Cited by 1,673PI3K/AKT/mTOR signaling in cancerAutophagy in Disease and TherapyMetabolism, Diabetes, and Cancer

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 access

Zoncu, Roberto, Bar-Peled, Liron, Efeyan, Alejo, Wang, Shuyu, Sancak, Yasemin, Sabatini, David M.·2011·Science

DOI 10.1126/science.1207056PMC PMC3211112

Open this paper in CoChat — free account

Abstract

Cellular sensing of amino acids occurs at the lysosome and is mediated by the vacuolar proton pump.

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 · 10.1126/science.1207056

Cites

26 of 26 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.

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-citation
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
Self-citation
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
Self-citation
Rheb GTPase is a direct target of TSC2 GAP activity and regulates mTOR signaling
Inoki, K., Li, Y., Xu, T., & Guan, K.-L. (2003) · Genes & Development · doi:10.1101/gad.1110003 · Cited by 1,911
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
Tuberous Sclerosis Complex Gene Products, Tuberin and Hamartin, Control mTOR Signaling by Acting as a GTPase-Activating Protein Complex toward Rheb
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

Show all 26 references

Sorted by citations

Items 501–600 of 1,003

The amino acid metabolite homocysteine activates mTORC1 to inhibit autophagy and form abnormal proteins in human neurons and mice
Khayati, K., Antikainen, H., Bonder, E. M., Weber, G. F., Kruger, W. D., Jakubowski, H., & Dobrowolski, R. (2016) · The FASEB Journal · doi:10.1096/fj.201600915r · Cited by 71
Age-induced reduction of autophagy-related gene expression is associated with onset of Alzheimer's disease.
Omata, Y., Lim, Y., Akao, Y., & Tsuda, L. (2014) · Europe PMC (PubMed Central) · Cited by 70
An intestinal zinc sensor regulates food intake and developmental growth
Redhai, S., Pilgrim, C., Gaspar, P., van Giesen, L., Lopes, T., Riabinina, O., Grenier, T., Milona, A., Chanana, B., Swadling, J. B., et al. (2020) · Nature · doi:10.1038/s41586-020-2111-5 · Cited by 70
Sublethal Levels of Antibiotics Promote Bacterial Persistence in Epithelial Cells
Liu, X., Liu, F., Ding, S., Shen, J., & Zhu, K. (2020) · Advanced Science · doi:10.1002/advs.201900840 · Cited by 72
The Inositol Phosphate System—A Coordinator of Metabolic Adaptability
Tu‐Sekine, B., & Kim, S. F. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23126747 · Cited by 72
mTOR direct interactions with Rheb-GTPase and raptor: sub-cellular localization using fluorescence lifetime imaging
Yadav, R. B., Burgos, P., Parker, A. W., Iadevaia, V., Proud, C. G., Allen, R. A., O’Connell, J. P., Jeshtadi, A., Stubbs, C. D., & Botchway, S. W. (2013) · BMC Cell Biology · doi:10.1186/1471-2121-14-3 · Cited by 71
The Golgi ribbon in mammalian cells negatively regulates autophagy by modulating mTOR activity
Gosavi, P., Houghton, F. J., McMillan, P. J., Hanssen, E. G., & Gleeson, P. A. (2018) · Journal of Cell Science · doi:10.1242/jcs.211987 · Cited by 66
Regulation of V-ATPase assembly and function of V-ATPases in tumor cell invasiveness
McGuire, C., Cotter, K., Stransky, L., & Forgac, M. (2016) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2016.02.010 · Cited by 70
MCRS1 Binds and Couples Rheb to Amino Acid-Dependent mTORC1 Activation
