Cited by 266PI3K/AKT/mTOR signaling in cancerAutophagy in Disease and TherapyMetabolism, Diabetes, and Cancer

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Amino Acid-Dependent mTORC1 Regulation by the Lysosomal Membrane Protein SLC38A9

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Jung, Jennifer, Genau, Heide Marika, Behrends, Christian·2015·Molecular and Cellular Biology

DOI 10.1128/mcb.00125-15PMC PMC4475919

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Abstract

The serine/threonine kinase mTORC1 regulates cellular homeostasis in response to many cues, such as nutrient status and energy level. Amino acids induce mTORC1 activation on lysosomes via the small Rag GTPases and the Ragulator complex, thereby controlling protein translation and cell growth. Here, we identify the human 11-pass transmembrane protein SLC38A9 as a novel component of the Rag-Ragulator complex. SLC38A9 localizes with Rag-Ragulator complex components on lysosomes and associates with Rag GTPases in an amino acid-sensitive and nucleotide binding state-dependent manner. Depletion of SLC38A9 inhibits mTORC1 activity in the presence of amino acids and in response to amino acid replenishment following starvation. Conversely, SLC38A9 overexpression causes RHEB (Ras homolog enriched in brain) GTPase-dependent hyperactivation of mTORC1 and partly sustains mTORC1 activity upon amino acid deprivation. Intriguingly, during amino acid starvation mTOR is retained at the lysosome upon SLC38A9 depletion but fails to be activated. Together, the findings of our study reveal SLC38A9 as a Rag-Ragulator complex member transducing amino acid availability to mTORC1 activity.

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Predicting transmembrane protein topology with a hidden markov model: application to complete genomes11Edited by F. Cohen
Krogh, A., Larsson, B., von Heijne, G., & Sonnhammer, E. L. L. (2001) · Journal of Molecular Biology · doi:10.1006/jmbi.2000.4315 · Cited by 12,654
Antimicrobial Autophagy: A Conserved Innate Immune Response in Drosophila
Moy, R. H., & Cherry, S. R. (2013) · Journal of Innate Immunity · doi:10.1159/000350326 · Cited by 3,551
mTOR Interacts with Raptor to Form a Nutrient-Sensitive Complex that Signals to the Cell Growth Machinery
Kim, D., Sarbassov, D. D., Ali, S. M., King, J. E., Latek, R. R., Erdjument‐Bromage, H., Tempst, P., & Sabatini, D. M. (2002) · Cell · doi:10.1016/s0092-8674(02)00808-5 · Cited by 3,051
Defining the role of mTOR in cancer
Guertin, D. A., & Sabatini, D. M. (2007) · Cancer Cell · doi:10.1016/j.ccr.2007.05.008 · Cited by 2,833
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 · cited 13×
“Cycling of mTOR between cytosol and lysosome generally is coupled to its inactive and active states, respectively, and depends on Rag GTPases, Ragulator, TSC, and RHEB GTPase (9, 16, 23, 31).”
BackgroundInfluential
Rheb GTPase is a direct target of TSC2 GAP activity and regulates mTOR signaling
Inoki, K., Li, Y., Xu, T., & Guan, K.-L. (2003) · Genes & Development · doi:10.1101/gad.1110003 · Cited by 1,911
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
A tissue-specific atlas of mouse protein phosphorylation and expression
Huttlin, E. L., Jedrychowski, M. P., Elias, J. E., Goswami, T., Rad, R., Beausoleil, S. A., Villén, J., Haas, W., Sowa, M. E., & Gygi, S. P. (2010) · Cell · doi:10.1016/j.cell.2010.12.001 · Cited by 1,778
Drug—target network
Yıldırım, M. A., Goh, K.-I., Cusick, M. E., Barabási, A.-Ĺ., & Vidal, M. (2007) · Nature Biotechnology · doi:10.1038/nbt1338 · Cited by 1,744

