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

The DOI matches its Crossref record; 40 of the 40 references it cites were found in a registry or an index.

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

Open access

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

Open this paper in CoChat — free account

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.

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Integrity signals

Registry

Crossref · 10.1038/nature14107

Cites

40 of 40 references verified0 citation errors · 0 not checkable

Statistics

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

mTOR Signaling in Growth Control and Disease
Laplante, M., & Sabatini, D. M. (2012) · Cell · doi:10.1016/j.cell.2012.03.017 · Cited by 8,509
Membrane transporters in drug development
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
Towards a knowledge-based Human Protein Atlas
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
The CRAPome: a contaminant repository for affinity purification–mass spectrometry data
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
Self-citation
mTORC1 Senses Lysosomal Amino Acids Through an Inside-Out Mechanism That Requires the Vacuolar H + -ATPase
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

Flagged first, then by citations

Show all 40 references

Sorted by citations

Items 201–300 of 672

Beyond indigestion: emerging roles for lysosome-based signaling in human disease
Ferguson, S. M. (2015) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2015.04.014 · Cited by 67
Nutrient sensing, signal transduction and immune responses
Walls, J. F., Sinclair, L. V., & Finlay, D. K. (2016) · Seminars in Immunology · doi:10.1016/j.smim.2016.09.001 · Cited by 69
PQLC2 recruits the C9orf72 complex to lysosomes in response to cationic amino acid starvation
Amick, J., Tharkeshwar, A. K., Talaia, G., & Ferguson, S. M. (2019) · The Journal of Cell Biology · doi:10.1083/jcb.201906076 · Cited by 68
Branched-Chain Aminotransferases Control TORC1 Signaling in Saccharomyces cerevisiae
Kingsbury, J. M., Sen, N. D., & Cardenas, M. E. (2015) · PLoS Genetics · doi:10.1371/journal.pgen.1005714 · Cited by 70
PAT4 levels control amino-acid sensitivity of rapamycin-resistant mTORC1 from the Golgi and affect clinical outcome in colorectal cancer
Fan, S.-J., Snell, C. E., Turley, H., Li, J., McCormick, R. D., Perera, S., Heublein, S., Kazi, S., Azad, A. K., WILSON, C. G., et al. (2015) · Oncogene · doi:10.1038/onc.2015.363 · Cited by 69
Dipeptide species regulate p38MAPK–Smad3 signalling to maintain chronic myelogenous leukaemia stem cells
Naka, K., Jomen, Y., Ishihara, K., Kim, J., Ishimoto, T., Bae, E., Mohney, R. P., Stirdivant, S. M., Oshima, H., Oshima, M., et al. (2015) · Nature Communications · doi:10.1038/ncomms9039 · Cited by 64
Membrane-anchored ubiquitin ligase complex is required for the turnover of lysosomal membrane proteins
Li, M., Koshi, T., & Emr, S. D. (2015) · The Journal of Cell Biology · doi:10.1083/jcb.201505062 · Cited by 65
The Complex Roles of Mechanistic Target of Rapamycin in Adipocytes and Beyond
Lee, P. L., Jung, S. M., & Guertin, D. A. (2017) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2017.01.004 · Cited by 66
Lysosomal Regulation of mTORC1 by Amino Acids in Mammalian Cells
Yao, Y., Jones, E. Y., & Inoki, K. (2017) · Biomolecules · doi:10.3390/biom7030051 · Cited by 69
Dynamic Regulation of Long-Chain Fatty Acid Oxidation by a Noncanonical Interaction between the MCL-1 BH3 Helix and VLCAD