Fawal, M.-A., Brandt, M., & Djouder, N. (2015) · Developmental Cell · doi:10.1016/j.devcel.2015.02.010 · Cited by 70
The role of innate immunity in mucopolysaccharide diseases
Parker, H., & Bigger, B. (2018) · Journal of Neurochemistry · doi:10.1111/jnc.14632 · Cited by 72
Retromer and TBC1D5 maintain late endosomal RAB7 domains to enable amino acid-induced mTORC1 signaling
Kvainickas, A., Nägele, H., Qi, W., Dokládal, L., Jimenez-Orgaz, A., Stehl, L., Gangurde, D., Zhao, Q., Hu, Z., Dengjel, J., et al. (2019) · Journal of Cell Biology · doi:10.1083/jcb.201812110 · Cited by 75
ATP6V0A1 encoding the a1-subunit of the V0 domain of vacuolar H+-ATPases is essential for brain development in humans and mice
Aoto, K., Kato, M., Akita, T., Nakashima, M., Mutoh, H., Akasaka, N., Tohyama, J., Nomura, Y., Hoshino, K., Ago, Y., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-22389-5 · Cited by 70
Guidelines for the use and interpretation of assays for monitoring autophagy (3rd edition)
Klionsky, D. J., Abdelmohsen, K., Abe, A., Abedin, J., Abeliovich, H., Acevedo‐Arozena, A., Adachi, H., Adams, C. M., Adams, P. D., Adeli, K., et al. (2016) · Kölner Universitäts PublikationsServer (Universität zu Köln) · doi:10.5167/uzh-131237 · Cited by 69
Lysosome signaling in cell survival and programmed cell death for cellular homeostasis
Patra, S., Patil, S., Klionsky, D. J., & Bhutia, S. K. (2022) · Journal of Cellular Physiology · doi:10.1002/jcp.30928 · Cited by 69
ATP6V0C Knockdown in Neuroblastoma Cells Alters Autophagy-Lysosome Pathway Function and Metabolism of Proteins that Accumulate in Neurodegenerative Disease
Mangieri, L. R., Mader, B. J., Thomas, C. E., Taylor, C. A., Luker, A. M., Tse, T. E., Huisingh, C., & Shacka, J. J. (2014) · PLoS ONE · doi:10.1371/journal.pone.0093257 · Cited by 67
mTOR Signaling in Autophagy Regulation in the Kidney
Inoki, K. (2013) · Seminars in Nephrology · doi:10.1016/j.semnephrol.2013.11.002 · Cited by 71
Regulated Assembly of Vacuolar ATPase Is Increased during Cluster Disruption-induced Maturation of Dendritic Cells through a Phosphatidylinositol 3-Kinase/mTOR-dependent Pathway
Liberman, R. N., Bond, S., Shainheit, M. G., Stadecker, M. J., & Forgac, M. D. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.524561 · Cited by 69
Metabolic Vulnerabilities of Prostate Cancer: Diagnostic and Therapeutic OpportunitiesPreprint
Zadra, G., & Loda, M. F. (2017) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a030569 · Cited by 65
Pharmacologic inhibition of vacuolar H+ ATPase reduces physiologic and oncogenic Notch signaling
Kobia, F., Duchi, S., Deflorian, G., & Vaccari, T. (2013) · Molecular Oncology · doi:10.1016/j.molonc.2013.11.002 · Cited by 65
Spatial and functional separation of mTORC1 signalling in response to different amino acid sources
Fernandes, S., Angelidaki, D.-D., Nüchel, J., Pan, J., Gollwitzer, P., Elkis, Y., Artoni, F., Wilhelm, S., Kovacevic-Sarmiento, M., & Demetriades, C. (2024) · Nature Cell Biology · doi:10.1038/s41556-024-01523-7 · Cited by 69
The vacuolar H+ ATPase is a novel therapeutic target for glioblastoma
Cristofori, A. D., Ferrero, S., Bertolini, I., Gaudioso, G., Russo, M. V., Berno, V., Vanini, M., Locatelli, M., Zavanone, M. L., Rampini, P. M., et al. (2015) · Oncotarget · doi:10.18632/oncotarget.4239 · Cited by 68
Neuronal systems and circuits involved in the control of food intake and adaptive thermogenesis
Caron, A., & Richard, D. (2016) · Annals of the New York Academy of Sciences · doi:10.1111/nyas.13263 · Cited by 69
