Oliver's mTOR Atlas Evidence Platform
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Pathway link ARG-CASTOR1

Arginine CASTOR1

Arginine inhibits CASTOR1.

Arginine sticks to CASTOR1 the same way leucine sticks to Sestrin2 – the same trick, for a different amino acid.

Cytosolic arginine binds CASTOR1 and breaks its grip on GATOR2 - the same trick as leucine/Sestrin2, but for a different amino acid.

The conditions it holds under

Human cells and structural work (CHA2016, SAX2016). Shows how arginine is sensed in cells. Whether this sensor matters for arginine supply in a whole animal or a person is not tested here.

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

Studies behind it

YearEvidenceStudy
2016 M The CASTOR Proteins Are Arginine Sensors for the mTORC1 PathwayCHA2016 Identified CASTOR1 as the direct arginine sensor: when arginine binds CASTOR1, it lets go of GATOR2, switching mTORC1 on. Together with Sestrin2 (leucine) this built the picture of mTORC1 as a cell that literally tastes individual amino acids.
2016 M Mechanism of arginine sensing by CASTOR1 upstream of mTORC1SAX2016 CASTOR1 is a direct arginine sensor upstream of mTORC1; structure reveals the arginine-binding mechanism.

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.

“Inhibits” describes the effect on the target's activity, not on how much of it there is.

“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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