Escudero, S., Zaganjor, E., Lee, S., Mill, C. P., Morgan, A. M., Crawford, E. B., Chen, J., Wales, T. E., Mourtada, R., Luccarelli, J., et al. (2018) · Molecular Cell · doi:10.1016/j.molcel.2018.02.005 · Cited by 67
Angiotensin II blockade: how its molecular targets may signal to mitochondria and slow aging. Coincidences with calorie restriction and mTOR inhibition
de Cavanagh, E. M. V., Inserra, F., & Ferder, L. (2015) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00459.2014 · Cited by 66
Novel insights into the transport mechanism of the human amino acid transporter LAT1 (SLC7A5). Probing critical residues for substrate translocation
Napolitano, L., Galluccio, M., Scalise, M., Parravicini, C., Palazzolo, L., Eberini, I., & Indiveri, C. (2017) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2017.01.013 · Cited by 63
Self-citation
Crystal structure of arginine-bound lysosomal transporter SLC38A9 in the cytosol-open state
Lei, H., Ma, J., Martinez, S. S., & Gonen, T. (2018) · Nature Structural & Molecular Biology · doi:10.1038/s41594-018-0072-2 · Cited by 63
Anti-Rheumatic Properties of Gentiopicroside Are Associated With Suppression of ROS-NF-κB-NLRP3 Axis in Fibroblast-Like Synoviocytes and NF-κB Pathway in Adjuvant-Induced Arthritis
Wang, M., Li, H., Wang, Y., Hao, Y., Huang, Y., Wang, X., Lu, Y., Du, Y., Fu, F., Xin, W., et al. (2020) · Frontiers in Pharmacology · doi:10.3389/fphar.2020.00515 · Cited by 63
Mitochondrial Threonyl-tRNA Synthetase TARS2 Is Required for Threonine-Sensitive mTORC1 Activation
Kim, S.-H., Choi, J.-H., Wang, P., Go, C. D., Hesketh, G. G., Gingras, A.-C., Jafarnejad, S. M., & Sonenberg, N. (2021) · Molecular Cell · doi:10.1016/j.molcel.2020.11.036 · Cited by 62
The complex network of mTOR signalling in the heart
Sciarretta, S., Forte, M., Frati, G., & Sadoshima, J. (2021) · Cardiovascular Research · doi:10.1093/cvr/cvab033 · Cited by 68
Sensing Gram-negative bacteria: a phylogenetic perspective
Neyen, C. D., & Lemaître, B. (2015) · Current Opinion in Immunology · doi:10.1016/j.coi.2015.10.007 · Cited by 61
Metabolic control of signalling pathways and metabolic auto‐regulation
Lorendeau, D., Christen, S., Rinaldi, G., & Fendt, S. (2015) · Biology of the Cell · doi:10.1111/boc.201500015 · Cited by 60
Altered mTOR signalling in nephropathic cystinosis
Ivanova, E. A., van den Heuvel, L. P., Elmonem, M. A., SMEDT, H. D., Missiaen, L., Pastore, A., Mekahli, D., Bultynck, G., & Levtchenko, E. N. (2016) · Journal of Inherited Metabolic Disease · doi:10.1007/s10545-016-9919-z · Cited by 60
Autophagosome Biogenesis Machinery
Walker, S. A., & Ktistakis, N. T. (2019) · Journal of Molecular Biology · doi:10.1016/j.jmb.2019.10.027 · Cited by 64
Role of autophagy in muscle disease
Franco‐Romero, A., & Sandri, M. (2021) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2021.101041 · Cited by 65
Genetic linkage of distinct adaptive traits in sympatrically speciating crater lake cichlid fish
Fruciano, C., Franchini, P., Kováčová, V., Elmer, K. R., Henning, F., & Meyer, A. (2016) · Nature Communications · doi:10.1038/ncomms12736 · Cited by 56
Rag GTPase in amino acid signaling
Kim, J., & Kim, E. (2016) · Amino Acids · doi:10.1007/s00726-016-2171-x · Cited by 65
mTORC1 Activation Requires DRAM-1 by Facilitating Lysosomal Amino Acid Efflux
Beaumatin, F., O’Prey, J., Barthet, V. J. A., Zunino, B., Parvy, J.-P., Bachmann, A., O’Prey, M., Kania, E., Gonzalez, P. S., Macintosh, R. L., et al. (2019) · Molecular Cell · doi:10.1016/j.molcel.2019.07.021 · Cited by 60
Causes and consequences of DNA damage-induced autophagy
