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
Cited by
Sorted by citations
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
Self-citationmTOR Signaling in Growth, Metabolism, and Disease
Saxton, R. A., & Sabatini, D. M. (2017) · Cell · doi:10.1016/j.cell.2017.02.004 · Cited by 7,555
Self-citationGuidelines for the use and interpretation of assays for monitoring autophagy (3rd edition).
Klionsky, D. J., Abdelmohsen, K., Abe, A., Abedin, M. J., Abeliovich, H., Acevedo Arozena, A., Adachi, H., Adams, C. M., Adams, P. D., Adeli, K., et al. (2016) · Autophagy · doi:10.1080/15548627.2015.1100356 · Cited by 5,894
Guidelines for the use and interpretation of assays for monitoring autophagy
Klionsky, D. J., Abdalla, F. C., Abeliovich, H., Abraham, R. T., Acevedo-Arozena, A., Adeli, K., Agholme, L., Agnello, M., Agostinis, P., Aguirre-Ghiso, J. A., et al. (2012) · Autophagy · doi:10.4161/auto.19496 · Cited by 3,996
Dynamics and functions of lipid droplets
Olzmann, J. A., & Carvalho, P. (2019) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-018-0085-z · Cited by 2,740
mTOR at the nexus of nutrition, growth, ageing and disease
Liu, G. Y., & Sabatini, D. M. (2020) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-019-0199-y · Cited by 2,737
Self-citationGuidelines for the use and interpretation of assays for monitoring autophagy (4th edition) 1
Klionsky, D. J., Abdel-Aziz, A. K., Abdelfatah, S., Abdellatif, M., Abdoli, A., Abel, S., Abeliovich, H., Abildgaard, M. H., Abudu, Y. P., Acevedo-Arozena, A., et al. (2021) · Autophagy · doi:10.1080/15548627.2020.1797280 · Cited by 2,897
Oxidative stress and autophagy: The clash between damage and metabolic needs
Filomeni, G., De Zio, D., & Cecconi, F. (2015) · Cell Death & Differentiation · doi:10.1038/cdd.2014.150 · Cited by 2,195
MTOR: a pharmacologic target for autophagy regulation
Kim, Y. C., & Guan, K.-L. (2015) · Journal of Clinical Investigation · doi:10.1172/jci73939 · Cited by 2,126
Chloroquine inhibits autophagic flux by decreasing autophagosome-lysosome fusion
Mauthe, M., Orhon, I., Rocchi, C., Zhou, X., Luhr, M., Hijlkema, K.-J., Coppes, R. P., Engedal, N., Mari, M., & Reggiori, F. (2018) · Autophagy · doi:10.1080/15548627.2018.1474314 · Cited by 2,122
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
Self-citationSignals from the lysosome: a control centre for cellular clearance and energy metabolism
Settembre, C., Fraldi, A., Medina, D. L., & Ballabio, A. (2013) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3565 · Cited by 1,742
Phosphoinositides: Tiny Lipids With Giant Impact on Cell Regulation
Balla, T. (2013) · Physiological Reviews · doi:10.1152/physrev.00028.2012 · Cited by 1,638
Mechanisms regulating skeletal muscle growth and atrophy
Schiaffino, S., Dyar, K. A., Ciciliot, S., Blaauw, B., & Sandri, M. (2013) · The FEBS Journal · doi:10.1111/febs.12253 · Cited by 1,492
Autophagy modulation as a potential therapeutic target for diverse diseases
Rubinsztein, D. C., Codogno, P., & Levine, B. (2012) · Nature Reviews Drug Discovery · doi:10.1038/nrd3802 · Cited by 1,463
Lysosomal calcium signalling regulates autophagy through calcineurin and TFEB
Medina, D. L., Paola, S. D., Peluso, I., Armani, A., Stefani, D. D., Venditti, R., Montefusco, S., Rosato, A. S., Prezioso, C., Forrester, A. R., et al. (2015) · Nature Cell Biology · doi:10.1038/ncb3114 · Cited by 1,452