Impaired Cargo Clearance in the Retinal Pigment Epithelium (RPE) Underlies Irreversible Blinding Diseases
Keeling, E., Lotery, A. J., Tumbarello, D. A., & Ratnayaka, J. A. (2018) · Cells · doi:10.3390/cells7020016 · Cited by 72
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
Therapeutic Approaches in Lysosomal Storage Diseases
Fernández-Pereira, C., Millán, B. S., Gallardo‐Gómez, M., Pérez-Márquez, T., Alves-Villar, M., Melcón-Crespo, C., Fernández-Martín, J., & Ortolano, S. (2021) · Biomolecules · doi:10.3390/biom11121775 · Cited by 70
V-ATPase/mTOR Signaling Regulates Megalin-Mediated Apical Endocytosis
Gleixner, E. M., Canaud, G., Hermle, T. F., Guida, M. C., Kretz, O., Helmstädter, M., Huber, T. B., Eimer, S., Terzi, F., & Simons, M. (2014) · Cell Reports · doi:10.1016/j.celrep.2014.05.035 · Cited by 65
mTORC1-independent autophagy regulates receptor tyrosine kinase phosphorylation in colorectal cancer cells via an mTORC2-mediated mechanism
Lampada, A., O’Prey, J., Szabadkai, G., Ryan, K. M., Hochhauser, D., & Salomoni, P. (2017) · Cell Death and Differentiation · doi:10.1038/cdd.2017.41 · Cited by 66
The lysosomal TRPML1 channel regulates triple negative breast cancer development by promoting mTORC1 and purinergic signaling pathways
Xu, M., Almasi, S., Yang, Y., Yan, C. W., Sterea, A. M., Syeda, A. K. R., Shen, B. Q., Clements, D. R., Huang, P., Gujar, S. A., et al. (2019) · Cell Calcium · doi:10.1016/j.ceca.2019.02.010 · Cited by 70
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
Perspective: The Potential Role of Essential Amino Acids and the Mechanistic Target of Rapamycin Complex 1 (mTORC1) Pathway in the Pathogenesis of Child Stunting
Semba, R. D., Trehan, I., González‐Freire, M., Kraemer, K., Moaddel, R., Ordiz, M. I., Ferrucci, L., & MANARY, M. J. (2016) · Advances in Nutrition · doi:10.3945/an.116.013276 · Cited by 74
Transcription Factor EB Activation Rescues Advanced αB‐Crystallin Mutation‐Induced Cardiomyopathy by Normalizing Desmin Localization
Ma, X., Mani, K. M., Liu, H., Kovács, A. D., Murphy, J. T., Foroughi, L., French, B. A., Weinheimer, C. J., Kraja, A. T., Benjamin, I. J., et al. (2019) · Journal of the American Heart Association · doi:10.1161/jaha.118.010866 · Cited by 65
Regulation of Muscle Growth in Early Postnatal Life in a Swine Model
Rudar, M., Fiorotto, M. L., & Davis, T. A. (2018) · Annual Review of Animal Biosciences · doi:10.1146/annurev-animal-020518-115130 · Cited by 69
The mTOR–lysosome axis at the centre of ageing
Carosi, J. M., Fourrier, C., Bensalem, J., & Sargeant, T. J. (2021) · FEBS Open Bio · doi:10.1002/2211-5463.13347 · Cited by 70
mTOR signaling as a molecular target for the alleviation of Alzheimer's disease pathogenesis
Rapaka, D., Bitra, V. R., Challa, S. R., & Adiukwu, P. C. (2022) · Neurochemistry International · doi:10.1016/j.neuint.2022.105311 · Cited by 65
Hypertonic stress promotes autophagy and microtubule-dependent autophagosomal clusters
Nunes, P., Ernandez, T., Roth, I., Qiao, X., Strebel, D., Bouley, R., Charollais, A., Ramadori, P., Foti, M., Meda, P., et al. (2013) · Autophagy · doi:10.4161/auto.23662 · Cited by 67
Unbreak My Heart: Targeting Mitochondrial Autophagy in Diabetic Cardiomyopathy
Kubli, D. A., & Gustafsson, Å. B. (2015) · Antioxidants and Redox Signaling · doi:10.1089/ars.2015.6322 · Cited by 66
Evolutionarily conserved regulation of TOR signalling
