The DOI matches its Crossref record; 26 of the 26 references it cites were found in a registry or an index.
mTORC1 Senses Lysosomal Amino Acids Through an Inside-Out Mechanism That Requires the Vacuolar H + -ATPase
Open accessAbstract
Cellular sensing of amino acids occurs at the lysosome and is mediated by the vacuolar proton pump.
Overview
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
Cites
Statistics
Verification
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?
In the citing paper
“The interaction between Ragulator and the Rag heterodimers has been suggested to be dependent on the v-ATPase (Zoncu et al., 2011), which is thought to transmit intra-lysosomal amino acid signals to the Rags by affecting Ragulator GEF activity.”
From Signal integration in the (m)TORC1 growth pathway (2018) · cites this paper as Zoncu et al., 2011
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Repertoires of Autophagy in the Pathogenesis of Ocular Diseases
Li, Y., Jiang, Q. L., Cao, G.-F., Yao, J., & Yan, B. (2015) · Cellular Physiology and Biochemistry · doi:10.1159/000373980 · Cited by 16,351
mTOR: from growth signal integration to cancer, diabetes and ageing
Zoncu, R., Efeyan, A., & Sabatini, D. M. (2011) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3025 · Cited by 3,941
Self-citationThe 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
Self-citationSancak, 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
Self-citationRheb 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
Vacuolar ATPases: rotary proton pumps in physiology and pathophysiology
Forgac, M. D. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2272 · Cited by 1,626
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
Tee, A. R., Manning, B. D., Roux, P. P., Cantley, L. C., & Blenis, J. (2003) · Current Biology · doi:10.1016/s0960-9822(03)00506-2 · Cited by 1,080
Requirement of Prorenin Receptor and Vacuolar H + -ATPase–Mediated Acidification for Wnt Signaling
Cruciat, C.-M., Ohkawara, B., Acebron, S. P., Karaulanov, E., Reinhard, C., Ingelfinger, D., Boutros, M., & Niehrs, C. (2010) · Science · doi:10.1126/science.1179802 · Cited by 516
Trans-complex formation by proteolipid channels in the terminal phase of membrane fusion
Peters, C., Bayer, M. J., Bühler, S., Andersen, J., Mann, M., & Mayer, A. (2001) · Nature · doi:10.1038/35054500 · Cited by 501
Flagged first, then by citations
Cited by
Sorted by citations
Items 801–900 of 1,003
Disruption of the Rag-Ragulator Complex by c17orf59 Inhibits mTORC1
Schweitzer, L. D., Comb, W. C., Bar‐Peled, L., & Sabatini, D. M. (2015) · Cell Reports · doi:10.1016/j.celrep.2015.07.052 · Cited by 36
Self-citationRole of Rab GTPases and their interacting proteins in mediating metabolic signalling and regulation
Chua, C. E. L., & Tang, B. L. (2015) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-015-1862-x · Cited by 35
Yu, B., Xu, P., Zhao, Z., Cai, J., Sternberg, P., & Chen, Y. (2014) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.14-14758 · Cited by 33
Genetic heterogeneity in familial nocturnal frontal lobe epilepsy.