Juretschke, T., & Beli, P. (2021) · Matrix Biology · doi:10.1016/j.matbio.2021.02.004 · Cited by 59
The role of endolysosomal trafficking in anticancer drug resistance
Hussein, N. A., Malla, S., Pasternak, M. A., Terrero, D., Brown, N. G., Ashby, C. R., Assaraf, Y. G., Chen, Z., & Tiwari, A. K. (2021) · Drug Resistance Updates · doi:10.1016/j.drup.2021.100769 · Cited by 58
Structural mechanism for the arginine sensing and regulation of CASTOR1 in the mTORC1 signaling pathway
Gai, Z., Wang, Q., Yang, C., Wang, L., Deng, W., & Wu, G. (2016) · Cell Discovery · doi:10.1038/celldisc.2016.51 · Cited by 58
Amino Acid Transporter SLC6A14 (ATB0,+) – A Target in Combined Anti-cancer Therapy
Nałęcz, K. A. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.594464 · Cited by 59
Glutamine metabolism in Th17/Treg cell fate: applications in Th17 cell-associated diseases
Yang, G., Xia, Y., & Ren, W. (2020) · Science China Life Sciences · doi:10.1007/s11427-020-1703-2 · Cited by 55
Is REDD1 a Metabolic Éminence Grise ?
Lipina, C., & Hundal, H. S. (2016) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2016.08.005 · Cited by 60
Endomembrane Tension and Trafficking
Sarić, A., & Freeman, S. A. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.611326 · Cited by 56
Next Generation Strategies for Geroprotection via mTORC1 Inhibition
Dumas, S. N., & Lamming, D. W. (2019) · The Journals of Gerontology Series A · doi:10.1093/gerona/glz056 · Cited by 53
The lysosomal GPCR-like protein GPR137B regulates Rag and mTORC1 localization and activity
Gan, L., Seki, A., Shen, K., Iyer, H., Han, K., Hayer, A., Wollman, R., Ge, X., Lin, J. R., Dey, G., et al. (2019) · Nature Cell Biology · doi:10.1038/s41556-019-0321-6 · Cited by 53
The Ion Transporter NKCC1 Links Cell Volume to Cell Mass Regulation by Suppressing mTORC1
Demian, W. L., Persaud, A. K., Jiang, C., Coyaud, É., Liu, S., Kapùs, A., Kafri, R., Raught, B., & Rotin, D. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.04.034 · Cited by 54
Cyst(e)ine in nutrition formulation promotes colon cancer growth and chemoresistance by activating mTORC1 and scavenging ROS
Wu, J., Yeung, S. J., Liu, S., Qdaisat, A. Z., Jiang, D., Liu, W., Cheng, Z., Liu, W., Wang, H., Li, L., et al. (2021) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-021-00581-9 · Cited by 53
Indole-3-acetic acid is a physiological inhibitor of TORC1 in yeast
Nicastro, R., Raucci, S., Michel, A. H., Stumpe, M., Osuna, G. M. G., Jaquenoud, M., Kornmann, B., & VIRGILIO, C. D. (2021) · PLoS Genetics · doi:10.1371/journal.pgen.1009414 · Cited by 53
SLC15A4 controls endolysosomal TLR7–9 responses by recruiting the innate immune adaptor TASL
Zhang, H., Bernaleau, L., Delacrétaz, M., Hasanovic, E., Drobek, A., Eibel, H., & Rebsamen, M. (2023) · Cell Reports · doi:10.1016/j.celrep.2023.112916 · Cited by 54
Self-citation
Lysosome-Mitochondrial Crosstalk in Cellular Stress and Disease
Kiraly, S., Stanley, J., & Eden, E. R. (2025) · Antioxidants · doi:10.3390/antiox14020125 · Cited by 58
The amino acid transporter SLC36A4 regulates the amino acid pool in retinal pigmented epithelial cells and mediates the mechanistic target of rapamycin, complex 1 signaling
Shang, P., Valapala, M., Grebe, R. R., Hose, S., Ghosh, S., Bhutto, I. A., Handa, J. T., Lutty, G. A., Lü, L., Wan, J., et al. (2017) · Aging Cell · doi:10.1111/acel.12561 · Cited by 52
Versatility of microglial bioenergetic machinery under starving conditions
Nagy, Á., Fekete, R., Horváth, G., Koncsos, G., Kriston, C., Sebestyén, A. R., Giricz, Z., Környei, Z., Madarász, E., & Tretter, L. (2017) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2017.12.002 · Cited by 53
