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This research aims to investigate the role of SLC38A9 in mTORC1 activation in response to arginine levels.

January 9, 2015Open Access

Metabolism. Lysosomal amino acid transporter SLC38A9 signals arginine sufficiency to mTORC1.

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Experimental findings reveal SLC38A9 regulates mTORC1 activation by arginine, indicating its role as an arginine sensor.

This research aims to investigate the role of SLC38A9 in mTORC1 activation in response to arginine levels.
Identified SLC38A9 as an amino acid-sensitive lysosomal protein interacting with Rag GTPases.
Assessed the effects of SLC38A9 loss and overexpression on mTORC1 signaling in response to amino acids.
Utilized biochemical assays to examine arginine transport and mTORC1 activity.
Loss of SLC38A9 significantly reduces mTORC1 activation by arginine (P<0.01).
Overexpression of SLC38A9 results in constant mTORC1 signaling, even with limited amino acids available.
SLC38A9 functions upstream of Rag GTPases in the mTORC1 activation pathway.

Wang et al. (2015) studied this question.

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