Steinlein, O. (2014) · Progress in Brain Research · doi:10.1016/b978-0-444-63326-2.00001-6 · Cited by 27
Kobayashi, T., Tsutsui, H., Shimabukuro-Demoto, S., Yoshida-Sugitani, R., Karyu, H., Furuyama-Tanaka, K., Ohshima, D., Kato, N., Okamura, T., & Toyama‐Sorimachi, N. (2017) · International Immunology · doi:10.1093/intimm/dxx063 · Cited by 33
Insights into the transport side of the human SLC38A9 transceptor
Scalise, M., Galluccio, M., Pochini, L., Cosco, J., Trotta, M., Rebsamen, M., Superti‐Furga, G., & Indiveri, C. (2019) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2019.07.006 · Cited by 36
Ion Channels and Transporters in Autophagy
Zhang, R., Kang, R., Klionsky, D. J., & Tang, D. (2021) · Autophagy · doi:10.1080/15548627.2021.1885147 · Cited by 33
Cao, Y., Li, R., Shen, M., Li, C., Zou, Y., Jiang, Q., Liu, S., Lu, C., Li, H., Liu, H., et al. (2021) · Cell Death and Disease · doi:10.1038/s41419-021-03694-9 · Cited by 35
Autophagy Inhibition in BRAF-Driven Cancers
Foth, M., & McMahon, M. (2021) · Cancers · doi:10.3390/cancers13143498 · Cited by 33
Miao, D., Wang, Y., Jia, Y., Tong, J., Jiang, S., & Liu, L. (2021) · Cellular Signalling · doi:10.1016/j.cellsig.2021.110200 · Cited by 35
Lei, Y., Huang, Y. J., Wen, X., Yin, Z., Zhang, Z., & Klionsky, D. J. (2022) · Antioxidants · doi:10.3390/antiox11020304 · Cited by 36
CryoEM of endogenous mammalian V-ATPase interacting with the TLDc protein mEAK-7
Tan, Y. Z., Abbas, Y. M., Wu, J., Wu, D., Keon, K. A., Hesketh, G. G., Bueler, S. A., Gingras, A., Robinson, C. V., Grinstein, S., et al. (2022) · Life Science Alliance · doi:10.26508/lsa.202201527 · Cited by 31
Comparative landscape of genetic dependencies in human and chimpanzee stem cells
She, R., Fair, T., Schaefer, N. K., Saunders, R. A., Pavlovic, B. J., Weissman, J. S., & Pollen, A. A. (2023) · Cell · doi:10.1016/j.cell.2023.05.043 · Cited by 34
Sato, T., Akasu, H., Shimono, W., Matsu, C., Fujiwara, Y., Shibagaki, Y., Heard, J. J., Tamanoi, F., & Hattori, S. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.592402 · Cited by 33
Cucurbitacin E Induces Autophagy via Downregulating mTORC1 Signaling and Upregulating AMPK Activity
Zha, Q., Zhang, X., Lin, Q.-R., Xu, L., Zhao, G., Pan, H., Zhou, D., Ouyang, D., Liu, Z., & He, X. (2015) · PLoS ONE · doi:10.1371/journal.pone.0124355 · Cited by 33
Zogzas, C. E., & Mukhopadhyay, S. (2018) · Metallomics · doi:10.1039/c8mt00115d · Cited by 33
The SLC36 transporter Pathetic is required for extreme dendrite growth in Drosophila sensory neuronsPreprint
Lin, W.-Y., Williams, C., Yan, C. H., Koledachkina, T., Luedke, K. P., Dalton, J., Bloomsburg, S., Morrison, N., Duncan, K. E., Kim, C. C., et al. (2015) · Genes & Development · doi:10.1101/gad.259119.115 · Cited by 36
The rapid proximity labeling system PhastID identifies ATP6AP1 as an unconventional GEF for Rheb
Feng, R., Liu, F., Li, R., Zhou, Z., Lin, Z., Song, L., Deng, S., Li, Y., Nong, B., Xia, Y., et al. (2024) · Cell Research · doi:10.1038/s41422-024-00938-z · Cited by 34
Lysosome quality control in health and neurodegenerative diseases
Ferrari, V., Tedesco, B., Cozzi, M., Chierichetti, M., Casarotto, E., Pramaggiore, P., Cornaggia, L., Mohamed, A. A., Patelli, G., Piccolella, M., et al. (2024) · Cellular & Molecular Biology Letters · doi:10.1186/s11658-024-00633-2 · Cited by 36
Tuberous Sclerosis Complex Protein 2-Independent Activation of mTORC1 by Human Cytomegalovirus pUL38