Amino acids and amino acid sensing: implication for aging and diseases
Dato, S., Hoxha, E., Crocco, P., Iannone, F., Passarino, G., & Rose, G. (2018) · Biogerontology · doi:10.1007/s10522-018-9770-8 · Cited by 52
A Compendium of Information on the Lysosome
Bouhamdani, N., Comeau, D., & Turcotte, S. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.798262 · Cited by 55
Dormant spores sense amino acids through the B subunits of their germination receptors
Artzi, L., Alon, A., Brock, K. P., Green, A. G., Tam, A., Ramírez‐Guadiana, F. H., Marks, D. S., Kruse, A. C., & Rudner, D. Z. (2021) · Nature Communications · doi:10.1038/s41467-021-27235-2 · Cited by 51
Getting Nervous: An Evolutionary Overhaul for Communication
Varoqueaux, F., & Fasshauer, D. (2017) · Annual Review of Genetics · doi:10.1146/annurev-genet-120116-024648 · Cited by 47
Glutamine transporters as pharmacological targets: From function to drug design
Scalise, M., Pochini, L., Galluccio, M., Console, L., & Indiveri, C. (2020) · Asian Journal of Pharmaceutical Sciences · doi:10.1016/j.ajps.2020.02.005 · Cited by 52
Self-citation
The human LAT1–4F2hc (SLC7A5–SLC3A2) transporter complex: Physiological and pathophysiological implications
Kahlhofer, J., & Teis, D. (2022) · Basic & Clinical Pharmacology & Toxicology · doi:10.1111/bcpt.13821 · Cited by 51
Regulation of mTORC1 by the Rag GTPases
Lama-Sherpa, T. D., Jeong, M., & Jewell, J. L. (2023) · Biochemical Society Transactions · doi:10.1042/bst20210038 · Cited by 52
Cysteine is not a substrate but a specific modulator of human ASCT2 (SLC1A5) transporter
Scalise, M., Pochini, L., Pingitore, P., Hedfalk, K., & Indiveri, C. (2015) · FEBS Letters · doi:10.1016/j.febslet.2015.10.011 · Cited by 51
Self-citation
Emerging roles of the solute carrier family in pancreatic cancer
Wu, Z., Xu, J., Chen, L., Meng, Q., Hua, J., Wang, W., Zhang, B., Liu, J., Yu, X., & Shi, S. (2021) · Clinical and Translational Medicine · doi:10.1002/ctm2.356 · Cited by 47
Transposable element insertions in fission yeast drive adaptation to environmental stressPreprint
Esnault, C., Lee, M., Ham, C., & Levin, H. L. (2018) · Genome Research · doi:10.1101/gr.239699.118 · Cited by 46
PRMT1 orchestrates with SAMTOR to govern mTORC1 methionine sensing via Arg-methylation of NPRL2
Jiang, C., Liu, J., He, S., Xu, W., Huang, R., Pan, W., Li, X., Dai, X., Guo, J., Zhang, T., et al. (2023) · Cell Metabolism · doi:10.1016/j.cmet.2023.11.001 · Cited by 49
The Lysosome and Intracellular Signalling
Hesketh, G. G., Wartosch, L., Davis, L. J., Bright, N. A., & Luzio, J. P. (2018) · Progress in molecular and subcellular biology · doi:10.1007/978-3-319-96704-2_6 · Cited by 47
Macropinosomes as units of signal transduction
Swanson, J. A., & Yoshida, S. (2018) · Philosophical Transactions of the Royal Society B Biological Sciences · doi:10.1098/rstb.2018.0157 · Cited by 47
Conserved and Divergent Mechanisms That Control TORC1 in Yeasts and Mammals
Morozumi, Y., & Shiozaki, K. (2021) · Genes · doi:10.3390/genes12010088 · Cited by 44
Mitochondrial hyperfusion via metabolic sensing of regulatory amino acids
Abdullah, M. O., Zeng, R. X., Margerum, C. L., Papadopoli, D. J., Monnin, C., Punter, K. B., Chu, C., Al-Rofaidi, M., Al‐Tannak, N. F., Berardi, D., et al. (2022) · Cell Reports · doi:10.1016/j.celrep.2022.111198 · Cited by 46
Targeting cancer-specific metabolic pathways for developing novel cancer therapeutics
Pal, S., Sharma, A. K., Mathew, S. P., & Jaganathan, B. G. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.955476 · Cited by 50