Roczniak-Ferguson, A., Petit, C. S. V., Froehlich, F., Qian, S., Ky, J., Angarola, B. L., Walther, T. C., & Ferguson, S. M. (2012) · Science Signaling · doi:10.1126/scisignal.2002790 · Cited by 1,393
The autophagosome: origins unknown, biogenesis complex
Lamb, C. A., Yoshimori, T., & Tooze, S. A. (2013) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3696 · Cited by 1,367
Sestrin2 is a leucine sensor for the mTORC1 pathway
Wolfson, R. L., Chantranupong, L., Saxton, R. A., Shen, K., Scaria, S. M., Cantor, J. R., & Sabatini, D. M. (2016) · Science · doi:10.1126/science.aab2674 · Cited by 1,306
Self-citationAutophagy promotes immune evasion of pancreatic cancer by degrading MHC-I
Yamamoto, K., Venida, A., Yano, J., Biancur, D. E., Kakiuchi, M., Gupta, S., Sohn, A. S. W., Mukhopadhyay, S., Lin, E. Y., Parker, S. J., et al. (2020) · Nature · doi:10.1038/s41586-020-2229-5 · Cited by 1,240
Emerging regulation and functions of autophagy
Boya, P., Reggiori, F., & Codogno, P. (2013) · Nature Cell Biology · doi:10.1038/ncb2788 · Cited by 1,216
AMPK: Sensing Glucose as well as Cellular Energy Status
Lin, S., & Hardie, D. G. (2017) · Cell Metabolism · doi:10.1016/j.cmet.2017.10.009 · Cited by 1,198
Nutrient-sensing mechanisms and pathways
Efeyan, A., Comb, W. C., & Sabatini, D. M. (2015) · Nature · doi:10.1038/nature14190 · Cited by 1,110
Self-citationBar-Peled, L., Chantranupong, L., Cherniack, A. D., Chen, W. W., Ottina, K. A., Grabiner, B. C., Spear, E. D., Carter, S. L., Meyerson, M., & Sabatini, D. M. (2013) · Science · doi:10.1126/science.1232044 · Cited by 1,080
“The resulting digests were analyzed by mass spectrometry as described (3).”
Self-citationmTOR as a central hub of nutrient signalling and cell growth
Kim, J., & Guan, K. (2018) · Nature Cell Biology · doi:10.1038/s41556-018-0205-1 · Cited by 1,094
Making new contacts: the mTOR network in metabolism and signalling crosstalk
Shimobayashi, M., & Hall, M. N. (2014) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3757 · Cited by 1,053
Xu, H., & Ren, D. (2015) · Annual Review of Physiology · doi:10.1146/annurev-physiol-021014-071649 · Cited by 1,060
Autophagy—a key player in cellular and body metabolism
Kim, K. H., & Lee, M. (2014) · Nature Reviews Endocrinology · doi:10.1038/nrendo.2014.35 · Cited by 972
Efficiency of siRNA delivery by lipid nanoparticles is limited by endocytic recycling
Sahay, G., Querbes, W., Alabi, C., Eltoukhy, A., Sarkar, S., Zurenko, C., Karagiannis, E., Love, K., Chen, D., Zoncu, R., et al. (2013) · Nature Biotechnology · doi:10.1038/nbt.2614 · Cited by 948
Self-citationRagulator Is a GEF for the Rag GTPases that Signal Amino Acid Levels to mTORC1
Bar-Peled, L., Schweitzer, L. D., Zoncu, R., & Sabatini, D. M. (2012) · Cell · doi:10.1016/j.cell.2012.07.032 · Cited by 918
Self-citationThe lysosome as a cellular centre for signalling, metabolism and quality control
Lawrence, R. E., & Zoncu, R. (2019) · Nature Cell Biology · doi:10.1038/s41556-018-0244-7 · Cited by 920
Self-citationAmino acid signalling upstream of mTOR
Jewell, J. L., Russell, R. C., & Guan, K.-L. (2013) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3522 · Cited by 894
Mechanisms and Functions of Long Non-Coding RNAs at Multiple Regulatory Levels
Zhang, X., Wang, W., Zhu, W., Dong, J., Cheng, Y., Yin, Z., & Shen, F. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20225573 · Cited by 906
