Cited by 673PI3K/AKT/mTOR signaling in cancerAutophagy in Disease and TherapyMetabolism, Diabetes, and Cancer

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SLC38A9 is a component of the lysosomal amino acid sensing machinery that controls mTORC1

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Rebsamen, Manuele, Pochini, Lorena, Stasyk, Taras, de Araújo, Mariana E. G., Galluccio, Michele, Kandasamy, Richard K., Snijder, Berend, Fauster, Astrid, Rudashevskaya, Elena L., Bruckner, Manuela, Scorzoni, Stefania, Filipek, Przemyslaw A., Huber, Kilian V. M., Bigenzahn, Johannes W., Heinz, Leonhard X., Kraft, Claudine, Bennett, Keiryn L., Indiveri, Cesare, Huber, Lukas A., Superti-Furga, Giulio·2015·Nature

DOI 10.1038/nature14107PMC PMC4376665

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Abstract

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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mTOR Signaling in Growth Control and Disease
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The International Transporter Consortium, Giacomini, K. M., Huang, S.-M., Tweedie, D. J., Benet, L. Z., Brouwer, K. L. R., Chu, X., Dahlin, A., Evers, R., Fischer, V., et al. (2010) · Nature Reviews Drug Discovery · doi:10.1038/nrd3028 · Cited by 3,340
The Rag GTPases Bind Raptor and Mediate Amino Acid Signaling to mTORC1
Sancak, Y., Peterson, T. R., Shaul, Y. D., Lindquist, R. A., Thoreen, C. C., Bar-Peled, L., & Sabatini, D. M. (2008) · Science · doi:10.1126/science.1157535 · Cited by 2,773
Ragulator-Rag Complex Targets mTORC1 to the Lysosomal Surface and Is Necessary for Its Activation by Amino Acids
Sancak, Y., Bar-Peled, L., Zoncu, R., Markhard, A. L., Nada, S., & Sabatini, D. M. (2010) · Cell · doi:10.1016/j.cell.2010.02.024 · Cited by 2,464
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Uhlen, M., Oksvold, P., Fagerberg, L., Lundberg, E., Jonasson, K., Forsberg, M., Zwahlen, M., Kampf, C., Wester, K., Hober, S., et al. (2010) · Nature Biotechnology · doi:10.1038/nbt1210-1248 · Cited by 2,440
A lysosome‐to‐nucleus signalling mechanism senses and regulates the lysosome via mTOR and TFEB
Settembre, C., Zoncu, R., Medina, D. L., Vetrini, F., Erdin, S., Erdin, S., Huynh, T., Ferron, M., Karsenty, G., Vellard, M. C., et al. (2012) · The EMBO Journal · doi:10.1038/emboj.2012.32 · Cited by 1,920
Bidirectional Transport of Amino Acids Regulates mTOR and Autophagy
Nicklin, P., Bergman, P., Zhang, B., Triantafellow, E., Wang, H., Nyfeler, B., Yang, H., Hild, M., Kung, C., Wilson, C., et al. (2009) · Cell · doi:10.1016/j.cell.2008.11.044 · Cited by 1,798
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Mellacheruvu, D., Wright, Z., Couzens, A. L., Lambert, J.-P., St-Denis, N. A., Li, T., Miteva, Y. V., Hauri, S., Sardiu, M. E., Low, T. Y., et al. (2013) · Nature Methods · doi:10.1038/nmeth.2557 · Cited by 1,686
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Zoncu, R., Bar-Peled, L., Efeyan, A., Wang, S., Sancak, Y., & Sabatini, D. M. (2011) · Science · doi:10.1126/science.1207056 · Cited by 1,673
Regulation of TORC1 by Rag GTPases in nutrient response
Kim, E., Goraksha-Hicks, P., Li, L., Neufeld, T. P., & Guan, K.-L. (2008) · Nature Cell Biology · doi:10.1038/ncb1753 · Cited by 1,349

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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: Rebsamen, Manuele
Pochini, Lorena
Stasyk, Taras
Galluccio, Michele
Kandasamy, Richard K.
Snijder, Berend
Fauster, Astrid
Scorzoni, Stefania
Filipek, Przemyslaw A.
Huber, Kilian V. M.
Bigenzahn, Johannes W.
Heinz, Leonhard X.
Kraft, Claudine
Bennett, Keiryn L.
Indiveri, Cesare
Huber, Lukas A.
Venue: Nature
Publisher: Springer Science and Business Media LLC
Published: 2015-01-07
Volume: 519
Issue: 7544
Pages: 477-481
ISSN: 0028-0836 (ISSN-L)
1476-4687
DOI: 10.1038/nature14107
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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SLC38A9 is a component of the lysosomal amino acid sensing machinery that controls mTORC1

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