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SLC38A9 is a component of the lysosomal amino acid sensing machinery that controls mTORC1
Open accessAbstract
Cell growth and proliferation are tightly linked to nutrient availability. The mechanistic target of rapamycin complex 1 (mTORC1) integrates the presence of growth factors, energy levels, glucose and amino acids to modulate metabolic status and cellular responses. mTORC1 is activated at the surface of lysosomes by the RAG GTPases and the Ragulator complex through a not fully understood mechanism monitoring amino acid availability in the lysosomal lumen and involving the vacuolar H(+)-ATPase. Here we describe the uncharacterized human member 9 of the solute carrier family 38 (SLC38A9) as a lysosomal membrane-resident protein competent in amino acid transport. Extensive functional proteomic analysis established SLC38A9 as an integral part of the Ragulator-RAG GTPases machinery. Gain of SLC38A9 function rendered cells resistant to amino acid withdrawal, whereas loss of SLC38A9 expression impaired amino-acid-induced mTORC1 activation. Thus SLC38A9 is a physical and functional component of the amino acid sensing machinery that controls the activation of mTOR.
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“The membrane-resident amino acid transporter SLC38A9 is a key component of this sensing machinery (452).”
From Placental Origins of Chronic Disease (2016) · cites this paper as [452]
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“Studies of SLC38A9 suggest that presence of amino acids, arginine in particular (Wang et al., 2015) are transmitted through SLC38A9-v-ATPase to the Rag GTPases (Jung et al., 2015; Rebsamen et al., 2015; Wang et al., 2015).”
From Signal integration in the (m)TORC1 growth pathway (2018) · cites this paper as Rebsamen et al., 2015
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Metadata
- Authors
- Rebsamen, M., Pochini, L., Stasyk, T., de Araújo, M. E. G., Galluccio, M., Kandasamy, R. K., Snijder, B., Fauster, A., Rudashevskaya, E. L., Bruckner, M., Scorzoni, S., Filipek, P. A., Huber, K. V. M., Bigenzahn, J. W., Heinz, L. X., Kraft, C., Bennett, K. L., Indiveri, C., Huber, L. A., & Superti-Furga, G.
- Affiliations
- Austrian Academy of Sciences (AT)
- University of Calabria (IT)
- Innsbruck Medical University (AT)
- University of Vienna (AT)
- ORCID
- Venue
- Nature
- Published
- 2015-01-07
- Volume
- 519
- Issue
- 7544
- Pages
- 477-481
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- PMC
- PMC4376665
- OpenAlex
- W2093154482
- Cited by
- 673
- References
- 40
- Citations by year
- 2026: 32 · 2025: 47 · 2024: 34 · 2023: 45 · 2022: 55 · 2021: 91 · 2020: 57 · 2019: 50 · 2018: 65 · 2017: 60 · 2016: 76 · 2015: 59
- FWCI
- 37.65
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- RePEc: Research Papers in Economics (submittedVersion)
- Archive of Doctoral Theses and Digital Collections (University of Calabria) (submittedVersion)
- Funders
- U.S. Department of Veterans Affairs (HIR 10-001)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › PI3K/AKT/mTOR signaling in cancer
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolism, Diabetes, and Cancer
- Keywords
- SLC38A9, mTORC1, amino acid sensing, lysosomes, Ragulator complex, Rag GTPases, amino acid transport, lysosomal membrane proteins, nutrient signaling, cell growth and proliferation
- MeSH terms
- Mechanistic Target of Rapamycin Complex 1, Amino Acids, Animals, Cell Line, Humans, Lysosomes, Nucleotides, Monomeric GTP-Binding Proteins, Amino Acid Transport Systems, Multiprotein Complexes, Mice, TOR Serine-Threonine Kinases
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