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

Show all 40 references

Sorted by citations

Items 501–600 of 672

mTOR: A possible therapeutic target against SARS-CoV-2 infection.
Khan, N. (2021) · PubMed · Cited by 6
Phosphoproteomics Analysis Reveals a Pivotal Mechanism Related to Amino Acid Signals in Goat Fetal Fibroblast
Xu, Z., Huimin, S., Wang, L., Yao, R., Ma, Y., Bai, L., Wang, Y., Guo, X., & Wang, Z. (2021) · Frontiers in Veterinary Science · doi:10.3389/fvets.2021.685548 · Cited by 6
Broad Anti-Cancer Activity Produced by Targeted Nutrients Deprivation (TND) of Multiple Non-Essential Amino Acids
Li, Z., Zhou, S. Y., Yang, X., Li, X., Yang, G. X., Chant, J., Snyder, M. P., & Wang, X. (2021) · Nutrition and Cancer · doi:10.1080/01635581.2021.2013904 · Cited by 6
Nutrient Digestion, Absorption, and Sensing
Bishu, S., & Quigley, E. M. M. (2015) · Wiley eBooks · doi:10.1002/9781118512074.ch29 · Cited by 6
Mitochondrial respiration supports cancer growth independent of OXPHOS
Chinopoulos, C. (2026) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2026.189593 · Cited by 5
The antiport mechanism of the human LAT1 transporter: defining the molecular determinants by means of wet and dry approaches
Scalise, M., Scanga, R., Console, L., Galluccio, M., & Indiveri, C. (2025) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2025.152277 · Cited by 5
Self-citation
Single-Locus and Multi-Locus Genome-Wide Association Studies Identify Genes Associated with Liver Cu Concentration in Merinoland Sheep
Adeniyi, O. O., Međugorac, I., Grochowska, E., Düring, R., & Lühken, G. (2023) · Genes · doi:10.3390/genes14051053 · Cited by 5
Conceptualizing Eukaryotic Metabolic Sensing and Signaling
Laxman, S. (2017) · Journal of the Indian Institute of Science · doi:10.1007/s41745-016-0013-1 · Cited by 5
CG4928 Is Vital for Renal Function in Fruit Flies and Membrane Potential in Cells: A First In-Depth Characterization of the Putative Solute Carrier UNC93A
Ceder, M. M., Aggarwal, T., Hosseini, K., Maturi, V., Patil, S., Perland, E., Williams, M. J., & Fredriksson, R. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.580291 · Cited by 5
A unified model of amino acid homeostasis in mammalian cellsPreprint
Gauthier-Coles, G., Vennitti, J., Zhang, Z., Comb, W. C., Javed, K., Bröer, A., & Bröer, S. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.02.08.430327 · Cited by 5
Multiplexed DNA-PAINT Imaging of the Heterogeneity of Late Endosome/Lysosome Protein CompositionPreprint
Bond, C., Hugelier, S., Xing, J., Sorokina, E. M., & Lakadamyali, M. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.03.18.585634 · Cited by 5
Amino Acid Metabolism and Autophagy in Atherosclerotic Cardiovascular Disease
Wu, Y., Avcilar-Kücükgöze, I., Santovito, D., & Atzler, D. (2024) · Biomolecules · doi:10.3390/biom14121557 · Cited by 5
SLC38A9 is directly involved in Tat-induced endolysosome dysfunction and senescence in astrocytes
Rezagholizadeh, N., Datta, G., Hasler, W. A., Nguon, E. C., Smokey, E. V., Khan, N., & Chen, X. (2025) · Life Science Alliance · doi:10.26508/lsa.202503231 · Cited by 5
Irisin-mediated hepatic autophagy remodels nutritional metabolism to prevent cognitive dysfunction
Zhang, X., Yang, Y., Song, H., Hu, X., Wang, X., & Yu, Y. (2025) · Ageing Research Reviews · doi:10.1016/j.arr.2025.102936 · Cited by 4
The rapamycin sTORy: 50-year journey from Easter Island to the frontiers of biology and medicine