Show all 55 references

Research works printed but not linked: 1

Pinilla J, 2011, Front Biosci, 3, 1289

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Jiang, C., Tan, X., Jin, J., & Wang, P. (2025) · Advanced Science · doi:10.1002/advs.202501889 · Cited by 12
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Gao, Z., Liu, C., Mai, K., & He, G. (2022) · Engineering · doi:10.1016/j.eng.2022.05.019 · Cited by 13
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Wang, D., Wan, X., Du, X., Zhong, Z., Peng, J., Xiong, Q., Chai, J., & Jiang, S. (2021) · Biomolecules · doi:10.3390/biom11091314 · Cited by 17
Review: Nutritional regulation of muscle growth in neonatal swine
Posey, E. A., & Davis, T. A. (2023) · animal · doi:10.1016/j.animal.2023.100831 · Cited by 12
Physical decline and survival in the elderly are affected by the genetic variability of amino acid transporter genes
Crocco, P., Hoxha, E., Dato, S., Rango, F. D., Montesanto, A., Rose, G., & Passarino, G. (2018) · Aging · doi:10.18632/aging.101420 · Cited by 12
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Retracted
Polarization and asymmetry in T cell metabolism
Kamiński, M. M., Liedmann, S., Milasta, S., & Green, D. R. (2016) · Seminars in Immunology · doi:10.1016/j.smim.2016.10.002 · Cited by 11
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Baskaran, P., Mihaylov, S. R., Vinsland, E., Shah, K., Granat, L., Ultanir, S. K., Tee, A. R., Murn, J., & Bateman, J. M. (2022) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2022.102788 · Cited by 10
Homeostatic responses to amino acid insufficiency
Anthony, T. G. (2015) · Animal nutrition · doi:10.1016/j.aninu.2015.10.001 · Cited by 10
Lysosomal membrane contact sites: Integrative hubs for cellular communication and homeostasis
Bandyopadhyay, S., Adebayo, D., Obaseki, E., & Hariri, H. H. (2024) · Current topics in membranes · doi:10.1016/bs.ctm.2024.07.001 · Cited by 9
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Wang, D., Guo, C., Wan, X., Guo, K., Niu, H., Zheng, R., Chai, J., & Jiang, S. (2021) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2021.06.083 · Cited by 6

Authors: Jung, J., Genau, H. M., & Behrends, C.
Affiliations: Goethe University Frankfurt (DE)
Corresponding author: Behrends, Christian
ORCID: Jung, Jennifer
Behrends, Christian
Venue: Molecular and Cellular Biology
Publisher: Informa UK Limited
Published: 2015-07-01
Volume: 35
Issue: 14
Pages: 2479-2494
ISSN: 0270-7306 (ISSN-L)
1098-5549
DOI: 10.1128/mcb.00125-15
PMC: PMC4475919
OpenAlex: W2257572427
Cited by: 266
References: 55
Citations by year: 2026: 9 · 2025: 11 · 2024: 16 · 2023: 23 · 2022: 23 · 2021: 37 · 2020: 20 · 2019: 28 · 2018: 29 · 2017: 33 · 2016: 30 · 2015: 6
FWCI: 14.19
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: journals.asm.org/non-commercial-tdm-license (tdm)
Locations: Molecular and Cellular Biology (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Funders: Deutsche Forschungsgemeinschaft (BE 4685/1‐1)
FP7 Ideas: European Research Council (282333)
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, Rag GTPases, amino acid signaling, lysosomes, Rheb, amino acid starvation, transmembrane proteins, translational regulation
MeSH terms: Ras Homolog Enriched in Brain Protein, Mechanistic Target of Rapamycin Complex 1, Amino Acids, Fluorescent Antibody Technique, Humans, Lysosomes, Neuropeptides, Protein Binding, Immunoblotting, GTP Phosphohydrolases, Monomeric GTP-Binding Proteins, Amino Acid Transport Systems, RNA Interference, Multiprotein Complexes, HEK293 Cells, TOR Serine-Threonine Kinases, Protein Interaction Maps

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Amino Acid-Dependent mTORC1 Regulation by the Lysosomal Membrane Protein SLC38A9

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