Reactive oxygen species
ROS generated by mitochondrial activity, both a consequence and a driver of mTOR signalling.
Chemical damage from burning fuel. Chemical damage from burning fuel.
Bidirectional and therefore a loop, not an arrow: unleashing mTORC1 by deleting TSC1 floods haematopoietic stem cells with ROS and exhausts them, rescued by an antioxidant (CHE2008); conversely oxidative stress activates a redox-sensitive PI3K–Akt–mTORC1–eIF4A cascade (JIN2026). Which direction dominates depends on cell type and how sustained the oxidative load is.
TL;DR. Reactive oxygen species appears in 3 curated studies in Oliver's mTOR Atlas: 1 in animal models; 1 at the molecular level (cells, biochemistry, structure); 1 preprint, not peer-reviewed. No study in people is recorded for it in the Atlas yet. It has 2 interactions in the curated pathway model.
In the pathway model
| Interaction | Mechanism | Evidence | Studies |
|---|---|---|---|
| Reactive oxygen species activates mTORC1 mechanism: signal-relay · this link in full · on the map table | Oxidative damage can itself switch on mTORC1 through a chain of signals, closing a feedback loop that can turn a brief stress into a lasting one. Oxidative stress activates a redox-sensitive PI3K–Akt–mTORC1–eIF4A cascade that selectively promotes cap-dependent translation of P-glycoprotein. Oxidative stress activates a redox-sensitive PI3K–Akt–mTORC1–eIF4A cascade that selectively promotes cap-dependent translation of P-glycoprotein. Holds under: One cell-line study in a multidrug-resistance context; whether the loop runs in normal physiology at these ROS levels is untested. not tested in people · emerging, few independent studies | M | JIN2026 |
| mTORC1 activates Reactive oxygen species mechanism: functional-consequence · this link in full · on the map table | Switching mTORC1 on too much pushes resting stem cells to start dividing and floods them with reactive, damaging molecules; giving them antioxidants restores their normal function. Unleashing mTORC1 by deleting TSC1 drives quiescent haematopoietic stem cells into cycle, raises mitochondrial biogenesis and floods them with ROS; an antioxidant rescues self-renewal. Unleashing mTORC1 by deleting TSC1 drives quiescent haematopoietic stem cells into cycle, raises mitochondrial biogenesis and floods them with ROS; an antioxidant rescues self-renewal. Holds under: Demonstrated in haematopoietic stem cells, where quiescence is the baseline state. Cell types that are already cycling need not behave this way. plausible in people, not shown directly · emerging, few independent studies | A | CHE2008 |
Evidence at a glance
| Evidence | What it means | Studies |
|---|---|---|
| A | Animal model | 1 |
| M | Molecular — cells, biochemistry, structure | 1 |
| PP | Preprint, not peer-reviewed | 1 |
No direct human evidence in the Atlas for this entity yet — everything below rests on animal or molecular work.
Studies
| Year | Evidence | Study |
|---|---|---|
| 2008 | A | TSC-mTOR maintains quiescence and function of hematopoietic stem cells by repressing mitochondrial biogenesis and reactive oxygen species CHE2008 Showed why blood stem cells must keep mTOR LOW. Deleting TSC1 (which unleashes mTOR) drove resting stem cells into rapid division, flooded them with reactive oxygen species, and burned out their ability to self-renew. An antioxidant rescued them. A key link between mTOR, stem-cell exhaustion, and tissue aging. |
| 2026 | M | Redox-sensitive mTOR-eIF4A signaling promotes selective P-glycoprotein translation. JIN2026 Oxidative stress activates a redox-sensitive PI3K-AKT-mTORC1-eIF4A cascade that selectively promotes P-glycoprotein translation via cap-dependent mRNA engagement, revealing a transcription-independent mechanism of rapid multidrug resistance induction. |
| 2026 | PP | Redox activation of ATG5 licenses autophagy upon nutrient restriction SHI2026 Dietary restriction selectively oxidizes a specific, tissue-resolved set of cysteines rather than oxidizing the proteome broadly. One of the most strongly oxidized is Cys19 on the core autophagy protein ATG5; this oxidation is required for ATG5 to bind ATG10 and form the ATG5-ATG12 conjugate that lipidates LC3B and builds the autophagosome. In mice lacking this redox switch, nutrient restriction fails to trigger autophagy, causing severe tissue pathology and early death -- a single oxidized cysteine gates the autophagic response to fasting. |
Related entities
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