Metabolic control of autophagy
Galluzzi, L., Pietrocola, F., Levine, B., & Kroemer, G. (2014) · Cell · doi:10.1016/j.cell.2014.11.006 · Cited by 855
The CASTOR Proteins Are Arginine Sensors for the mTORC1 Pathway
Chantranupong, L., Scaria, S. M., Saxton, R. A., Gygi, M. P., Shen, K., Wyant, G. A., Wang, T., Harper, J. W., Gygi, S. P., & Sabatini, D. M. (2016) · Cell · doi:10.1016/j.cell.2016.02.035 · Cited by 843
Self-citationNapolitano, G., & Ballabio, A. (2016) · Journal of Cell Science · doi:10.1242/jcs.146365 · Cited by 864
AMPK and TOR: The Yin and Yang of Cellular Nutrient Sensing and Growth Control
González, A., Hall, M. N., Lin, S.-C., & Hardie, D. G. (2020) · Cell Metabolism · doi:10.1016/j.cmet.2020.01.015 · Cited by 797
Lysosomal amino acid transporter SLC38A9 signals arginine sufficiency to mTORC1
Wang, S., Tsun, Z.-Y., Wolfson, R. L., Shen, K., Wyant, G. A., Plovanich, M., Yuan, E. D., Jones, T. D., Chantranupong, L., Comb, W. C., et al. (2015) · Science · doi:10.1126/science.1257132 · Cited by 865
Self-citationTranscriptional control of autophagy-lysosome function drives pancreatic cancer metabolism
Perera, R. M., Stoykova, S., Nicolay, B. N., Ross, K. N., Fitamant, J., Boukhali, M., Lengrand, J., Deshpande, V., Selig, M. K., Ferrone, C. R., et al. (2015) · Nature · doi:10.1038/nature14587 · Cited by 799
Self-citationYim, W. W., & Mizushima, N. (2020) · Cell Discovery · doi:10.1038/s41421-020-0141-7 · Cited by 839
Regulation of mTORC1 by amino acids
Bar-Peled, L., & Sabatini, D. M. (2014) · Trends in Cell Biology · doi:10.1016/j.tcb.2014.03.003 · Cited by 773
Self-citationMenon, S., Dibble, C. C., Talbott, G., Hoxhaj, G., Valvezan, A. J., Takahashi, H., Cantley, L. C., & Manning, B. D. (2014) · Cell · doi:10.1016/j.cell.2013.11.049 · Cited by 766
Differential regulation of mTORC1 by leucine and glutamine
Jewell, J. L., Kim, Y. C., Russell, R. C., Yu, F.-X., Park, H. W., Plouffe, S. W., Tagliabracci, V. S., & Guan, K.-L. (2015) · Science · doi:10.1126/science.1259472 · Cited by 757
Lipton, J. O., & Şahin, M. (2014) · Neuron · doi:10.1016/j.neuron.2014.09.034 · Cited by 767
Nutrient sensing and TOR signaling in yeast and mammals
González, A., & Hall, M. N. (2017) · The EMBO Journal · doi:10.15252/embj.201696010 · Cited by 752
Glutaminolysis Activates Rag-mTORC1 Signaling
Durán, R. V., Oppliger, W., Robitaille, A. M., Heiserich, L., Skendaj, R., Gottlieb, E., & Hall, M. N. (2012) · Molecular Cell · doi:10.1016/j.molcel.2012.05.043 · Cited by 766
Signal integration by mTORC1 coordinates nutrient input with biosynthetic output
Dibble, C. C., & Manning, B. D. (2013) · Nature Cell Biology · doi:10.1038/ncb2763 · Cited by 743
Protein breakdown in muscle wasting: Role of autophagy-lysosome and ubiquitin-proteasome
Sandri, M. (2013) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2013.04.023 · Cited by 689
Cysteine cathepsin proteases: regulators of cancer progression and therapeutic response
Olson, O. C., & Joyce, J. A. (2015) · Nature reviews. Cancer · doi:10.1038/nrc4027 · Cited by 703
Lysosomal storage disorders: The cellular impact of lysosomal dysfunction
Platt, F. M., Boland, B., & van der Spoel, A. C. (2012) · Journal of Cell Biology · doi:10.1083/jcb.201208152 · Cited by 689
Abu-Remaileh, M., Wyant, G. A., Kim, C., Laqtom, N. N., Abbasi, M., Chan, S. H., Freinkman, E., & Sabatini, D. M. (2017) · Science · doi:10.1126/science.aan6298 · Cited by 680
