Oliver's mTOR Atlas Evidence Platform
Reading level
Mode

SAMTOR

Gene/Protein · 2 studies in the Atlas

Sensor of S-adenosylmethionine (SAM), linking methionine / one-carbon metabolism to mTORC1 via GATOR1.

A methionine detector. A sensor for S-adenosylmethionine (SAM), a molecule that reports how much of the amino acid methionine is available. It links methionine metabolism to mTORC1 through the GATOR1 brake.

SAM binding dissociates SAMTOR from GATOR1–KICSTOR, relieving GATOR1 activity. Wires one-carbon metabolism into nutrient sensing.

TL;DR. SAMTOR appears in 2 curated studies in Oliver's mTOR Atlas: 1 at the molecular level (cells, biochemistry, structure); 1 review. 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 (1 acting from SAMTOR, 1 acting on it). Each row is a claim with the evidence behind it; the evidence code is the kind of study, not its quality.

InteractionMechanismEvidenceStudies
SAMTOR activates GATOR1 mechanism: binding · this link in full · on the map table When methionine is low, SAMTOR teams up with GATOR1 to help keep mTORC1 switched off. Methionine-starved SAMTOR binds the GATOR1-KICSTOR complex and helps it keep mTORC1 off. Methionine-starved SAMTOR binds the GATOR1-KICSTOR complex and helps it keep mTORC1 off. Holds under: One biochemical study in human cells (GU2017). A single study in cell culture; the consensus is emerging, not settled. plausible in people, not shown directly · emerging, few independent studies M GU2017
S-adenosylmethionine (SAM) inhibits SAMTOR mechanism: binding · this link in full · on the map table SAM, a byproduct of methionine, binds SAMTOR and pulls it away from GATOR1 – the proposed way the cell senses how much methionine it has. Worked out in cells; whether this sensor is what matters in a whole animal has not been shown. S-adenosylmethionine, the cell's methyl-donor currency, binds SAMTOR and pulls it off GATOR1 - this is how methionine availability reaches mTORC1. S-adenosylmethionine, the cell's methyl-donor currency, binds SAMTOR and pulls it off GATOR1 - this is how methionine availability reaches mTORC1. Holds under: Single-study edge. Needs independent replication before it is treated as established. plausible in people, not shown directly · emerging, few independent studies M GU2017

Evidence at a glance

EvidenceWhat it meansStudies
M Molecular — cells, biochemistry, structure1
R Review — secondary literature, not a new result1

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

Studies

YearEvidenceStudy
2017 M SAMTOR is an S-adenosylmethionine sensor for the mTORC1 pathway GU2017 Extended nutrient sensing beyond amino acids to METABOLITES: SAMTOR reads S-adenosylmethionine (SAM), the cell's methyl-donor currency, linking methionine and one-carbon metabolism to mTORC1. Relevant to why methionine restriction affects aging.
2017 R The Dawn of the Age of Amino Acid Sensors for the mTORC1 Pathway WOLF2017 Review of the newly discovered amino-acid sensors feeding into mTORC1.

Related entities

mTORC1 2CASTOR1 1Sestrin2 1SLC38A9 1S-adenosylmethionine (SAM) 1GATOR1 1

Cite this page

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

@misc{atlas_gene_samtor,
  author       = {Barton, Oliver},
  title        = {{Oliver's mTOR Atlas}: SAMTOR},
  howpublished = {Entity page in a data set},
  year         = {2026},
  url          = {https://mtor-atlas.org/gene/samtor/},
  doi          = {10.5281/zenodo.22059963}
}
Was this page useful?