Oliver's mTOR Atlas Evidence Platform
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Pathway link LARS-RAG

LARS (leucyl-tRNA synthetase) Rag GTPases

LARS (leucyl-tRNA synthetase) activates Rag GTPases.

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.

The conditions it 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.

Time it takes
seconds
Step
not yet resolved
Measured in
human cells
Where in the cell
lysosome
Reaches people?
not tested in people
How settled
disputed: at least one study points the other way

Studies behind it

YearEvidenceStudy
2012 M Leucyl-tRNA synthetase is an intracellular leucine sensor for the mTORC1-signaling pathwayHAN2012 Leucyl-tRNA synthetase acts as an intracellular leucine sensor activating mTORC1 via the Rag pathway.

Points the other way

No study in the Atlas contradicts this link. That means none in this curated set, not none in the literature.

Who has checked this

Checked by
No researcher outside the project has checked this link yet.
Curator sign-off
Not signed off yet. This link was drafted with AI help and has not been reviewed link by link; treat it as a proposal until it is.
Curated by
Oliver Barton, with AI help for drafting; see how links are checked.

The source works as a GAP: it changes the GTP or GDP state of the target. The label says what that does to the target, not that the target is switched on or off everywhere.

“How settled” describes how far researchers in the field agree. It is not the same as the sign-off above, which only says whether a named curator has checked this page.

If this link rests on your own work: a click on “This looks right” below, or a short note through “Report an error”, helps us more than anything else on this page.

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