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Sodium-coupled neutral amino acid transporter 7 (SLC38A7, also known as SNAT7) is a **lysosomal membrane transporter** belonging to the solute carrier (SLC) family of proteins. It mediates the sodium-dependent export of **L-glutamine and L-asparagine from the lysosome into the cytosol** following lysosomal protein degradation[1][3][4][5]. SNAT7 is highly specific to these amino acids and is activated under acidic lysosomal pH, unlike other broadly-selective SLC38 family members[1]. SNAT7 is crucial for nutrient supply and growth in cancer cells facing glutamine scarcity, where it enables utilization of extracellular proteins internalized via macropinocytosis and processed by lysosomes[1][4][6]. It has also been identified as a regulator of mTORC1, a central pathway in cell growth and metabolism, particularly upon uptake of extracellular proteins[6]. In the brain, SLC38A7 is expressed in neurons and likely participates in neurotransmitter recycling, further contributing to CNS amino acid metabolism[2]. SLC38A7 does not have approved drugs directly targeting it but is under investigation as a candidate for anti-cancer strategies aimed at disrupting amino acid supply in nutrient-scavenging tumors[1][6]. Its essential role in normal physiological processes, including possible neuronal function, presents therapeutic challenges regarding specificity and safety[1][2].
Sodium-coupled symport of L-glutamine and L-asparagine from lysosome to cytoplasm, activation of mTORC1 pathway via nutrient sensing, supporting cell proliferation in glutamine-depleted environments
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