Oliver's mTOR Atlas Evidence Platform
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Pathway link GATOR1-RAG

GATOR1 Rag GTPases

GATOR1 inhibits Rag GTPases.

GATOR1 forces the Rag proteins into their "off" shape, so they can no longer hold onto mTORC1.

GATOR1 acts as a GAP: it forces RagA/B to hydrolyse GTP, flipping the Rag heterodimer into the inactive shape that cannot hold mTORC1.

The conditions it holds under

Human cell biochemistry with cancer genomics (BAR2013) and a cryo-EM structure (SHE2018). GAP activity is shown on purified and cellular Rags; the cited studies do not test it in whole animals or in people.

Time it takes
seconds
Step
direct (one molecule acts on the other)
Measured in
human cells
Where in the cell
lysosome
Reaches people?
plausible in people, not shown directly
How settled
settled in the literature

Studies behind it

YearEvidenceStudy
2013 M A Tumor suppressor complex with GAP activity for the Rag GTPases that signal amino acid sufficiency to mTORC1BAR2013 Found the OFF switch for amino acid signaling: the GATOR1 complex is a GAP that shuts the Rag GTPases (and thus mTORC1) down when amino acids run low, while GATOR2 opposes it. GATOR1 genes are mutated in cancers, making those tumors 'blind' to starvation and hypersensitive to rapamycin.
2018 M Architecture of the human GATOR1 and GATOR1-Rag GTPases complexesSHE2018 Cryo-EM structures of GATOR1 and GATOR1-Rag complexes reveal GAP and inhibitory-clamp mechanisms.

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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