Self-citationSLC38A9 is a component of the lysosomal amino acid sensing machinery that controls mTORC1
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., et al. (2015) · Nature · doi:10.1038/nature14107 · Cited by 673
Regulation of mTORC1 and its impact on gene expression at a glance
Laplante, M., & Sabatini, D. M. (2013) · Journal of Cell Science · doi:10.1242/jcs.125773 · Cited by 695
Self-citationThe Lysosome as a Regulatory Hub
Perera, R. M., & Zoncu, R. (2016) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev-cellbio-111315-125125 · Cited by 688
Self-citationmTORC1 and muscle regeneration are regulated by the LINC00961-encoded SPAR polypeptide
Matsumoto, A., Pasut, A., Matsumoto, M., Yamashita, R., Fung, J., Monteleone, E., Saghatelian, A., Nakayama, K., Clohessy, J., & Pandolfi, P. (2016) · Nature · doi:10.1038/nature21034 · Cited by 594
mTORC1 signaling and the metabolic control of cell growth
Ben‐Sahra, I., & Manning, B. D. (2017) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2017.02.012 · Cited by 663
Martina, J. A., Diab, H. I., Lishu, L., Jeong-A, L., Patange, S., Raben, N., & Puertollano, R. (2014) · Science Signaling · doi:10.1126/scisignal.2004754 · Cited by 677
Nutrient sensing and signaling in the yeast Saccharomyces cerevisiae
Conrad, M., Schothorst, J., Kankipati, H. N., Zeebroeck, G. V., Rubio‐Texeira, M., & Thevelein, J. M. (2014) · FEMS Microbiology Reviews · doi:10.1111/1574-6976.12065 · Cited by 630
TBC1D7 Is a Third Subunit of the TSC1-TSC2 Complex Upstream of mTORC1
Dibble, C. C., Elis, W., Menon, S., Qin, W., Klekota, J., Asara, J. M., Finan, P. M., Kwiatkowski, D. J., Murphy, L. O., & Manning, B. D. (2012) · Molecular Cell · doi:10.1016/j.molcel.2012.06.009 · Cited by 612
Disrupting proton dynamics and energy metabolism for cancer therapy
Parks, S. K., Chiche, J., & Pouysségur, J. (2013) · Nature reviews. Cancer · doi:10.1038/nrc3579 · Cited by 631
The position of lysosomes within the cell determines their luminal pH
Johnson, D. E., Ostrowski, P., Jaumouillé, V., & Grinstein, S. (2016) · Journal of Cell Biology · doi:10.1083/jcb.201507112 · Cited by 590
Endosome maturation, transport and functions
Scott, C. C., Vacca, F., & Grüenberg, J. (2014) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2014.03.034 · Cited by 616
Tsun, Z.-Y., Bar-Peled, L., Chantranupong, L., Zoncu, R., Wang, T., Kim, C., Spooner, E., & Sabatini, D. M. (2013) · Molecular Cell · doi:10.1016/j.molcel.2013.09.016 · Cited by 565
Self-citationAn Autophagic Flux Probe that Releases an Internal Control
Kaizuka, T., Morishita, H., Hama, Y., Tsukamoto, S., Matsui, T., Toyota, Y., Kodama, A., Ishihara, T., Mizushima, T., & Mizushima, N. (2016) · Molecular Cell · doi:10.1016/j.molcel.2016.09.037 · Cited by 578
Autophagy: The spotlight for cellular stress responses
Ravanan, P., Florance, I., & Talwar, P. (2017) · Life Sciences · doi:10.1016/j.lfs.2017.08.029 · Cited by 595
mTORC1 as the main gateway to autophagy
Rabanal‐Ruiz, Y., Otten, E. G., & Korolchuk, V. I. (2017) · Essays in Biochemistry · doi:10.1042/ebc20170027 · Cited by 591
Colacurcio, D. J., & Nixon, R. A. (2016) · Ageing Research Reviews · doi:10.1016/j.arr.2016.05.004 · Cited by 548
Mechanisms and functions of lysosome positioning