Xiao, X., & Dokudovskaya, S. (2026) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2026.02.004 · Cited by 4
Intermittent Bolus Compared With Continuous Feeding Enhances Insulin and Amino Acid Signaling to Translation Initiation in Skeletal Muscle of Neonatal Pigs
Suryawan, A., El‐Kadi, S. W., Nguyen, H. V., Fiorotto, M. L., & Davis, T. A. (2021) · Journal of Nutrition · doi:10.1093/jn/nxab190 · Cited by 4
Exploring biomarkers for autophagy‐mediated macrophage pyroptosis in atherosclerosis
Yang, R., Wang, D., Ding, Y., & Liu, Q. (2023) · Cell Biology International · doi:10.1002/cbin.12080 · Cited by 4
Inhibition of the mTORC1/NF‐κB Axis Alters Amino Acid Metabolism in Human Hepatocytes
Zhang, M., Fu, Y., Chen, Y., Ma, Y., Guo, Z., Wang, Y., Hao, H., Fu, Q., & Wang, Z. (2021) · BioMed Research International · doi:10.1155/2021/8621464 · Cited by 4
Picking the arginine lock on PQLC2 cycling
Jain, A., & Zoncu, R. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2112682118 · Cited by 4
Rapamycin and rapalogs
Lamming, D. W. (2023) · Elsevier eBooks · doi:10.1016/b978-0-12-823679-6.00002-3 · Cited by 4
A novel 5q11.2 microdeletion in a child with mild developmental delay and dysmorphic features
Fontana, P., Tortora, C., Petillo, R., Falco, M., Miniero, M., Brasi, D. D., & Pisanti, M. A. (2016) · American Journal of Medical Genetics Part A · doi:10.1002/ajmg.a.37824 · Cited by 4
New insights into MTORC1 amino acid sensing and activation
Gatica, D., & Klionsky, D. J. (2017) · Biotarget · doi:10.21037/biotarget.2017.04.01 · Cited by 4
The regulatory role and mechanism of energy metabolism and immune response in head and neck cancer
Li, H., Qiu, P., Oyang, L., Yang, W., Li, S., Han, Y., Peng, M., Tan, S., Xia, L., Lin, J., et al. (2025) · Genes & Diseases · doi:10.1016/j.gendis.2025.101607 · Cited by 3
Soybean Cyst Nematode‐Resistant Protein AATRhg1 Affects Amino Acid Homeostasis and Betalain Accumulation
Du, Y., Jung, S., Maeda, H. A., & Bent, A. F. (2025) · Plant Direct · doi:10.1002/pld3.70098 · Cited by 3
Analysis of the Stimulative Effect of Arginine on Translation Initiation of Protein Synthesis in Skeletal Muscle
Suzuki, D., Takami, Y., Sato, Y., Toyoshima, Y., & Yoshizawa, F. (2025) · Nutrients · doi:10.3390/nu17182981 · Cited by 3
The Role of Mammalian Target of Rapamycin (mTOR) and Adenosine Monophosphate-Activated Protein Kinase (AMPK) Signaling in Skeletal Muscle Hypertrophy: A Literature Review With Implications for Health and Disease
Jeong, S. Y. (2025) · Cureus · doi:10.7759/cureus.96018 · Cited by 5
Angel or demon? The dual role of branched-chain amino acids in chronic inflammatory and injury-related diseases
Li, J., Chen, H., Zhou, Y., Sun, L., Xing, Y., Sun, Y., Yang, Y., & Shi, Y. (2026) · Frontiers in Immunology · doi:10.3389/fimmu.2026.1778455 · Cited by 3
Production of the recombinant human riboflavin transporters SLC52A1, 3 and functional assay in proteoliposomes
Console, L., Tolomeo, M., Travo, L., Giudice, D., Nisco, A. D., Barile, M., & Indiveri, C. (2025) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2025.110327 · Cited by 3
Self-citation
Nutrient sensing receptor GPRC6A regulates mTORC1 signaling and Tau biology
Ma, C., Campbell, K., Kovalenko, A., Li, J., Sandusky‐Beltran, L. A., Liang, H., Hunt, J. B., Calahatian, J. I. T., Kallupurackal, M., Pandey, S., et al. (2025) · Neurobiology of Disease · doi:10.1016/j.nbd.2025.107054 · Cited by 3
Genetic dissection of Ragulator structure and function in amino acid-dependent regulation of mTORC1.