Takahara, T., & Maeda, T. (2013) · The Journal of Biochemistry · doi:10.1093/jb/mvt047 · Cited by 64
The tumor susceptibility gene TMEM127 is mutated in renal cell carcinomas and modulates endolysosomal function
Qin, Y., Deng, Y., Ricketts, C. J., Srikantan, S., Wang, E., Maher, E. R., & Dahia, P. L. M. (2013) · Human Molecular Genetics · doi:10.1093/hmg/ddt638 · 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
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
Interpretation of bafilomycin, pH neutralizing or protease inhibitor treatments in autophagic flux experiments: Novel considerations
Juhász, G. (2012) · Autophagy · doi:10.4161/auto.21544 · Cited by 66
Rab5 Proteins Regulate Activation and Localization of Target of Rapamycin Complex 1
Bridges, D., Fisher, K., Zolov, S. N., Xiong, T., Inoki, K., Weisman, L. S., & Saltiel, A. R. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.334060 · Cited by 62
Ego3 Functions as a Homodimer to Mediate the Interaction between Gtr1-Gtr2 and Ego1 in the EGO Complex to Activate TORC1
Zhang, T., Gulli, M., Yang, H., VIRGILIO, C. D., & Ding, J. (2012) · Structure · doi:10.1016/j.str.2012.09.019 · Cited by 63
WAC Regulates mTOR Activity by Acting as an Adaptor for the TTT and Pontin/Reptin Complexes
David, G., Xu, Z., Rui, Y., Charng, W., Jaiswal, M., Yamamoto, S., Xiong, B., Zhang, K., Sandoval, H., Duraine, L., et al. (2016) · Developmental Cell · doi:10.1016/j.devcel.2015.12.019 · Cited by 69
Identification of modulators of autophagic flux in an image-based high content siRNA screen
Hale, C. M., Cheng, Q., Ortuno, D., Huang, M. X., Nojima, D., Kassner, P. D., Wang, S., Ollmann, M. M., & Carlisle, H. J. (2016) · Autophagy · doi:10.1080/15548627.2016.1147669 · Cited by 61
Self-citation
Autophagy and cancer cell metabolism
Anderson, C. M., & Macleod, K. F. (2019) · International review of cytology · doi:10.1016/bs.ircmb.2019.06.002 · Cited by 63
Oncogenic Rag GTPase signalling enhances B cell activation and drives follicular lymphoma sensitive to pharmacological inhibition of mTOR
Ortega-Molina, A., Deleyto-Seldas, N., Carreras, J., Sanz, A., Lebrero‐Fernández, C., Menéndez, C., Vandenberg, A., Fernández-Ruiz, B., Marín-Arraiza, L., Arregui, C. D. L. C., et al. (2019) · Nature Metabolism · doi:10.1038/s42255-019-0098-8 · Cited by 67
Self-citation
Regulation of mTORC1 by amino acids in mammalian cells: A general picture of recent advances
Zhang, S., Lin, X., Hou, Q., Hu, Z., Wang, Y., & Wang, Z. (2021) · Animal nutrition · doi:10.1016/j.aninu.2021.05.003 · Cited by 68
Cardiac macrophages and emerging roles for their metabolism after myocardial infarction
Thorp, E. B. (2023) · Journal of Clinical Investigation · doi:10.1172/jci171953 · Cited by 66
FK506, an Immunosuppressive Drug, Induces Autophagy by Binding to the V-ATPase Catalytic Subunit A in Neuronal Cells
Kim, D., Hwang, H., Kim, J. Y., Lee, J. Y., Yoo, J. S., Marko‐Varga, G., & Kwon, H. J. (2016) · Journal of Proteome Research · doi:10.1021/acs.jproteome.6b00638 · Cited by 59
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
Autophagy is required for G 1 /G 0 quiescence in response to nitrogen starvation in Saccharomyces cerevisiae
An, Z., Tassa, A., Thomas, C., Zhong, R. M., Xiao, G., Fotedar, R., Tu, B. P., Klionsky, D. J., & Levine, B. (2014) · Autophagy · doi:10.4161/auto.32122 · Cited by 62
Altered autophagic flux enhances inflammatory responses during inflammation-induced preterm labor