Pu, J., Guardia, C. M., Keren-Kaplan, T., & Bonifacino, J. S. (2016) · Journal of Cell Science · doi:10.1242/jcs.196287 · Cited by 570
Lysosomal cholesterol activates mTORC1 via an SLC38A9–Niemann-Pick C1 signaling complex
Castellano, B. M., Thelen, A. M., Moldavski, O., Feltes, M., van der Welle, R. E. N., Mydock-McGrane, L., Jiang, X., van Eijkeren, R. J., Davis, O. B., Louie, S. M., et al. (2017) · Science · doi:10.1126/science.aag1417 · Cited by 562
Self-citationZhang, C., Jiang, B., Li, M., Zhu, M., Peng, Y., Zhang, Y., Wu, Y., Li, T. Y., Yu, L., Lu, Z., et al. (2014) · Cell Metabolism · doi:10.1016/j.cmet.2014.06.014 · Cited by 565
The Dawn of the Age of Amino Acid Sensors for the mTORC1 Pathway
Wolfson, R. L., & Sabatini, D. M. (2017) · Cell Metabolism · doi:10.1016/j.cmet.2017.07.001 · Cited by 563
Self-citationWhere is mTOR and what is it doing there?
Betz, C., & Hall, M. N. (2013) · The Journal of Cell Biology · doi:10.1083/jcb.201306041 · Cited by 531
Twenty-five years of mTOR: Uncovering the link from nutrients to growth
Sabatini, D. M. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1716173114 · Cited by 525
Self-citationAmino acid homeostasis and signalling in mammalian cells and organisms
Bröer, S., & Bröer, A. (2017) · Biochemical Journal · doi:10.1042/bcj20160822 · Cited by 518
Pearce, E. J., & Everts, B. (2014) · Nature reviews. Immunology · doi:10.1038/nri3771 · Cited by 499
Lysosome biogenesis: Regulation and functions
Yang, C., & Wang, X. (2021) · The Journal of Cell Biology · doi:10.1083/jcb.202102001 · Cited by 491
Chantranupong, L., Wolfson, R. L., Orozco, J. M., Saxton, R. A., Scaria, S. M., Bar-Peled, L., Spooner, E., Isasa, M., Gygi, S. P., & Sabatini, D. M. (2014) · Cell Reports · doi:10.1016/j.celrep.2014.09.014 · Cited by 466
Self-citationDoxorubicin Blocks Cardiomyocyte Autophagic Flux by Inhibiting Lysosome Acidification
Li, D. ‘., Wang, Z. V., Ding, G., Tan, W. H., Luo, X., Criollo, A., Xie, M., Jiang, N., May, H. I., Kyrychenko, V., et al. (2016) · Circulation · doi:10.1161/circulationaha.115.017443 · Cited by 469
Structural basis for leucine sensing by the Sestrin2-mTORC1 pathway
Saxton, R. A., Knockenhauer, K. E., Wolfson, R. L., Chantranupong, L., Pacold, M. E., Wang, T., Schwartz, T. U., & Sabatini, D. M. (2016) · Science · doi:10.1126/science.aad2087 · Cited by 457
Self-citationRegulation of mTORC1 by the Rag GTPases is necessary for neonatal autophagy and survival
Efeyan, A., Zoncu, R., Chang, S. H., Gumper, I., Snitkin, H., Wolfson, R. L., Kirak, O., Sabatini, D. M., & Sabatini, D. M. (2012) · Nature · doi:10.1038/nature11745 · Cited by 473
Self-citationTOR Signaling and Nutrient Sensing
Dobrenel, T., Caldana, C., Hanson, J., Robaglia, C., Vincentz, M., Veit, B., & Meyer, C. (2016) · Annual Review of Plant Biology · doi:10.1146/annurev-arplant-043014-114648 · Cited by 469
The Autophagy–Lysosomal Pathway in Neurodegeneration: A TFEB Perspective
Martini-Stoica, H., Xu, Y., Ballabio, A., & Zheng, H. (2016) · Trends in Neurosciences · doi:10.1016/j.tins.2016.02.002 · Cited by 436
Amino acids and mTORC1: from lysosomes to disease
Efeyan, A., Zoncu, R., & Sabatini, D. M. (2012) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2012.05.007 · Cited by 436
“This study also identified the vacuolar H+-ATPase (vATPase) as an essential mediator of the inside-out signal that engages in extensive, amino acid-regulated interactions with Ragulator and Rags [35].”