Nada, S., & Okada, M. (2020) · Journal of Biochemistry (Tokyo) · doi:10.1093/jb/mvaa076 · Cited by 2
Functional Study of the Human Riboflavin Transporter 2 Using Proteoliposomes System
Console, L., Tolomeo, M., & Indiveri, C. (2021) · Methods in molecular biology · doi:10.1007/978-1-0716-1286-6_4 · Cited by 3
Self-citation
The fission yeast FLCN/FNIP complex augments TORC1 repression or activation in response to amino acid (AA) availability
Calvo, I. A., Sharma, S., Paulo, J. A., Gulka, A. O. D., Boeszoermenyi, A., Zhang, J., Lombana, J. M., Palmieri, C. M., Laviolette, L. A., Arthanari, H., et al. (2021) · iScience · doi:10.1016/j.isci.2021.103338 · Cited by 3
Influence of Mechanistic Target of Rapamycin (mTOR)-Regulated Anabolic Pathways on Equine Skeletal Muscle Health
Semanchik, P. L., Wesolowski, L. T., Ryan, P. J., White-Springer, S. H., & Fluckey, J. D. (2023) · Journal of Equine Veterinary Science · doi:10.1016/j.jevs.2023.104281 · Cited by 3
S100A9 Affects Milk Protein Content by Regulating Amino Acid Transporters and the PI3K-Akt, WNT, and mTOR Signaling Pathways
Zhang, X., Teng, J., Chen, Z., Zhao, P., Jiang, L., & Zhang, Q. (2024) · Genes · doi:10.3390/genes15111486 · Cited by 3
SLC38A10 Deficiency in Mice Affects Plasma Levels of Threonine and Histidine in Males but Not in Females: A Preliminary Characterization Study of SLC38A10−/− Mice
Lindberg, F. A., Nordenankar, K., Forsberg, E. C., & Fredriksson, R. (2023) · Genes · doi:10.3390/genes14040835 · Cited by 3
Stress Relief Downstream of TOR
Stocker, H. (2015) · Developmental Cell · doi:10.1016/j.devcel.2015.04.013 · Cited by 3
From glucose sensing to a unified model of AMPK and mTOR regulation
Fu, S. (2017) · 中国科学通报：英文版 · doi:10.1016/j.scib.2017.08.001 · Cited by 3
Investigation of LAMTOR1 gene and protein expressions in germinal vesicle and metaphase II oocytes and embryos from 1-cell to blastocyst stage in a mouse model
Gümüş, E., Sarı, İ., Yilmaz, M., & Çetin, A. (2018) · Gene Expression Patterns · doi:10.1016/j.gep.2018.03.002 · Cited by 3
Molecular Processes and Regulation of Autophagy
Nasb, M., Kirberger, M., & Chen, N. (2021) · Springer eBooks · doi:10.1007/978-981-16-4525-9_1 · Cited by 3
Purification and biochemical characterization of the Rag GTPase heterodimer
Doxsey, D. D., & Shen, K. (2022) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2022.07.007 · Cited by 4
Leishmania parasite arginine deprivation response pathway influences the host macrophage lysosomal arginine sensing machinery
Madan, E., Ganguly, N. K., Puri, M., Pawar, H., Selvapandiyan, A., Muthuswami, R., Zilberstein, D., & Madhubala, R. (2024) · Medical Research Archives · doi:10.18103/mra.v12i10.5800 · Cited by 3
Synergistic Role of Amino Acids in Enhancing mTOR Activation Through Lysosome PositioningPreprint
Kolaczkowski, O. M., Goodson, B. A., Vazquez, V. F. M., Jia, J., Bhat, A. Q., Kim, T., & Pu, J. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.10.12.618047 · Cited by 3
Reduction of Buchnera with rifampicin impairs the density‐dependent induction of winged morph in pea aphid
Yuan, E., Du, B., & Sun, Y. (2025) · Insect Science · doi:10.1111/1744-7917.70098 · Cited by 2
A small-molecule anti-cancer drug for long-acting lysosomal damage
