Oliver's mTOR Atlas Evidence Platform
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SLC38A9

Gene/Protein · 5 studies in the Atlas

Lysosomal amino-acid transporter and signaling component; acts as an arginine sensor on the lysosomal membrane. Works together with v-ATPase and Ragulator to relay luminal arginine availability to the Rag GTPases and thereby recruit mTORC1. Loss of SLC38A9 impairs arginine-dependent mTORC1 activation.

A lysosomal arginine sensor and exporter.

Its cytosolic N-terminus binds Rag–Ragulator arginine-dependently; the transport and signalling functions are separable and both matter.

Evidence at a glance

EvidenceWhat it meansStudies
M Molecular — cells, biochemistry, structure5

No direct human evidence in the Atlas for this entity yet — everything below rests on animal or molecular work.

Studies

YearEvidenceStudy
2018 M Crystal structure of arginine-bound lysosomal transporter SLC38A9 in the cytosol-open state LEI2018 Crystal structure of arginine-bound SLC38A9 reveals the basis of lysosomal arginine sensing.
2017 M mTORC1 Activator SLC38A9 Is Required to Efflux Essential Amino Acids from Lysosomes and Use Protein as a Nutrient WYA2017 SLC38A9 effluxes essential amino acids (e.g. leucine) from lysosomes to activate mTORC1.
2015 M Amino Acid-Dependent mTORC1 Regulation by the Lysosomal Membrane Protein SLC38A9 JUN2015 SLC38A9, a lysosomal membrane protein, mediates amino-acid-dependent mTORC1 activation.
2015 M SLC38A9 is a component of the lysosomal amino acid sensing machinery that controls mTORC1 REB2015 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 mTORC1 WAN2015 The lysosomal transporter SLC38A9 signals arginine sufficiency to mTORC1.

Related entities

Arginine 3Leucine 1