Agrawal, V., Jaiswal, M. K., Mallers, T. M., Katara, G. K., Gilman‐Sachs, A., Beaman, K. D., & Hirsch, E. (2015) · Scientific Reports · doi:10.1038/srep09410 · Cited by 61
Metabolic regulation of the cell cycle
Lee, I. H., & Finkel, T. (2013) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2013.07.002 · Cited by 63
Evidence-based support for the use of proton pump inhibitors in cancer therapy
Fais, S. (2015) · Journal of Translational Medicine · doi:10.1186/s12967-015-0735-2 · Cited by 61
The Journey of the Autophagosome through Mammalian Cell Organelles and Membranes
Molino, D., Zemirli, N., Codogno, P., & Morel, É. (2016) · Journal of Molecular Biology · doi:10.1016/j.jmb.2016.12.013 · Cited by 68
VAMP associated proteins are required for autophagic and lysosomal degradation by promoting a PtdIns4P-mediated endosomal pathway
Mao, D., Lin, G., Tepe, B., Zuo, Z., Tan, K. L., Şentürk, M., Zhang, S., Arenkiel, B. R., Sardiello, M., & Bellen, H. J. (2019) · Autophagy · doi:10.1080/15548627.2019.1580103 · Cited by 59
Target of Rapamycin in Control of Autophagy: Puppet Master and Signal Integrator
Mugume, Y., Kazibwe, Z., & Bassham, D. C. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21218259 · Cited by 62
Epidermal Growth Factor-induced Vacuolar (H+)-ATPase Assembly
Xu, Y., Parmar, A., Roux, E., Balbis, A., Dumas, V., Chevalier, S., & Posner, B. I. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.352229 · Cited by 59
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
Nutrients and growth factors in mTORC1 activation
Efeyan, A., & Sabatini, D. M. (2013) · Biochemical Society Transactions · doi:10.1042/bst20130063 · Cited by 59
Self-citation
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
Phagocytosis: Hungry, Hungry Cells
Gray, M. A., & Botelho, R. J. (2016) · Methods in molecular biology · doi:10.1007/978-1-4939-6581-6_1 · Cited by 59
Proton pump inhibition and cancer therapeutics: A specific tumor targeting or it is a phenomenon secondary to a systemic buffering?
Spugnini, E. P., & Fais, S. (2017) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2017.01.003 · Cited by 59
Molecular basis for the binding and modulation of V-ATPase by a bacterial effector protein
Zhao, J., Beyrakhova, K. A., Liu, Y., Alvarez, C., Bueler, S. A., Xu, L., Xu, C., Boniecki, M. T., Kanelis, V., Luo, Z., et al. (2017) · PLoS Pathogens · doi:10.1371/journal.ppat.1006394 · Cited by 60
Glucosamine promotes hepatitis B virus replication through its dual effects in suppressing autophagic degradation and inhibiting MTORC1 signaling
Lin, Y., Wu, C., Wang, X., Liu, S., Zhao, K., Kemper, T., Yu, H., Li, M., Zhang, J., Chen, M., et al. (2019) · Autophagy · doi:10.1080/15548627.2019.1632104 · Cited by 60
(Pro)renin Receptor Inhibition Reprograms Hepatic Lipid Metabolism and Protects Mice From Diet-Induced Obesity and Hepatosteatosis
Ren, L., Sun, Y., Lu, H., Ye, D., Han, L., Wang, N., Daugherty, A., Li, F., Wang, M., Su, F., et al. (2018) · Circulation Research · doi:10.1161/circresaha.117.312422 · Cited by 59
Pharmacology of metformin – An update
Glossmann, H. H., & Lutz, O. M. D. (2019) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2019.172782 · Cited by 62
Vacuolar H+-ATPase: An Essential Multitasking Enzyme in Physiology and Pathophysiology
Holliday, L. S. (2014) · New Journal of Science · doi:10.1155/2014/675430 · Cited by 60
