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mTOR at the nexus of nutrition, growth, ageing and disease
Open accessAbstract
The mTOR pathway integrates a diverse set of environmental cues, such as growth factor signals and nutritional status, to direct eukaryotic cell growth. Over the past two and a half decades, mapping of the mTOR signalling landscape has revealed that mTOR controls biomass accumulation and metabolism by modulating key cellular processes, including protein synthesis and autophagy. Given the pathway's central role in maintaining cellular and physiological homeostasis, dysregulation of mTOR signalling has been implicated in metabolic disorders, neurodegeneration, cancer and ageing. In this Review, we highlight recent advances in our understanding of the complex regulation of the mTOR pathway and discuss its function in the context of physiology, human disease and pharmacological intervention.
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“a notable feature of effective anti-aging interventions, such as lowered insulin/IGF-1 signaling 296 and disruption of the TORC1 complex 296,297 , is the diverse mechanisms by which they target different aging hallmarks in different tissues to maintain healthspan of the whole organism.”
From Hallmarks of aging: An expanding universe (2023) · cites this paper as [296]
In the citing paper
“Conversely, during protein breakdown, the amino acids released by lysosome and proteasome directly stimulate mTOR5 and therefore, protein synthesis might increase during muscle atrophy.”
From Mechanisms of muscle atrophy and hypertrophy: implications in health and disease (2021) · cites this paper as [5]
In the citing paper
“This kinase integrates multiple stimuli coming not only from hormones but also from cytokines, nutrients, ATP/AMP ratio, and signals to the translation machinery via p70S6K1, which controls the ribosomal protein S6, and factor 4E binding protein 1 (4EBP1), which negatively regulates the ribosomal eukaryotic translation initiator factor 4E5.”
From Mechanisms of muscle atrophy and hypertrophy: implications in health and disease (2021) · cites this paper as [5]
In the citing paper
“While mTORC2 is related to glucose and lipids homeostasis5, mTORC1 regulates several anabolic processes, including protein synthesis, ribosome, and mitochondria biogenesis.”
From Mechanisms of muscle atrophy and hypertrophy: implications in health and disease (2021) · cites this paper as [5]
In the citing paper
“Amino acids, especially the branched ones, are well-known growth-promoting agents because they directly stimulate mTOR5.”
From Mechanisms of muscle atrophy and hypertrophy: implications in health and disease (2021) · cites this paper as [5]
In the citing paper
“The mTOR kinase is part of the multiprotein complexes mTORC1 and mTORC2, which participate in the sensing of high amino acid concentrations and regulate multiple aspects of anabolic metabolism.219”
From Meta-hallmarks of aging and cancer (2023) · cites this paper as [219]
In the citing paper
“Hamartin (encoded by TSC1)–tuberin (encoded by TSC2) complexes negatively regulate mTORC1 by inhibiting GTP binding protein RHEB”
From Autophagy in kidney homeostasis and disease (2020) · cites this paper as [15]
In the citing paper
“mTORC1 is a master regulator of autophagy that is activated by amino acids or growth factors, such as insulin and insulin-like growth factor-1”
From Autophagy in kidney homeostasis and disease (2020) · cites this paper as [15]
In the citing paper
“Under nutrient-rich conditions, active mTORC1 suppresses autophagy by phosphorylating ULK1 and ATG13 to inhibit the ULK1–ULK2 complex.”