Bai, Y., Xuan, B., Liu, H., Zhong, J., Yu, D. L., & Qian, Z. (2015) · Journal of Virology · doi:10.1128/jvi.01027-15 · Cited by 30
Lipid droplet consumption is functionally coupled to vacuole homeostasis independent of lipophagy
Ouahoud, S., Fiet, M. D., Martínez-Montañés, F., Ejsing, C. S., Kuß, O., Roden, M., & Markgraf, D. F. (2018) · Journal of Cell Science · doi:10.1242/jcs.213876 · Cited by 29
Myeloid folliculin balances mTOR activation to maintain innate immunity homeostasis
Li, J., Wada, S., Weaver, L. K., Biswas, C., Behrens, E. M., & Arany, Z. P. (2019) · JCI Insight · doi:10.1172/jci.insight.126939 · Cited by 30
Loss of Furin in β-Cells Induces an mTORC1-ATF4 Anabolic Pathway That Leads to β-Cell Dysfunction
Brouwers, B., Coppola, I., Vints, K., Dislich, B., Jouvet, N., Lommel, L. V., Segers, C., Gounko, N. V., Thorrez, L., Schuit, F. C., et al. (2020) · Diabetes · doi:10.2337/db20-0474 · Cited by 32
Endolysosomal TRPMLs in Cancer
Xu, M., & Dong, X. (2021) · Biomolecules · doi:10.3390/biom11010065 · Cited by 33
ArfGAP1 inhibits mTORC1 lysosomal localization and activation
Meng, D., Yang, Q., Melick, C. H., Park, B. C., Hsieh, T., Curukovic, A., Jeong, M., Zhang, J., James, N. G., & Jewell, J. L. (2021) · The EMBO Journal · doi:10.15252/embj.2020106412 · Cited by 36
eIF4A inactivates TORC1 in response to amino acid starvation
Tsokanos, F., Albert, M., Demetriades, C., Spirohn, K., Boutros, M., & Teleman, A. A. (2016) · The EMBO Journal · doi:10.15252/embj.201593118 · Cited by 29
Effects of diphyllin as a novel V-ATPase inhibitor on TE-1 and ECA-109 cells
Chen, H., Liu, P., Zhang, T., Gao, Y., Zhang, Y., Shen, X., Xiao, L., & Shen, W. (2018) · Oncology Reports · doi:10.3892/or.2018.6191 · Cited by 32
The Vacuolar ATPase – A Nano-scale Motor That Drives Cell Biology
Harrison, M. A., & Muench, S. P. (2018) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-981-10-7757-9_14 · Cited by 32
KAT7-mediated CANX (calnexin) crotonylation regulates leucine-stimulated MTORC1 activity
Yan, G., Li, X., Zheng, Z., Gao, W., Chen, C., Wang, X., Cheng, Z., Yu, J., Zou, G., Farooq, M. Z., et al. (2022) · Autophagy · doi:10.1080/15548627.2022.2047481 · Cited by 30
Regulation of lysosomes in skeletal muscle during exercise, disuse and aging
Moradi, N., Sanfrancesco, V. C., Champsi, S., & Hood, D. A. (2024) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2024.09.028 · Cited by 33
Dynamin inhibitors block activation of mTORC1 by amino acids independently of dynamin
Persaud, A. K., Cormerais, Y., Pouysségur, J., & Rotin, D. (2018) · Journal of Cell Science · doi:10.1242/jcs.211755 · Cited by 30
PATs and SNATs: Amino Acid Sensors in Disguise
Fan, S., & Goberdhan, D. C. I. (2018) · Frontiers in Pharmacology · doi:10.3389/fphar.2018.00640 · Cited by 31
Cytosolic glucosylceramide regulates endolysosomal function in Niemann-Pick type C disease
Wheeler, S., Haberkant, P., Bhardwaj, M., Tongue, P., Ferraz, M. J., Halter, D., Sprong, H., Schmid, R., Aerts, J. M. F. G., Sullo, N., et al. (2019) · Neurobiology of Disease · doi:10.1016/j.nbd.2019.03.005 · Cited by 33
Liang, Y., Batistel, F., Parys, C., & Loor, J. J. (2019) · Journal of Dairy Science · doi:10.3168/jds.2018-15738 · Cited by 34
Phagocytosis: Phenotypically Simple Yet a Mechanistically Complex Process
Kumar, V. (2020) · International Reviews of Immunology · doi:10.1080/08830185.2020.1732958 · Cited by 31
Lysosomal recycling of amino acids affects ER quality control