Phosphofructokinases Axis Controls Glucose-Dependent mTORC1 Activation Driven by E2F1
Almacellas, E., Pelletier, J., Manzano, À., Gentilella, A., Ambrosio, S., Mauvezin, C., & Tauler, A. (2019) · iScience · doi:10.1016/j.isci.2019.09.040 · Cited by 59
Autophagy in Glomerular Health and Disease
Hartleben, B., Wanner, N., & Huber, T. B. (2013) · Seminars in Nephrology · doi:10.1016/j.semnephrol.2013.11.007 · Cited by 58
Mammalian target of rapamycin and the kidney. I. The signaling pathway
Lieberthal, W., & Levine, J. S. (2012) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00014.2012 · Cited by 58
Rag GTPase in amino acid signaling
Kim, J., & Kim, E. (2016) · Amino Acids · doi:10.1007/s00726-016-2171-x · Cited by 65
C9orf72 and smcr8 mutant mice reveal MTORC1 activation due to impaired lysosomal degradation and exocytosis
Shao, Q., Yang, M., Chen, L., Ma, L., Zhang, W., Jiang, Z., Luo, J., Lee, J., Liang, C., & Chen, J. (2019) · Autophagy · doi:10.1080/15548627.2019.1703353 · Cited by 62
Amino Acids Activate Mammalian Target of Rapamycin (mTOR) Complex 1 without Changing Rag GTPase Guanyl Nucleotide Charging
Oshiro, N., Rapley, J., & Avruch, J. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.528505 · Cited by 57
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
Specific amino acid supplementation rescues the heart from lipid overload-induced insulin resistance and contractile dysfunction by targeting the endosomal mTOR–v-ATPase axis
Wang, S., Schianchi, F., Neumann, D., Wong, L.-Y., Sun, A., van Nieuwenhoven, F. A., Zeegers, M. P., Strzelecka‐Kiliszek, A., Cöl, Ü., Glatz, J. F. C., et al. (2021) · Molecular Metabolism · doi:10.1016/j.molmet.2021.101293 · Cited by 59
Self-citation
Phosphoinositide 3-kinase (PI3K) classes: From cell signaling to endocytic recycling and autophagy
Safaroghli‐Azar, A., Sanaei, M., Pourbagheri‐Sigaroodi, A., & Bashash, D. (2023) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2023.175827 · Cited by 60
Lysosomal pH Plays a Key Role in Regulation of mTOR Activity in Osteoclasts
Hu, Y., Carraro‐Lacroix, L. R., Wang, A., Owen, C., Bajenova, E., Corey, P., Brumell, J. H., & Voronov, I. (2015) · Journal of Cellular Biochemistry · doi:10.1002/jcb.25287 · Cited by 58
The I-BAR protein Ivy1 is an effector of the Rab7 GTPase Ypt7 involved in vacuole membrane homeostasis
Numrich, J., Gulli, M., Arlt, H., Sardu, A., Griffith, J. M., Levine, T. P., Engelbrecht-Vandré, S., Reggiori, F., VIRGILIO, C. D., & Ungermann, C. (2015) · Journal of Cell Science · doi:10.1242/jcs.164905 · Cited by 57
Imaging the electrical activity of organelles in living cells
Matamala, E., Castillo, C., Vivar, J. P., Rojas, P. A., & Brauchi, S. E. (2021) · Communications Biology · doi:10.1038/s42003-021-01916-6 · Cited by 56
Lysosomal Ion Channels: What Are They Good For and Are They Druggable Targets?
Riederer, E. A., Cang, C., & Ren, D. (2022) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev-pharmtox-051921-013755 · Cited by 58
Excessive Leucine-mTORC1-Signalling of Cow Milk-Based Infant Formula: The Missing Link to Understand Early Childhood Obesity
Melnik, B. C. (2012) · Journal of Obesity · doi:10.1155/2012/197653 · Cited by 57
Iron depletion suppresses mTORC1-directed signalling in intestinal Caco-2 cells via induction of REDD1
Watson, A., Lipina, C., McArdle, H. J., Taylor, P. M., & Hundal, H. S. (2016) · Cellular Signalling · doi:10.1016/j.cellsig.2016.01.014 · 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
