Oliver's mTOR Atlas Evidence Platform
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Glutamine

Nutrient/Metabolite · 4 studies in the Atlas

Most abundant free amino acid; activates mTORC1 partly through glutaminolysis and, in some settings, through a Rag-independent Arf1 route - one of the clearest examples that 'amino acid sensing' is not a single mechanism.

Abundant amino acid with a disputed route in. The most abundant free amino acid in the body. It switches on mTORC1 partly by being broken down for fuel and, in some cell types, through a completely separate route that skips the usual Rag-GTPase sensors - a reminder that 'amino acid sensing' isn't just one single mechanism.

Rag-independent glutamine signalling via Arf1 is reported but not universally reproduced; treat the route as unsettled.

TL;DR. Glutamine appears in 4 curated studies in Oliver's mTOR Atlas: 2 in animal models; 2 at the molecular level (cells, biochemistry, structure). 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

2 interactions in the curated mTOR pathway model. Each row is a claim with the evidence behind it; the evidence code is the kind of study, not its quality.

InteractionMechanismEvidenceStudies
Glutamine activates Rag GTPases mechanism: signal-relay · this link in full · on the map table Glutamine can switch on mTORC1 partly just by being burned for fuel: burning it makes a molecule that helps the Rag proteins pull mTORC1 to the lysosome. Glutamine burned through glutaminolysis raises alpha-ketoglutarate, which promotes RagB GTP loading and mTORC1 translocation to the lysosome. This edge asserts the Rag-dependent route only. Glutamine burned through glutaminolysis raises alpha-ketoglutarate, which promotes RagB GTP loading and mTORC1 translocation to the lysosome. This edge asserts the Rag-dependent route only. Holds under: Cell-type dependent, and deliberately narrow: the separate claim that glutamine can reach mTORC1 without the Rags is carried by its own edge rather than folded in here. not tested in people · emerging, few independent studies M DUR2012
Glutamine activates mTORC1 mechanism: signal-relay · this link in full · on the map table Some experiments say glutamine has a second way in that skips the Rag proteins entirely. If that is right, the lysosome story is not the whole story – which is a big claim resting on thin evidence. A second and contested way in: JEW2015 reports that glutamine activates mTORC1 without the Rag GTPases, through Arf1, and that leucine and glutamine therefore do not share one entry point. If it holds, Rag-dependent lysosomal recruitment is not the only route to the kinase. A second and contested way in: JEW2015 reports that glutamine activates mTORC1 without the Rag GTPases, through Arf1, and that leucine and glutamine therefore do not share one entry point. If it holds, Rag-dependent lysosomal recruitment is not the only route to the kinase. Holds under: Cell-type dependent and not uniformly reproduced across labs. The Rag-dependent route is the separate GLN-RAG edge; neither edge should be read as covering the other. not tested in people · disputed: at least one study points the other way M JEW2015

Evidence at a glance

EvidenceWhat it meansStudies
A Animal model2
M Molecular — cells, biochemistry, structure2

No direct human evidence in the Atlas for this entity yet — everything below rests on animal or molecular work.

Studies

YearEvidenceStudy
2026 A Glutamine alleviates bisphenol A-induced jejunal injury in piglets involving mitochondrial function restoration and AMPK-mTOR signaling regulation. XIE2026 Glutamine supplementation alleviated bisphenol A-induced jejunal injury in piglets, restoring mitochondrial energy metabolism and barrier integrity alongside modulation of AMPK-mTOR signalling.
2011 A The transcription factor Myc controls metabolic reprogramming upon T lymphocyte activation WAN2011 The transcription factor Myc drives metabolic reprogramming of activated T cells downstream of mTOR.
2015 M Metabolism. Differential regulation of mTORC1 by leucine and glutamine JEW2015 Glutamine activates mTORC1 via a Rag-independent, Arf1-dependent route distinct from leucine.
2012 M Glutaminolysis activates Rag-mTORC1 signaling DUR2012 Glutaminolysis activates Rag-mTORC1 signalling through alpha-ketoglutarate production.

Related entities

Bisphenol ALeucine 1AMPK 1

Cite this page

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Barton, O. (2026). Glutamine [Entity page]. In Oliver's mTOR Atlas [Data set]. https://mtor-atlas.org/nutrient/glutamine/ · Dataset DOI 10.5281/zenodo.22059963

@misc{atlas_nutrient_glutamine,
  author       = {Barton, Oliver},
  title        = {{Oliver's mTOR Atlas}: Glutamine},
  howpublished = {Entity page in a data set},
  year         = {2026},
  url          = {https://mtor-atlas.org/nutrient/glutamine/},
  doi          = {10.5281/zenodo.22059963}
}
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