Vacuolar ATPase in phago(lyso)some biology
Kissing, S., Säftig, P., & Haas, A. (2017) · International Journal of Medical Microbiology · doi:10.1016/j.ijmm.2017.08.007 · Cited by 48
Biogenesis of lysosome‐related organelles complex‐1 (BORC) regulates late endosomal/lysosomal size through PIKfyve‐dependent phosphatidylinositol‐3,5‐bisphosphate
Yordanov, T. E., Hipolito, V. E. B., Liebscher, G., Vogel, G. F., Stasyk, T., Herrmann, C., Geley, S., Teis, D., Botelho, R. J., Hess, M. W., et al. (2019) · Traffic · doi:10.1111/tra.12679 · Cited by 46
Self-citation
SLC36A1-mTORC1 signaling drives acquired resistance to CDK4/6 inhibitors
Yoshida, A., Bu, Y., Qie, S., Wrangle, J. M., Camp, E. R., Hazard, E. S., Hardiman, G., de Leeuw, R., Knudsen, K. E., & Diehl, J. A. (2019) · Science Advances · doi:10.1126/sciadv.aax6352 · Cited by 46
A DNA nanodevice for mapping sodium at single-organelle resolution
Zou, J., Mitra, K., Anees, P., Oettinger, D., Ramirez, J. R., Veetil, A. T., Gupta, P., Rao, R., Smith, J. J., Kratsios, P., et al. (2023) · Nature Biotechnology · doi:10.1038/s41587-023-01950-1 · Cited by 48
Ultrastructural Morphometry Points to a New Role for LAMTOR2 in Regulating the Endo/Lysosomal System
Vogel, G. F., Ebner, H. L., de Araújo, M. E. G., Schmiedinger, T., Eiter, O., Pircher, H., Gutleben, K., Witting, B., Teis, D., Huber, L. A., et al. (2015) · Traffic · doi:10.1111/tra.12271 · Cited by 46
Self-citation
On the structure and mechanism of two‐pore channels
Kintzer, A. F., & Stroud, R. M. (2017) · FEBS Journal · doi:10.1111/febs.14154 · Cited by 45
Targeting the mTOR Signaling Pathway Utilizing Nanoparticles: A Critical Overview
Lunová, M., Smolková, B., Lynnyk, A., Uzhytchak, M., Jirsa, M., Kubinová, Š., Dejneka, A., & Lunov, O. (2019) · Cancers · doi:10.3390/cancers11010082 · Cited by 47
Harnessing Solute Carrier Transporters for Precision Oncology
Nyquist, M. D., Prasad, B., & Mostaghel, E. A. (2017) · Molecules · doi:10.3390/molecules22040539 · Cited by 44
Multiple Transceptors for Macro- and Micro-Nutrients Control Diverse Cellular Properties Through the PKA Pathway in Yeast: A Paradigm for the Rapidly Expanding World of Eukaryotic Nutrient Transceptors Up to Those in Human Cells
Steyfkens, F., Zhang, Z., Zeebroeck, G. V., & Thevelein, J. M. (2018) · Frontiers in Pharmacology · doi:10.3389/fphar.2018.00191 · Cited by 48
Amino acid response by Halofuginone in Cancer cells triggers autophagy through proteasome degradation of mTOR
Follo, C., Vidoni, C., Morani, F., Ferraresi, A., Seca, C., & Isidoro, C. (2019) · Cell Communication and Signaling · doi:10.1186/s12964-019-0354-2 · Cited by 45
The metabolic regulator Lamtor5 suppresses inflammatory signaling via regulating mTOR-mediated TLR4 degradation
Zhang, W. K., Zhuang, N., Liu, X., He, L., He, Y., Mahinthichaichan, P., Zhang, H., Kang, Y., Lu, Y., Wu, Q., et al. (2019) · Cellular and Molecular Immunology · doi:10.1038/s41423-019-0281-6 · Cited by 45
Membrane Transporters for Amino Acids as Players of Cancer Metabolic Rewiring
Scalise, M., Console, L., Rovella, F., Galluccio, M., Pochini, L., & Indiveri, C. (2020) · Cells · doi:10.3390/cells9092028 · Cited by 45
Self-citation
Mechanistic Target of Rapamycin Complex 1: From a Nutrient Sensor to a Key Regulator of Metabolism and Health
Wang, G., Chen, L., Qin, S., Zhang, T., Yao, J., Yi, Y., & Deng, L. (2022) · Advances in Nutrition · doi:10.1093/advances/nmac055 · Cited by 45
The Central Role of mTORC1 in Amino Acid Sensing
Yue, S., Li, G., He, S., & Li, T. (2022) · Cancer Research · doi:10.1158/0008-5472.can-21-4403 · Cited by 45
