LARS (leucyl-tRNA synthetase)
Enzyme that charges tRNA with leucine, proposed as an alternative intracellular leucine sensor acting as a GAP for RagD. Competes with the Sestrin2 model - an unresolved question in the field.
A contested second leucine detector. An enzyme that loads the amino acid leucine onto its transport molecule (tRNA) so cells can build proteins. Some scientists think it might also work as a second sensor that tells mTORC1 when leucine is available - a rival idea to the more established Sestrin2 sensor, and the two ideas haven't been fully reconciled.
The moonlighting-GAP model has not reproduced cleanly across labs and competes with the Sestrin2 model; shown here as contested rather than omitted.
TL;DR. LARS (leucyl-tRNA synthetase) appears in 1 curated study in Oliver's mTOR Atlas: 1 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
| Interaction | Mechanism | Evidence | Studies |
|---|---|---|---|
| LARS (leucyl-tRNA synthetase) activates Rag GTPases mechanism: gap-activity · this link in full · on the map table | In that model, this enzyme flips the other Rag protein into its working shape – an alternative route from leucine to the Rags. In this model LARS acts as a GAP for RagD, doing for the RagC/D half what FLCN does - an alternative route from leucine to the Rags. In this model LARS acts as a GAP for RagD, doing for the RagC/D half what FLCN does - an alternative route from leucine to the Rags. Holds under: Human cell biochemistry only, and cell-type dependence was never mapped. The reaction it claims - GAP activity on the RagC/D half - is the same reaction this Atlas assigns to FLCN, and the two assignments have never been reconciled head-to-head. Read together with LEU-LARS: if the upstream leucine-sensing claim does not hold, this edge loses its input. not tested in people · disputed: at least one study points the other way | M | HAN2012 |
| Leucine activates LARS (leucyl-tRNA synthetase) mechanism: binding · this link in full · on the map table | One competing idea: the enzyme that loads leucine onto its transport molecule for protein-building doubles as the leucine sensor. A competing model: the enzyme that loads leucine onto tRNA doubles as the leucine sensor, binding free leucine directly. A competing model: the enzyme that loads leucine onto tRNA doubles as the leucine sensor, binding free leucine directly. Holds under: Proposed before the Sestrin2 model and never cleanly reconciled with it. not tested in people · disputed: at least one study points the other way | M | HAN2012 |
Evidence at a glance
| Evidence | What it means | Studies |
|---|---|---|
| M | Molecular — cells, biochemistry, structure | 1 |
No direct human evidence in the Atlas for this entity yet — everything below rests on animal or molecular work.
Studies
| Year | Evidence | Study |
|---|---|---|
| 2012 | M | Leucyl-tRNA synthetase is an intracellular leucine sensor for the mTORC1-signaling pathway HAN2012 Leucyl-tRNA synthetase acts as an intracellular leucine sensor activating mTORC1 via the Rag pathway. |
Related entities
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