Zhao, S., Bai, Q., Xue, G., Wang, J., Hu, L., Wang, X., Li, Y., Lü, S., Sun, Y., Zhang, Z., et al. (2025) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2025.09.005 · Cited by 2
Amino acid sensing in cancer
Lin, Z., He, L., Wang, J., Zhang, H., Yao, S., Guo, J., Zhang, X., Liang, T., & Bai, X. (2025) · Pharmacological Research · doi:10.1016/j.phrs.2025.108003 · Cited by 3
Global cellular responses to lysosomal damage
Jia, J. (2026) · Current Biology · doi:10.1016/j.cub.2026.05.050 · Cited by 2
Ygr125w/Vsb1-dependent accumulation of basic amino acids into vacuoles of Saccharomyces cerevisiae
Kawano‐Kawada, M., Ichimura, H., Ohnishi, S., Yamamoto, Y., Kawasaki, Y., & Sekito, T. (2021) · Bioscience Biotechnology and Biochemistry · doi:10.1093/bbb/zbab015 · Cited by 2
Tumor starvation by L-arginine deprivation
Fried, R., Carlton, R. M., & Fried, D. A. (2021) · Elsevier eBooks · doi:10.1016/b978-0-12-824013-7.00005-5 · Cited by 2
The exception to the rule? TORC1 triggers growth under low nutrient environments
Lopez, L. E., Pacheco, J. M., & Estevez, J. M. (2023) · Trends in Plant Science · doi:10.1016/j.tplants.2023.10.001 · Cited by 2
The deubiquitinase USP45 inhibits autophagy through actin regulation by Coronin 1B
Lin, Y. J., Huang, L., Ke, P., & Chen, G. (2025) · The Journal of Cell Biology · doi:10.1083/jcb.202407014 · Cited by 2
Glutamate Supplementation Regulates Nitrogen Metabolism in the Colon and Liver of Weaned Rats Fed a Low-Protein Diet
Jiang, D., Zhang, J., Ji, Y. S., Dai, Z., Yang, Y., & Wu, Z. (2025) · Nutrients · doi:10.3390/nu17091465 · Cited by 2
Arginine sensing in intracellular parasitism of Leishmania
Zilberstein, D., & Myler, P. J. (2021) · Current Opinion in Microbiology · doi:10.1016/j.mib.2021.09.003 · Cited by 2
Regulation of Macroautophagy by Nutrients and Metabolites
Lorin, S., Pattingre, S., Meijer, A. J., & Codogno, P. (2016) · Elsevier eBooks · doi:10.1016/b978-0-12-802167-5.00014-1 · Cited by 2
Protein Metabolism in the Elderly
Dillon, E. L. (2016) · Elsevier eBooks · doi:10.1016/b978-0-12-802167-5.00007-4 · Cited by 3
Nutrient sensing
Venugopal, A., & Bishu, S. (2021) · Current Opinion in Gastroenterology · doi:10.1097/mog.0000000000000709 · Cited by 2
Optical recordings of organellar membrane potentials and the components of membrane conductance in lysosomes
Castillo-Velásquez, C., Matamala, E., Becerra, D., Orio, P., & Brauchi, S. (2024) · The Journal of Physiology · doi:10.1113/jp283825 · Cited by 2
Surviving starvation simply without TFEB
Soukas, A. A., & Zhou, B. Z. (2019) · PLoS Biology · doi:10.1371/journal.pbio.3000285 · Cited by 3
Effect of amino acids on IGF1 gene expression in human myotubes and skeletal muscle
Lednev, E. M., Kravchenko, I. V., Furalyov, V. A., Lysenko, E. A., Лемешева, Ю. С., Grushin, A. A., Дубров, В. Э., Виноградова, О. Л., & Викторович, П. Д. (2020) · Growth Hormone & IGF Research · doi:10.1016/j.ghir.2020.101323 · Cited by 2
TFEB, Master Regulator of Cellular Clearance
Diez-Roux, G., & Ballabio, A. (2016) · doi:10.1002/9781118978320.ch7 · Cited by 1
A lipid-mTORC1 nutrient sensing pathway regulates animal development by peroxisome-derived hormonesPreprint
Li, N., Hua, B., Chen, Q., Ruan, M., Zhu, M., Shen, H., Zhang, L., & Zhu, H. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.05.15.444169 · Cited by 1