From Autophagy in kidney homeostasis and disease (2020) · cites this paper as [15]
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Items 201–286 of 286
GCN2 sustains mTORC1 suppression upon amino acid deprivation by inducing Sestrin2Preprint
Ye, J., Palm, W., Peng, M., King, B., Lindsten, T., Li, M. O., Koumenis, C., & Thompson, C. B. (2015) · Genes & Development · doi:10.1101/gad.269324.115 · Cited by 285
Wagle, N., Grabiner, B. C., Allen, E. M. V., Hodis, E., Jacobus, S. J., Supko, J. G., Stewart, M. L., Choueiri, T. K., Gandhi, L., Cleary, J. M., et al. (2014) · Cancer Discovery · doi:10.1158/2159-8290.cd-13-0353 · Cited by 282
Self-citationModulation of Autophagy by BDNF Underlies Synaptic Plasticity
Nikoletopoulou, V., Sidiropoulou, K., Kallergi, E., Dalezios, Y., & Tavernarakis, N. (2017) · Cell Metabolism · doi:10.1016/j.cmet.2017.06.005 · Cited by 280
Rac1 Regulates the Activity of mTORC1 and mTORC2 and Controls Cellular Size
Saci, A., Cantley, L. C., & Carpenter, C. L. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.03.017 · Cited by 275
Inhibition of mTOR Signaling in Parkinson’s Disease Prevents l -DOPA–Induced Dyskinesia
Santini, E., Heiman, M., Greengard, P., Valjent, E., & Fisone, G. (2009) · Science Signaling · doi:10.1126/scisignal.2000308 · Cited by 272
Transcriptional activation of RagD GTPase controls mTORC1 and promotes cancer growth
Malta, C. D., Siciliano, D., Calcagnì, A., Monfregola, J., Punzi, S., Pastore, N., Eastes, A., Davis, O. B., Cegli, R. D., Zampelli, A., et al. (2017) · Science · doi:10.1126/science.aag2553 · Cited by 246
Thomanetz, V., Angliker, N., Cloëtta, D., Lustenberger, R. M., Schweighauser, M., Oliveri, F., 昇, 鈴., & Rüegg, M. A. (2013) · The Journal of Cell Biology · doi:10.1083/jcb.201205030 · Cited by 233
AMPK directly activates mTORC2 to promote cell survival during acute energetic stress
Kazyken, D., Magnuson, B., Bodur, Ç., Acosta-Jaquez, H. A., Zhang, D., Tong, X., Barnes, T. M., Steinl, G. K., Patterson, N., Altheim, C. H., et al. (2019) · Science Signaling · doi:10.1126/scisignal.aav3249 · Cited by 226
Peng, M., Yin, N., & Li, M. O. (2014) · Cell · doi:10.1016/j.cell.2014.08.038 · Cited by 220
Recurrent mTORC1-activating RRAGC mutations in follicular lymphoma
Okosun, J., Wolfson, R. L., Wang, J., Araf, S., Wilkins, L., Castellano, B. M., Escudero‐Ibarz, L., Seraihi, A. A., Richter, J., Bernhart, S. H., et al. (2015) · Nature Genetics · doi:10.1038/ng.3473 · Cited by 220
Self-citationEvidence for Direct Activation of mTORC2 Kinase Activity by Phosphatidylinositol 3,4,5-Trisphosphate
Gan, X., Wang, J., Su, B., & Wu, D. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.195016 · Cited by 217
Localization of mTORC2 activity inside cells
Ebner, M., Sinkovics, B., Szczygieł, M., Ribeiro, D. W., & Yudushkin, I. A. (2017) · The Journal of Cell Biology · doi:10.1083/jcb.201610060 · Cited by 214
Structural basis for the docking of mTORC1 on the lysosomal surface
Rogala, K. B., Gu, X., Kedir, J. F., Abu-Remaileh, M., Bianchi, L. F., Bottino, A. M. S., Dueholm, R., Niehaus, A., Overwijn, D., Fils, A.-C. P., et al. (2019) · Science · doi:10.1126/science.aay0166 · Cited by 214
Self-citationmTORC2 Regulates Neutrophil Chemotaxis in a cAMP- and RhoA-Dependent Fashion
Liu, L., Das, S., Losert, W., & Parent, C. A. (2010) · Developmental Cell · doi:10.1016/j.devcel.2010.11.004 · Cited by 208
Woo, S.-Y., Kim, D., Jun, C., Kim, Y. M., Haar, E. V., Lee, S.-I., Hegg, J. W., Bandhakavi, S., Griffin, T. J., & Kim, D. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m704343200 · Cited by 206
The mTORC1 Signaling Network Senses Changes in Cellular Purine Nucleotide Levels
Hoxhaj, G., Hallett, J. E. H., Timson, R. C., Ilagan, E., Yuan, M., Asara, J. M., Ben‐Sahra, I., & Manning, B. D. (2017) · Cell Reports · doi:10.1016/j.celrep.2017.10.029 · Cited by 203
Stracka, D., Jozefczuk, S., Rudroff, F., Sauer, U., & Hall, M. N. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.574335 · Cited by 196
Shor, B., Wu, J., Shakey, Q., Toral‐Barza, L., Shi, C., Follettie, M. T., & Yu, K. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.071639 · Cited by 195
SZT2 dictates GATOR control of mTORC1 signalling
