylate ULK1 to regulate autophagy |
In the Atlas
Related topics
More studies on this topic
- Ulk1-mediated phosphorylation of AMPK constitutes a negative regulatory feedback loop (2011)
- Urolithin A activates mitophagy via the AMPK-mTOR axis and modulates the gut-ceramide axis to ameliorate cardiac remodeling in HFpEF (2026)
- Nutrient-dependent mTORC1 association with the ULK1-Atg13-FIP200 complex required for autophagy (2009)
- Association of rapamycin treatment with the modulation of purine metabolism, reduced microglial inflammatory responses, improved mitochondrial energy metabolism, and alleviation of fatigue symptoms in ME/CFS subjects: pilot findings from phase-II observational study (2026)
Learn the biology
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