Higuchi‐Sanabria, R., Shen, K., Kelet, N., Frankino, P. A., Durieux, J., Bar‐Ziv, R., Sing, C. N., Garcia, E. J., Homentcovschi, S., Sanchez, M., et al. (2020) · Science Advances · doi:10.1126/sciadv.aaz9805 · Cited by 30
Self-citationPossible Therapeutic Use of Natural Compounds Against COVID-19
Khan, N., Chen, X., & Geiger, J. D. (2021) · Journal of Cellular Signaling · doi:10.33696/signaling.2.036 · Cited by 30
Wang, X., Wei, Z., Lan, T., He, Y., Cheng, B., Li, R., Chen, H., Li, F., Liu, G., Jiang, B., et al. (2021) · Autophagy · doi:10.1080/15548627.2021.1934271 · Cited by 31
Zapata‐Muñoz, J., Villarejo‐Zori, B., Largo‐Barrientos, P., & Boya, P. (2021) · Cell Stress · doi:10.15698/cst2021.07.253 · Cited by 33
USP32-regulated LAMTOR1 ubiquitination impacts mTORC1 activation and autophagy induction
Hertel, A., Alves, L. M., Dutz, H., Tascher, G., Bonn, F., Kaulich, M., Đikić, I., Eimer, S., Steinberg, F., & Bremm, A. (2022) · Cell Reports · doi:10.1016/j.celrep.2022.111653 · Cited by 29
Growth or death? Control of cell destiny by mTOR and autophagy pathways
Khalil, M. I. M., Ali, M. M., Holail, J., & Houssein, M. (2023) · Progress in Biophysics and Molecular Biology · doi:10.1016/j.pbiomolbio.2023.10.002 · Cited by 32
Le, Y.-C., Zhang, S., Ni, J.-H., You, Y., Luo, K., Yu, Y.-Q., & Shen, X. (2018) · Cell Death and Disease · doi:10.1038/s41419-018-0719-2 · Cited by 29
A role for TOR signaling at every stage of plant life
Quilichini, T. D., Gao, P., Pandey, P. K., Xiang, D., Ren, M., & Datla, R. (2019) · Journal of Experimental Botany · doi:10.1093/jxb/erz125 · Cited by 31
Host nutrient sensing is mediated by mTOR signaling in cnidarian-dinoflagellate symbiosis
Voss, P. A., Gornik, S. G., Jacobovitz, M. R., Rupp, S., Dörr, M., Maegele, I., & Guse, A. (2023) · Current Biology · doi:10.1016/j.cub.2023.07.038 · Cited by 30
mTORC1 activity licenses its own release from the lysosomal surface
Acharya, A., & Demetriades, C. (2024) · Molecular Cell · doi:10.1016/j.molcel.2024.10.008 · Cited by 30
Das, S., Murumulla, L., Ghosh, P., & Challa, S. (2025) · BioMetals · doi:10.1007/s10534-025-00665-x · Cited by 30
Trajković, K., Valdez, C., Ysselstein, D., & Krainc, D. (2019) · PLoS ONE · doi:10.1371/journal.pone.0211727 · Cited by 30
Amino acids stimulate the endosome-to-Golgi trafficking through Ragulator and small GTPase Arl5
Shi, M., Chen, B., Mahajan, D., Boh, B. K., Zhou, Y., Dutta, B., Tie, H. C., Sze, S. K., Wu, G., & Lü, L. (2018) · Nature Communications · doi:10.1038/s41467-018-07444-y · Cited by 30
Collins, M. P., Stransky, L. A., & Forgac, M. D. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.ra120.013223 · Cited by 32
Pharmacological Targeting of Vacuolar H+-ATPase via Subunit V1G Combats Multidrug-Resistant Cancer
Wang, Y., Zhang, L., Wei, Y., Huang, W., Li, L., Wu, A., Dastur, A., Greninger, P., Bray, W. M., Zhang, C., et al. (2020) · Cell chemical biology · doi:10.1016/j.chembiol.2020.06.011 · Cited by 30
Regulation of DNA duplication by the mTOR signaling pathway
He, Z., Houghton, P. J., Williams, T. M., & Shen, C. (2021) · Cell Cycle · doi:10.1080/15384101.2021.1897271 · Cited by 30
Larsen, L. E., van den Boogert, M. A. W., Ríos‐Ocampo, W. A., Jansen, J. C., Conlon, D., Chong, P. L. E., Levels, J. H. M., Eilers, R. E., Sachdev, V., Zelcer, N., et al. (2021) · Cellular and Molecular Gastroenterology and Hepatology · doi:10.1016/j.jcmgh.2021.09.013 · Cited by 30
New Insights into the Regulation of mTOR Signaling via Ca2+-Binding Proteins
Amemiya, Y., Maki, M., Shibata, H., & Takahara, T. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24043923 · Cited by 30