Increasing the availability of threonine, isoleucine, valine, and leucine relative to lysine while maintaining an ideal ratio of lysine:methionine alters mammary cellular metabolites, mammalian target of rapamycin signaling, and gene transcription
Dong, X., Zhou, Z., Wang, L.-Y., Saremi, B., Helmbrecht, A., Wang, Z., & Loor, J. J. (2018) · Journal of Dairy Science · doi:10.3168/jds.2017-13707 · Cited by 43
Resolution of macropinosomes, phagosomes and autolysosomes: Osmotically driven shrinkage enables tubulation and vesiculation
Freeman, S. A., & Grinstein, S. (2018) · Traffic · doi:10.1111/tra.12614 · Cited by 48
PP2A-dependent TFEB activation is blocked by PIKfyve-induced mTORC1 activity
Hasegawa, J., Tokuda, E. Y., Yao, Y., Sasaki, T., Inoki, K., & Weisman, L. S. (2022) · Molecular Biology of the Cell · doi:10.1091/mbc.e21-06-0309 · Cited by 43
Low‐level lysosomal membrane permeabilization for limited release and sublethal functions of cathepsin proteases in the cytosol and nucleus
Reinheckel, T., & Tholen, M. (2022) · FEBS Open Bio · doi:10.1002/2211-5463.13385 · Cited by 46
Structural basis for FLCN RagC GAP activation in MiT-TFE substrate-selective mTORC1 regulation
Jansen, R. M., Peruzzo, R., Fromm, S. A., Yokom, A. L., Zoncu, R., & Hurley, J. H. (2022) · Science Advances · doi:10.1126/sciadv.add2926 · Cited by 42
Detection of Chemical Engagement of Solute Carrier Proteins by a Cellular Thermal Shift Assay
Hashimoto, M., Girardi, E., Eichner, R., & Superti‐Furga, G. (2018) · ACS Chemical Biology · doi:10.1021/acschembio.8b00270 · Cited by 43
Self-citation
Targeting fuel pocket of cancer cell metabolism: A focus on glutaminolysis
Sharma, S., Agnihotri, N., & Kumar, S. (2022) · Biochemical Pharmacology · doi:10.1016/j.bcp.2022.114943 · Cited by 42
Making sense of amino acid sensing
Abraham, R. T. (2015) · Science · doi:10.1126/science.aaa4570 · Cited by 42
Amino acids-Rab1A-mTORC1 signaling controls whole-body glucose homeostasis
Zhang, X., Wang, X., Yuan, Z., Radford, S. J., Liu, C., Libutti, S. K., & Zheng, X. F. S. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.108830 · Cited by 41
Functional Amino Acids and Autophagy: Diverse Signal Transduction and Application
Liu, C., Ji, L., Hu, J., Zhao, Y., Johnston, L. J., Zhang, X., & Ma, X. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms222111427 · Cited by 44
Lysosomes at the Crossroads of Cell Metabolism, Cell Cycle, and Stemness
Nowosad, A., & Besson, A. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23042290 · Cited by 39
Targeting mTOR for the treatment of B cell malignancies
Lee, J. S., Vo, T.-T. T., & Fruman, D. A. (2016) · British Journal of Clinical Pharmacology · doi:10.1111/bcp.12888 · Cited by 39
Src regulates amino acid-mediated mTORC1 activation by disrupting GATOR1-Rag GTPase interaction
Pal, R., Palmieri, M., Chaudhury, A., Klisch, T. J., di Ronza, A., Neilson, J. R., Rodney, G. G., & Sardiello, M. (2018) · Nature Communications · doi:10.1038/s41467-018-06844-4 · Cited by 40
mTOR Signaling Pathway and Gut Microbiota in Various Disorders: Mechanisms and Potential Drugs in Pharmacotherapy
Gao, Y., & Tian, T. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241411811 · Cited by 39
Heterogeneity of late endosome/lysosomes shown by multiplexed DNA-PAINT imaging
Bond, C., Hugelier, S., Xing, J., Sorokina, E. M., & Lakadamyali, M. (2024) · The Journal of Cell Biology · doi:10.1083/jcb.202403116 · Cited by 43
Targeting P-glycoprotein function, p53 and energy metabolism: Combination of metformin and 2-deoxyglucose reverses the multidrug resistance of MCF-7/Dox cells to doxorubicin