Loss of CLN7 results in depletion of soluble lysosomal proteins and impaired mTOR reactivation
Danyukova, T., Ariunbat, K., Thelen, M., Brocke‐Ahmadinejad, N., Mole, S., & Storch, S. (2018) · Human Molecular Genetics · doi:10.1093/hmg/ddy076 · Cited by 56
Connecting lysosomes and mitochondria – a novel role for lipid metabolism in cancer cell death
Bartel, K., Pein, H., Popper, B., Schmitt, S., Janaki‐Raman, S., Schulze, A., Lengauer, F., Koeberle, A., Werz, O., Zischka, H., et al. (2019) · Cell Communication and Signaling · doi:10.1186/s12964-019-0399-2 · Cited by 56
Depalmitoylation by Palmitoyl-Protein Thioesterase 1 in Neuronal Health and Degeneration
Koster, K. P., & Yoshii, A. (2019) · Frontiers in Synaptic Neuroscience · doi:10.3389/fnsyn.2019.00025 · Cited by 55
Manifestations of Age on Autophagy, Mitophagy and Lysosomes in Skeletal Muscle
Triolo, M., & Hood, D. A. (2021) · Cells · doi:10.3390/cells10051054 · Cited by 60
Inositol polyphosphate multikinase signaling in the regulation of metabolism
Lee, J., Kim, Y., Park, J., & Kim, S. (2012) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2012.06725.x · Cited by 56
The yeast protein kinase Sch9 adjusts V-ATPase assembly/disassembly to control pH homeostasis and longevity in response to glucose availability
Wilms, T., Swinnen, E., Eskes, E., Edo, L. D., Uwineza, A., Essche, R. V., Rosseels, J., Zabrocki, P., Cameroni, E., Franssens, V., et al. (2017) · PLoS Genetics · doi:10.1371/journal.pgen.1006835 · Cited by 57
Regulation of V-ATPase Assembly in Nutrient Sensing and Function of V-ATPases in Breast Cancer Metastasis
Collins, M. P., & Forgac, M. D. (2018) · Frontiers in Physiology · doi:10.3389/fphys.2018.00902 · Cited by 59
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
Lysosome (Dys)function in Atherosclerosis—A Big Weight on the Shoulders of a Small Organelle
Marques, A. R. A., Ramos, C., Machado-Oliveira, G., & Vieira, O. V. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.658995 · Cited by 53
Phosphoinositides: Key modulators of energy metabolism
Bridges, D., & Saltiel, A. R. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2014.11.008 · Cited by 56
Current Models of Mammalian Target of Rapamycin Complex 1 (mTORC1) Activation by Growth Factors and Amino Acids
Zheng, X., Liang, Y., He, Q., Yao, R., Bao, W., Bao, L., Wang, Y., & Wang, Z. (2014) · International Journal of Molecular Sciences · doi:10.3390/ijms151120753 · Cited by 54
Beyond starvation: An update on the autophagic machinery and its functions
Kawabata, T., & Yoshimori, T. (2015) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2015.12.005 · Cited by 56
Autophagy in cardiomyopathies
Zech, A. T. L., Singh, S. R., Schlossarek, S., & Carrier, L. (2019) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2019.01.013 · Cited by 56

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.
ORCID: Zoncu, Roberto
Efeyan, Alejo
Wang, Shuyu
Sancak, Yasemin
Sabatini, David M.
Venue: Science
Publisher: American Association for the Advancement of Science (AAAS)
Published: 2011-11-04
Volume: 334
Issue: 6056
Pages: 678-683
ISSN: 0036-8075 (ISSN-L)
1095-9203
DOI: 10.1126/science.1207056
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

mTORC1 Senses Lysosomal Amino Acids Through an Inside-Out Mechanism That Requires the Vacuolar H + -ATPase

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