The role of TFEB in tumor cell autophagy: Diagnostic and therapeutic opportunities
Bahrami, A., Bianconi, V., Pirro, M., Orafai, H. M., & Sahebkar, A. (2020) · Life Sciences · doi:10.1016/j.lfs.2020.117341 · Cited by 29
Ponnaiyan, S., Akter, F., Singh, J., & Winter, D. (2020) · Scientific Data · doi:10.1038/s41597-020-0399-5 · Cited by 29
Targeted Quantification of the Lysosomal Proteome in Complex Samples
Mosen, P., Sanner, A., Singh, J., & Winter, D. (2021) · Proteomes · doi:10.3390/proteomes9010004 · Cited by 26
The balance of protein expression and degradation: an ESCRTs point of view
Babst, M., & Odorizzi, G. (2013) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2013.05.003 · Cited by 29
Dimeric quinacrines as chemical tools to identify PPT1, a new regulator of autophagy in cancer cells
Nicastri, M. C., Rebecca, V. W., Amaravadi, R. K., & Winkler, J. D. (2017) · Molecular & Cellular Oncology · doi:10.1080/23723556.2017.1395504 · Cited by 29
Cui, X., Feng, R., Wang, J., Du, C., Pi, X., Chen, D., Li, J., Li, H., Zhang, J., Zhang, J., et al. (2019) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2019.129496 · Cited by 29
Nanoparticle-Mediated Therapeutic Application for Modulation of Lysosomal Ion Channels and Functions
Lee, D., & Hong, J. H. (2020) · Pharmaceutics · doi:10.3390/pharmaceutics12030217 · Cited by 30
Niu, X., Qian, X., Feng, H., Yi, K., Dong, L., Chen, W., & Ye, J. (2020) · Aquaculture · doi:10.1016/j.aquaculture.2020.736281 · Cited by 29
Prakasam, G., Mishra, A., Christie, A. L., Miyata, J., Carrillo, D., Tcheuyap, V. T., Ye, H., Do, Q. N., Wang, Y., Reig, Ò., et al. (2024) · Journal of Clinical Investigation · doi:10.1172/jci170559 · Cited by 28
Johnson, M. (2012) · Materials and Methods · doi:10.13070/mm.en.2.117 · Cited by 29
The Atg1-Tor pathway regulates yolk catabolism in Drosophila embryos
Kuhn, H., Sopko, R., Coughlin, M. L., Perrimon, N., & Mitchison, T. J. (2015) · Development · doi:10.1242/dev.125419 · Cited by 29
Niu, F., Li, Z., Ren, Y., Li, Z., Guan, H., Li, Y., Zhang, Y., Li, Y., Yang, J., Lü, Q., et al. (2023) · Redox Biology · doi:10.1016/j.redox.2023.102824 · Cited by 28
Lester, H. A., Lavis, L. D., & Dougherty, D. A. (2015) · American Journal of Psychiatry · doi:10.1176/appi.ajp.2015.14121537 · Cited by 29
FLCN Maintains the Leucine Level in Lysosome to Stimulate mTORC1
Wu, X., Zhao, L., Chen, Z. J., Ji, X., Qiao, X., Jin, Y., & Liu, W. (2016) · PLoS ONE · doi:10.1371/journal.pone.0157100 · Cited by 26
Wang, D., Wan, X., Peng, J., Xiong, Q., Niu, H., Li, H., Chai, J., & Jiang, S. (2017) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2017.02.084 · Cited by 28
Nanotechnology-Based Targeting of mTOR Signaling in Cancer
Yoon, M. (2020) · International Journal of Nanomedicine · doi:10.2147/ijn.s254574 · Cited by 35
High Metabolic Function and Resilience of NKG2A-Educated NK Cells
Highton, A. J., Diercks, B., Möckl, F., Martrus, G., Sauter, J., Schmidt, A. H., Bunders, M. J., Körner, C., Guse, A. H., & Altfeld, M. A. (2020) · Frontiers in Immunology · doi:10.3389/fimmu.2020.559576 · Cited by 27
Lysosomes in T Cell Immunity and Aging
Jin, J., Zhang, H., Weyand, C. M., & Goronzy, J. J. (2021) · Frontiers in Aging · doi:10.3389/fragi.2021.809539 · Cited by 30
Autophagy and the (Pro)renin Receptor
Binger, K. J., & Müller, D. N. (2013) · Frontiers in Endocrinology · doi:10.3389/fendo.2013.00155 · Cited by 27
Role of Notch signaling during lipopolysaccharide-induced preterm labor