Xue, C., Wang, C., Sun, Y., Meng, Q., Liu, Z., Huo, X., Sun, P., Sun, H., Ma, X., Ma, X., et al. (2016) · Oncotarget · doi:10.18632/oncotarget.14373 · Cited by 39
Exploiting cancer vulnerabilities: mTOR, autophagy, and homeostatic imbalance
Johnson, C. E., & Tee, A. R. (2017) · Essays in Biochemistry · doi:10.1042/ebc20170056 · Cited by 40
Sensors for the mTORC1 pathway regulated by amino acids
Li, X.-Z., & Yan, X. (2019) · Journal of Zhejiang University SCIENCE B · doi:10.1631/jzus.b1900181 · Cited by 41
Structural insight into the arginine-binding specificity of CASTOR1 in amino acid-dependent mTORC1 signaling
Xia, J., Wang, R., Zhang, T., & Ding, J. (2016) · Cell Discovery · doi:10.1038/celldisc.2016.35 · Cited by 38
Lysosomal Functions in Glia Associated with Neurodegeneration
Kreher, C., Favret, J., Maulik, M., & Shin, D. (2021) · Biomolecules · doi:10.3390/biom11030400 · Cited by 38
A conformational change in the N terminus of SLC38A9 signals mTORC1 activation
Lei, H., Mu, X., Hattne, J., & Gonen, T. (2020) · Structure · doi:10.1016/j.str.2020.11.014 · Cited by 40
Mechanistic Target of Rapamycin Is a Novel Molecular Mechanism Linking Folate Availability and Cell Function
Silva, E., Rosario, F. J., Powell, T. L., & Jansson, T. (2017) · Journal of Nutrition · doi:10.3945/jn.117.248823 · Cited by 39
Dietary protein considerations for muscle protein synthesis and muscle mass preservation in older adults
Olaniyan, E. T., O’Halloran, F., & McCarthy, A. L. (2020) · Nutrition Research Reviews · doi:10.1017/s0954422420000219 · Cited by 39
Elucidating the underlying mechanism of amino acids to regulate muscle protein synthesis: Effect on human health
Lv, X., Zhou, C., Yan, Q., Tan, Z., Kang, J., & Tang, S. (2022) · Nutrition · doi:10.1016/j.nut.2022.111797 · Cited by 41
A virulence factor as a therapeutic: the probiotic Enterococcus faecium SF68 arginine deiminase inhibits innate immune signaling pathways
Ghazisaeedi, F., Meens, J., Hansche, B. F., Maurischat, S., Schwerk, P., Goethe, R., Wieler, L. H., Fulde, M., & Tedin, K. (2022) · Gut Microbes · doi:10.1080/19490976.2022.2106105 · Cited by 40
Amino acid sensing and lysosomal signaling complexes
Cui, Z., Joiner, A. M. N., Jansen, R. M., & Hurley, J. H. (2023) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2023.102544 · Cited by 36
Membrane transporters in cell physiology, cancer metabolism and drug response
Alam, S., Doherty, E., Ortega-Prieto, P., Arizanova, J., & Fets, L. (2023) · Disease Models & Mechanisms · doi:10.1242/dmm.050404 · Cited by 44
Organelle proteomic profiling reveals lysosomal heterogeneity in association with longevity
Yu, Y., Gao, S. M., Guan, Y., Hu, P.-W., Zhang, Q., Liu, J., Jing, B., Zhao, Q., Sabatini, D. M., Abu-Remaileh, M., et al. (2024) · eLife · doi:10.7554/elife.85214 · Cited by 37
Survival strategies of cancer cells: the role of macropinocytosis in nutrient acquisition, metabolic reprogramming, and therapeutic targeting
Xu, G., Zhang, Q., Cheng, R., Qu, J., & Li, W. (2025) · Autophagy · doi:10.1080/15548627.2025.2452149 · Cited by 41
microRNA regulation in an ancient obligate endosymbiosis
Feng, H., Wang, L., Wuchty, S., & Wilson, A. C. C. (2017) · Molecular Ecology · doi:10.1111/mec.14464 · Cited by 37

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

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

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

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Self-check

Citations

Cites

Cited by

Related

Metadata

Record

About these checks