Oliver's mTOR Atlas Evidence Platform
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Pathway link SLC38A9-RAG

SLC38A9 Rag GTPases

SLC38A9 activates Rag GTPases.

SLC38A9 sits in the lysosome's wall, senses arginine inside, and then flips RagA into its "on" shape, telling the Rag proteins there's enough.

SLC38A9 sits in the lysosomal membrane and reads arginine on the inside. Arginine-bound SLC38A9 acts as an exchange factor that loads RagA with GTP, switching the Rag dimer on (SHE2018B); it also pumps essential amino acids, including leucine, back out into the cytosol.

The conditions it holds under

Mammalian cell studies and purified-protein work (REB2015, WAN2015, JUN2015, WYA2017, SHE2018B). Cell and biochemical evidence; whole-animal and human relevance are not tested here.

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
2015 M SLC38A9 is a component of the lysosomal amino acid sensing machinery that controls mTORC1REB2015 SLC38A9 is a component of the lysosomal amino-acid sensing machinery controlling mTORC1.
2015 M Metabolism. Lysosomal amino acid transporter SLC38A9 signals arginine sufficiency to mTORC1WAN2015 The lysosomal transporter SLC38A9 signals arginine sufficiency to mTORC1.
2015 M Amino Acid-Dependent mTORC1 Regulation by the Lysosomal Membrane Protein SLC38A9JUN2015 SLC38A9, a lysosomal membrane protein, mediates amino-acid-dependent mTORC1 activation.
2017 M mTORC1 Activator SLC38A9 Is Required to Efflux Essential Amino Acids from Lysosomes and Use Protein as a NutrientWYA2017 SLC38A9 effluxes essential amino acids (e.g. leucine) from lysosomes to activate mTORC1.
2018 M Ragulator and SLC38A9 activate the Rag GTPases through noncanonical GEF mechanismsSHE2018B Ragulator and SLC38A9 each act as an unusual guanine-nucleotide exchange factor on the Rag heterodimer, and together they push it into its active state. Ragulator triggers GTP release from RagC, which unlocks the inactive configuration; arginine-bound SLC38A9 converts RagA from the GDP- to the GTP-loaded state. Boundary: purified proteins and cultured human cells. This is the biochemistry of the switch, not a measurement in tissue.

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.

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