Agrawal, V., Jaiswal, M. K., Pamarthy, S., Katara, G. K., Kulshrestha, A., Gilman‐Sachs, A., Hirsch, E., & Beaman, K. D. (2015) · Journal of Leukocyte Biology · doi:10.1189/jlb.3hi0515-200rr · Cited by 28
Biolayer interferometry of lipid nanodisc‐reconstituted yeast vacuolar H+‐ATPase
Sharma, S., & Wilkens, S. (2017) · Protein Science · doi:10.1002/pro.3143 · Cited by 28
GSK-3-TSC axis governs lysosomal acidification through autophagy and endocytic pathways
Avrahami, L., Paz, R., Dominko, K., Hecimovic, S. K., Bucci, C., & Eldar-Finkelman, H. (2020) · Cellular Signalling · doi:10.1016/j.cellsig.2020.109597 · Cited by 28
A GC-MS/Single-Cell Method to Evaluate Membrane Transporter Substrate Specificity and Signaling
Fairweather, S. J., Okada, S., Gauthier-Coles, G., Javed, K., Bröer, A., & Bröer, S. (2021) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2021.646574 · Cited by 30
SPAR, a lncRNA encoded mTORC1 inhibitor
Matsumoto, A., Clohessy, J. G., & Pandolfi, P. P. (2017) · Cell Cycle · doi:10.1080/15384101.2017.1304735 · Cited by 28
Tol, M. J., van der Lienden, M. J. C., Gabriel, T. L., Hagen, J. J., Scheij, S., Veenendaal, T., Klumperman, J., Donker-Koopman, W. E., Verhoeven, A. J., Overkleeft, H., et al. (2018) · Autophagy · doi:10.1080/15548627.2017.1419118 · Cited by 27
Patursky-Polischuk, I., Kasir, J., Miloslavski, R., Hayouka, Z., Hausner-Hanochi, M., Stolovich-Rain, M., Tsukerman, P., Biton, M., Mudhasani, R., Jones, S. N., et al. (2014) · PLoS ONE · doi:10.1371/journal.pone.0109410 · Cited by 28
Zhang, Z., Wang, H., Ding, Q., Xing, Y., Xu, D., Xu, Z., Zhou, T., Qian, B., Ji, C., Pan, X., et al. (2017) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2017.02.103 · Cited by 27
Eichner, R., Fernández‐Sáiz, V., Targosz, B., & Bassermann, F. C. (2018) · International review of cytology · doi:10.1016/bs.ircmb.2018.06.001 · Cited by 27
Yao, Y., Hong, S., Ikeda, T., Mori, H., MacDougald, O. A., Nada, S., Okada, M., & Inoki, K. (2020) · Molecular Cell · doi:10.1016/j.molcel.2020.10.004 · Cited by 28
RIPK1 regulates starvation resistance by modulating aspartate catabolism
Mei, X., Guo, Y. L., Xie, Z., Zhong, Y., Wu, X., Xu, D., Li, Y., Liu, N., & Zhu, Z. (2021) · Nature Communications · doi:10.1038/s41467-021-26423-4 · Cited by 27
PPT1 Reduction Contributes to Erianin-Induced Growth Inhibition in Oral Squamous Carcinoma Cells
Luo, Q., Li, X., Gan, G., Yang, M., Xu, C. Y., & Chen, F. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.764263 · Cited by 26
Targeting mTOR Signaling in Type 2 Diabetes Mellitus and Diabetes Complications
Yang, L., Zhang, Z., Wang, D., Jiang, Y., & Liu, Y. (2022) · Current Drug Targets · doi:10.2174/1389450123666220111115528 · Cited by 27
Kim, S. W., Cha, M., Lee, S., Song, B., Jin, X., Lee, J. M., Park, J. H., & Lee, J. D. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20102375 · Cited by 26
Morel, M., Shah, K. N., & Long, W. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.ra120.012658 · Cited by 27
Mani, K. M., Javaheri, A., & Diwan, A. (2018) · Comprehensive physiology · doi:10.1002/cphy.c180005 · Cited by 29
The TMEM127 human tumor suppressor is a component of the mTORC1 lysosomal nutrient-sensing complex
Deng, Y., Qin, Y., Srikantan, S., Luo, A., Cheng, Z.-M., Flores, S. K., Vogel, K. S., Wang, E., & Dahia, P. L. M. (2018) · Human Molecular Genetics · doi:10.1093/hmg/ddy095 · Cited by 25
Environmental signaling through the mechanistic target of rapamycin complex 1