A Toxoplasma gondii putative arginine transporter localizes to the plant-like vacuolar compartment and controls parasite extracellular survival and stage differentiationPreprint
Piro, F., Masci, S., Kannan, G., Focaia, R., Schultz, T. L., Carruthers, V. B., & Cristina, M. D. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.08.31.555807 · Cited by 2
Functional Characterization of the Lysosomal Peptide/Histidine Transporter PHT1 (SLC15A4) by Solid Supported Membrane Electrophysiology (SSME)Preprint
Pujol‐Giménez, J., & Hediger, M. A. (2023) · Preprints.org · doi:10.20944/preprints202312.1302.v1 · Cited by 1
Multi-omic Analysis of Human B-cell Activation Reveals a Key Lysosomal BCAT1 Role in mTOR Hyperactivation by B-cell receptor and TLR9Preprint
Guo, R., Lim, M. Y., Shah, H., Paulo, J. A., Zhang, Y., Yang, H., Wang, L. W., Strebinger, D., Smith, N., Li, M., et al. (2024) · Research Square · doi:10.21203/rs.3.rs-4413958/v1 · Cited by 2
Sialin2 Senses Nitrate to Activate Endosomal PI3K-AKT- NOS SignalingPreprint
Li, X., Jiang, O., Cao, Z., Zhou, B., Chen, X., Feng, Y., Zhang, C., Wang, J., Zhou, J., Yan, R., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.05.04.652107 · Cited by 4
Amino acid–dependent TSC2 dephosphorylation by lysosome–PP2A regulates mTORC1 signaling transduction
Nakamura, T., Nada, S., Matsumoto, M., Othman, N. L., Kosako, H., Ikeda, K., Koshikawa, N., Masumoto, J., Sawasaki, T., Takekawa, M., et al. (2025) · Life Science Alliance · doi:10.26508/lsa.202503206 · Cited by 1
TOR signaling on membranes
Loewith, R., & Tafur, L. (2025) · FEBS Letters · doi:10.1002/1873-3468.70171 · Cited by 2
“Benign” Metastasizing Fibrous Histiocytoma Harboring PRKCD Gene Fusions With Malignant Clinical Course
Wang, C. I., Giersch, A. B. S., Lozano‐Calderón, S. A., Choy, E., Giap, F. N., Hung, Y. P., Nielsen, G. P., & Chebib, I. A. (2025) · Genes Chromosomes and Cancer · doi:10.1002/gcc.70094 · Cited by 1
Impact of fish oil-enriched high protein peptide-based formula on free fatty acid profiles and metabolomic changes in home enterally fed patients: A pilot study
Elfadil, O. M., Johnson, D. A., Pattinson, A. K., Hurt, R. T., & Mundi, M. S. (2025) · Clinical Nutrition ESPEN · doi:10.1016/j.clnesp.2025.11.155 · Cited by 1
Molecular and structural mechanisms of nutrient sensing in the mTORC1 pathway
Yang, S., Bian, T., & Zoncu, R. (2026) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2026.02.009 · Cited by 3
Dual targeting of SLC6A14 and autophagy/macropinocytosis enhances therapeutic efficacy in pancreatic ductal adenocarcinoma
Syed, M. M., Rajasekaran, D., Sennoune, S. R., Sharker, T., Sanchez, O., Jurek, M. K., Kou, L., Chen, R., Ganapathy, V., & Bhutia, Y. D. (2026) · Biochemical Journal · doi:10.1042/bcj20250155 · Cited by 2
T‐Cell Exhaustion in the Tumor Microenvironment: Subcellular Dysfunction, Pan‐Cancer Characteristics, and Therapeutic Interventions
Wang, M., Dong, W., Chen, J., Zhou, Z., Fu, S., Wu, T., Jiang, H., Wang, Z., Zhong, Z., & Zhong, Y. (2026) · Advanced Science · doi:10.1002/advs.75651 · Cited by 2
Targeting arginine metabolism overcomes chemotherapy resistance in aggressive-variant prostate cancers
Subramani, E., Pilie, P. G., Slack-Tidwell, R., Viscuse, P. V., Kuang, X., Kandasamy, T., Awad, D., Han, J. J., Huang, L., Peterson, C. B., et al. (2026) · iScience · doi:10.1016/j.isci.2026.116184 · Cited by 1