Self-citationGe, L., Melville, D., Zhang, M., & Schekman, R. W. (2013) · eLife · doi:10.7554/elife.00947 · Cited by 450
mTOR and autophagy: A dynamic relationship governed by nutrients and energy
Dunlop, E. A., & Tee, A. R. (2014) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2014.08.006 · Cited by 452
TFEB and TFE3: Linking Lysosomes to Cellular Adaptation to Stress
Raben, N., & Puertollano, R. (2016) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev-cellbio-111315-125407 · Cited by 437
The Emerging Role of Branched-Chain Amino Acids in Insulin Resistance and Metabolism
Yoon, M. (2016) · Nutrients · doi:10.3390/nu8070405 · Cited by 454
Goding, C. R., & Arnheiter, H. (2019) · Genes & Development · doi:10.1101/gad.324657.119 · Cited by 430
Mechanisms of autophagy–lysosome dysfunction in neurodegenerative diseases
Nixon, R. A., & Rubinsztein, D. C. (2024) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-024-00757-5 · Cited by 435
Lysosomal storage diseases: from pathophysiology to therapy
Parenti, G., Andria, G., & Ballabio, A. (2015) · Annual Review of Medicine · doi:10.1146/annurev-med-122313-085916 · Cited by 404
Nutrient signaling to mTOR and cell growth
Jewell, J. L., & Guan, K. (2013) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2013.01.004 · Cited by 420
A multiprotein supercomplex controlling oncogenic signalling in lymphoma
Phelan, J. D., Young, R. M., Webster, D. E., Roulland, S., Wright, G. W., Kasbekar, M., Shaffer, A. L., Ceribelli, M., Wang, J. Q., Schmitz, R., et al. (2018) · Nature · doi:10.1038/s41586-018-0290-0 · Cited by 416
Zhou, J., Tan, S.-H., Nicolas, V., Bauvy, C., Yang, N., Zhang, J., Xue, Y., Codogno, P., & Shen, H. (2013) · Cell Research · doi:10.1038/cr.2013.11 · Cited by 397
Clark, C. A., Gupta, H. B., Sareddy, G. R., Pandeswara, S., Lao, S., Yuan, B., Drerup, J. M., Padron, A. S., Conejo-Garcia, J. R., Murthy, K., et al. (2016) · Cancer Research · doi:10.1158/0008-5472.can-16-0258 · Cited by 403
Endocytosis and CancerPreprint
Mellman, I., & Yarden, Y. (2013) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a016949 · Cited by 402
A molecular mechanism to regulate lysosome motility for lysosome positioning and tubulation
Li, X., Rydzewski, N., Hider, A., Zhang, X., Yang, J., Wang, W., Gao, Q., Cheng, X., & Xu, H. (2016) · Nature Cell Biology · doi:10.1038/ncb3324 · Cited by 387
PtdIns(3,4,5) P 3-Dependent Activation of the mTORC2 Kinase Complex
Liu, P., Gan, W., Chin, Y. R., Ogura, K., Guo, J., Zhang, J., Wang, B., Blenis, J., Cantley, L. C., Toker, A., et al. (2015) · Cancer Discovery · doi:10.1158/2159-8290.cd-15-0460 · Cited by 403
Autophagy: An Essential Degradation Program for Cellular Homeostasis and Life
Chun, Y., & Kim, J. (2018) · Cells · doi:10.3390/cells7120278 · Cited by 396
Sarkar, S. (2013) · Biochemical Society Transactions · doi:10.1042/bst20130134 · Cited by 379
Autophagy, cancer stem cells and drug resistance
Smith, A. G., & Macleod, K. F. (2018) · The Journal of Pathology · doi:10.1002/path.5222 · Cited by 369
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