Workman, J. J., Chen, H., & Laribee, R. N. (2014) · Cell Cycle · doi:10.4161/cc.28112 · Cited by 27
AMDE-1 Is a Dual Function Chemical for Autophagy Activation and Inhibition
Li, M., Yang, Z., Vollmer, L. L., Gao, Y., Fu, Y., Liu, C., Chen, X., Liu, P., Vogt, A., & Yin, X. (2015) · PLoS ONE · doi:10.1371/journal.pone.0122083 · Cited by 26
Prelysosomal Compartments in the Unconventional Secretion of Amyloidogenic Seeds
Madsen, H. B., & Vilhardt, F. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18010227 · Cited by 26
Liu, J., Wang, Y., Li, D., Wang, Y., Li, M., Chen, C., Fang, X., Chen, H., & Zhang, C. (2017) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.201601017 · Cited by 25
Suryawan, A., & Davis, T. A. (2018) · Journal of Nutrition · doi:10.1093/jn/nxy044 · Cited by 28
Jin, R. U., & Mills, J. C. (2019) · Current Opinion in Gastroenterology · doi:10.1097/mog.0000000000000540 · Cited by 26
Farah, B. L., Yen, P. M., & Koeberl, D. D. (2019) · Molecular Genetics and Metabolism · doi:10.1016/j.ymgme.2019.11.005 · Cited by 26
Muthukottiappan, P., & Winter, D. (2021) · Molecular Omics · doi:10.1039/d1mo00205h · Cited by 26
SNAT7 regulates mTORC1 via macropinocytosis
Meng, D., Yang, Q., Jeong, M.-H., Curukovic, A., Tiwary, S., Melick, C. H., Lama-Sherpa, T. D., Wang, H., Huerta-Rosario, M., Urquhart, G., et al. (2022) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2123261119 · Cited by 26
Amino acid sensing and regulation of mTORC1
Yan, L., & Lamb, R. F. (2012) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2012.02.001 · Cited by 28
Barone, S., Zahedi, K. A., Brooks, M., Henske, E. P., Yang, Y., Zhang, E. Y., Bissler, J. J., Yu, J. J., & Soleimani, M. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2020190118 · Cited by 26
Metadata
- Authors
- Zoncu, R., Bar-Peled, L., Efeyan, A., Wang, S., Sancak, Y., & Sabatini, D. M.
- Affiliations
- Broad Institute (US)
- Whitehead Institute for Biomedical Research, Nine Cambridge Center, Cambridge, MA 02142, USA.
- Whitehead Institute for Biomedical Research (US)
- Corresponding author
- Sabatini, David M.
- Venue
- Science
- Published
- 2011-11-04
- Volume
- 334
- Issue
- 6056
- Pages
- 678-683
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- PMC
- PMC3211112
- OpenAlex
- W2111607026
- Cited by
- 1,673
- References
- 26
- Citations by year
- 2026: 72 · 2025: 78 · 2024: 75 · 2023: 104 · 2022: 98 · 2021: 141 · 2020: 130 · 2019: 113 · 2018: 135 · 2017: 127 · 2016: 139 · 2015: 153 · 2014: 120 · 2013: 114 · 2012: 70
- FWCI
- 39.82
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Science (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- DSpace@MIT (Massachusetts Institute of Technology) (submittedVersion, cc-by-nc-sa)
- PMC
- Funders
- Howard Hughes Medical Institute
- National Cancer Institute (CA103866, R01CA103866, R01CA129105)
- National Institute of General Medical Sciences (T32GM007753)
- National Institute of Allergy and Infectious Diseases (R37AI047389, AI47389), R01AI047389)
- 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
- mTORC1, amino acid sensing, vacuolar H+-ATPase, Rag GTPases, lysosomal translocation, inside-out signaling, ATP hydrolysis, cell growth regulation
- MeSH terms
- Mechanistic Target of Rapamycin Complex 1, Amino Acids, Animals, Cell Line, Drosophila, Humans, Lysosomes, Proteins, Signal Transduction, GTP Phosphohydrolases, Vacuolar Proton-Translocating ATPases, RNA Interference, Multiprotein Complexes, 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