SLC15A3-mediated dipeptide metabolism confers antimetabolite resistance in lymphoma via mTORC1 activation
Yang, H., Zingaro, V. A., Boardman, K., Noronha, A., Güney, E., Xue, L., Hoigebazar, S., Liu, I., Miglani, S., Chen, S., et al. (2026) · Journal of Clinical Investigation · doi:10.1172/jci199709 · Cited by 1
Role of Amino Acid Transporters in Protein Metabolism
Taylor, P. M. (2016) · Elsevier eBooks · doi:10.1016/b978-0-12-802167-5.00005-0 · Cited by 1
Nutrient Sensors Regulating Peptides
Çakır, I., & Nillni, E. A. (2018) · Springer eBooks · doi:10.1007/978-3-319-89506-2_6 · Cited by 1
The Role of mTOR in Osteoclasts
Zirngibl, R. A., & Voronov, I. (2018) · Stem cell biology and regenerative medicine · doi:10.1007/978-3-319-98146-8_5 · Cited by 1
Bacterial over-production of the functionally active human SLC38A2 (SNAT2) exploiting the mistic tag: a cheap and fast tool for testing ligands
Galluccio, M., Tripicchio, M., Console, L., & Indiveri, C. (2024) · Molecular Biology Reports · doi:10.1007/s11033-023-08976-3 · Cited by 1
Self-citation
Assessment of genes involved in lysosomal diseases using the ClinGen Clinical Validity framework
Groopman, E., Mohan, S., Waddell, A., Wilke, M. V. M. B., Fernandez, R., Weaver, M. A., Chen, H., Liu, H., Bali, D. S., Baudet, H., et al. (2024) · Molecular Genetics and Metabolism · doi:10.1016/j.ymgme.2024.108593 · Cited by 1
Mechanistic Target of Rapamycin
McKee-Muir, O. C., & Russell, R. C. (2017) · Elsevier eBooks · doi:10.1016/b978-0-12-812146-7.00009-3 · Cited by 2
Tumorigenic effects of TLX overexpression in HEK 293T cells
Parris, T. Z., Vizlin‐Hodzic, D., Salmela, S., & Funa, K. (2019) · Cancer Reports · doi:10.1002/cnr2.1204 · Cited by 1
A New Crosslinking Assay to Study Guanine Nucleotide Binding in the Gtr Heterodimer of S. cerevisiae
Doxsey, D. D., Veinotte, K., & Shen, K. (2022) · Small GTPases · doi:10.1080/21541248.2022.2141019 · Cited by 1
PAT2 regulates autophagy through vATPase assembly and lysosomal acidification in brown adipocytesPreprint
Wang, J., Krueger, M. C., Hauck, S. M., & Ussar, S. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.01.24.918078 · Cited by 1
Anti-androgens induce Rab11a-exosome secretion in prostate cancer by suppressing amino acid-sensitive PAT4-mTORC1 signallingPreprint
McCormick, K., Sanitt, P., Fan, S., Mason, J. D., Harris, A. L., Hamdy, F. C., Verrill, C. L., Bryant, R. J., & Goberdhan, D. C. I. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.09.18.300137 · Cited by 1
Lysosomal Diseases
Cox, T. M. (2015) · Elsevier eBooks · doi:10.1016/b978-0-12-394447-4.10086-0 · Cited by 1
A Novel XACT lncRNA Transcript with Functions Transcending X-Chromosome InactivationPreprint
Zhang, P., Angles, P. H., Zhang, H., Li, T., Mulet‐Lazaro, R., van IJcken, W. F. J., Philipsen, S., Delwel, R., Gribnau, J. H., Huylebroeck, D., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.01.03.631201 · Cited by 1
Reconstructing The S. Cerevisiae Growth Control Network In Stress Conditions
Worley, J. (2015) · UA Campus Repository (The University of Arizona)
Efeitos da suplementação com glutamina e/ou do treinamento físico resistido nas vias de sinalização da síntese e degradação de proteínas no músculo esquelético de ratos.
