Nutrient-dependent mTORC1 association with the ULK1-Atg13-FIP200 complex required for autophagy
What this study shows
Showed the DIRECT brake mTORC1 uses on autophagy: when nutrients are plentiful, mTORC1 physically joins the ULK1-Atg13-FIP200 complex (the autophagy-starter kinase) and phosphorylates ULK1 to keep it off. Starvation or rapamycin releases this brake and autophagy begins.
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 | Molecular Biology of the Cell |
| Year | 2009 |
| Peer reviewed | Yes |
| Record last updated | 2026-08-22 |
| Source | DOI 10.1091/mbc.e08-12-1248 · PMID 19211835 · Free full text (PMC2663915) |
Extracted findings
| Intervention | Genetic/biochemical (mTORC1/ULK1-Atg13-FIP200) |
| Target | mTORC1 / ULK1-Atg13-FIP200 |
| Model | Mammalian cells |
| Effect | Nutrient-dependent mTORC1 association with the ULK1-Atg13-FIP200 complex controls autophagy induction |
In the Atlas
Related topics
More studies on this topic
- AMPK and mTOR regulate autophagy through direct phosphorylation of Ulk1 (2011)
- 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)
- 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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