Rodrigues, C. (2015) · Digital Library of Theses and Dissertations (Universidade de São Paulo) · doi:10.11606/t.42.2015.tde-07122015-184843
Human population studies of transcriptome-wide expression in age-related traits
Pilling, L. C. (2015) · Open Research Exeter (University of Exeter)
Regulation of Hepatic Metabolism by the Mechanistic Target of Rapamycin
Lamming, D. W. (2015) · Springer eBooks · doi:10.1007/978-3-319-25065-6_3
NUTRIENT REGULATION OF AUTOPHAGY IN THE HEART
Trivedi, P. C. (2016) · DalSpace (Dalhousie University)
Role of Occludin in the Regulation of Epithelial Tight Junctions
Manda, B. (2016) · doi:10.21007/etd.cghs.2016.0415
The Molecular Machinery of Amino Acid Transport across the Vacuolar/Lysosomal Membrane
Sekito, T., & Kakinuma, Y. (2016) · KAGAKU TO SEIBUTSU · doi:10.1271/kagakutoseibutsu.54.324
The role of glutamine in the regulation of mTOR signalling in pancreatic β-cells
Alghanim, G. (2017) · Leicester Research Archive (University of Leicester)
Mutation of SLC7A14 Causes Syndromic Hearing Loss
Giffen, K. P. (2020) · Creighton Digital Repository (CDR)
A Sphingolipid-mTORC1 Nutrient-Sensing Machinery Enables Animal Development by Suppression of the Intestinal Peroxisome Relocation, Hormone Secretion and the Gut-Brain CrosstalkPreprint
Li, N., Hua, B., Chen, Q., Ruan, M., Teng, F., Zhu, M., Zhang, L., Huali, S., & Zhu, H. (2021) · SSRN Electronic Journal · doi:10.2139/ssrn.3917161
Regulation | mTOR and its Substrates
Proud, C. G., & Xie, J. (2020) · Elsevier eBooks · doi:10.1016/b978-0-12-819460-7.00001-3
Pengaruh Penerapan Keselamatan dan Kesehatan Kerja (K3) dan Kondisi Kelayakan Bengkel Terhadap Prestasi Belajar Peserta Didik pada Bengkel Pemesinan SMK Negeri 3 Boyolangu Kabupaten Tulungagung
Wibowo, A. (2014) · SKRIPSI Jurusan Teknik Mesin - Fakultas Teknik UM
トマトにおける果実生長および光合成産物の転流の動態に対する環境作用 (第3報) 塩ストレスの影響
荒木, 卓., 北野, 雅., OKANO, K., 吉田, 敏., & 江口, 壽. (2001) · 生物環境調節
Faculty Opinions recommendation of SLC38A10 (SNAT10) is located in ER and golgi compartments and has a role in regulating nascent protein synthesis.
Gleeson, P. A. (2021) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.737102915.793585379
Faculty Opinions recommendation of ER-lysosome contacts enable cholesterol sensing by mTORC1 and drive aberrant growth signalling in Niemann-Pick type C.
Anand, P. (2021) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.736651236.793581802

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