Peng, M., Yin, N., & Li, M. O. (2017) · Nature · doi:10.1038/nature21378 · Cited by 192
Architecture of the human GATOR1 and GATOR1–Rag GTPases complexes
Shen, K., Huang, R. K., Brignole, E. J., Condon, K. J., Valenstein, M. L., Chantranupong, L., Bomaliyamu, A., Choe, A., Hong, C., Yu, Z., et al. (2018) · Nature · doi:10.1038/nature26158 · Cited by 192
Self-citationmTORC1 Directly Phosphorylates and Regulates Human MAF1
Michels, A. A., Robitaille, A. M., Buczynski-Ruchonnet, D., Hodroj, W., Reina, J. H., Hall, M. N., & Hernandez, N. (2010) · Molecular and Cellular Biology · doi:10.1128/mcb.00319-10 · Cited by 189
mTOR Signaling in Epilepsy: Insights from Malformations of Cortical DevelopmentPreprint
Crino, P. B. (2015) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a022442 · Cited by 188
Carroll, B., Nelson, G., Rabanal‐Ruiz, Y., Kucheryavenko, O., Dunhill-Turner, N. A., Chesterman, C. C., Zahari, Q., Zhang, T., Conduit, S. E., Mitchell, C. A., et al. (2017) · The Journal of Cell Biology · doi:10.1083/jcb.201610113 · Cited by 188
Arriola Apelo, S. I., Neuman, J. C., Baar, E. L., Syed, F. A., Cummings, N. E., Brar, H. K., Pumper, C. P., Kimple, M. E., & Lamming, D. W. (2016) · Aging Cell · doi:10.1111/acel.12405 · Cited by 182
Involvement of GATOR complex genes in familial focal epilepsies and focal cortical dysplasia
Weckhuysen, S., Marsan, E., Lambrecq, V., Marchal, C., Morin‐Brureau, M., An-Gourfinkel, I., Baulac, M., Fohlen, M., Zetchi, C. K., Seeck, M., et al. (2016) · Epilepsia · doi:10.1111/epi.13391 · Cited by 181
Systematic analysis of ribophagy in human cells reveals bystander flux during selective autophagy
An, H., & Harper, J. W. (2018) · Nature Cell Biology · doi:10.1038/s41556-017-0007-x · Cited by 181
A Kinase Inhibitor Targeted to mTORC1 Drives Regression in Glioblastoma
Fan, Q., Aksoy, O., Wong, R. A., Ilkhanizadeh, S., Novotny, C. J., Gustafson, W. C., Truong, A. Y.-Q., Cayanan, G., Simonds, E. F., Haas-Kogan, D., et al. (2017) · Cancer Cell · doi:10.1016/j.ccell.2017.01.014 · Cited by 180
Rapamycin and Alzheimer’s disease: Time for a clinical trial?
Kaeberlein, M. R., & Galván, V. (2019) · Science Translational Medicine · doi:10.1126/scitranslmed.aar4289 · Cited by 171
Ragulator and SLC38A9 activate the Rag GTPases through noncanonical GEF mechanisms
Shen, K., & Sabatini, D. M. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1811727115 · Cited by 165
Self-citationHuman brain tumor xenografts in nude mice as a chemotherapy model
Houchens, D. P., Ovejera, A. A., Riblet, S. M., & Slagel, D. E. (1983) · European Journal of Cancer and Clinical Oncology · doi:10.1016/0277-5379(83)90012-3 · Cited by 164
Yuan, M., Pino, E. C., Wu, L., Kacergis, M. C., & Soukas, A. A. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.386854 · Cited by 163
Valvezan, A. J., Turner, M., Belaïd, A., Lam, H. C., Miller, S. K., McNamara, M. C., Baglini, C. V., Housden, B. E., Perrimon, N., Kwiatkowski, D. J., et al. (2017) · Cancer Cell · doi:10.1016/j.ccell.2017.09.013 · Cited by 163
Lysosomal recruitment of TSC2 is a universal response to cellular stress
Demetriades, C., Plescher, M., & Teleman, A. A. (2016) · Nature Communications · doi:10.1038/ncomms10662 · Cited by 160
The Functional Proximal Proteome of Oncogenic Ras Includes mTORC2
Kovalski, J. R., Bhaduri, A., Zehnder, A. M., Neela, P. H., Che, Y., Wozniak, G. G., & Khavari, P. A. (2019) · Molecular Cell · doi:10.1016/j.molcel.2018.12.001 · Cited by 154
Direct stimulation of NADP + synthesis through Akt-mediated phosphorylation of NAD kinase
Hoxhaj, G., Ben‐Sahra, I., Lockwood, S. E., Timson, R. C., Byles, V., Henning, G. T., Gao, P., Selfors, L. M., Asara, J. M., & Manning, B. D. (2019) · Science · doi:10.1126/science.aau3903 · Cited by 150
You, J.-S., Mcnally, R. M., Jacobs, B. L., Privett, R. E., Gundermann, D. M., Lin, K.-H., Steinert, N. D., Goodman, C. A., & Hornberger, T. A. (2019) · The FASEB Journal · doi:10.1096/fj.201801653rr · Cited by 149
Inactivation of mTORC1 in the Developing Brain Causes Microcephaly and Affects Gliogenesis
Cloëtta, D., Thomanetz, V., Baranek, C., Lustenberger, R. M., Lin, S., Oliveri, F., Atanasoski, S., & Rüegg, M. A. (2013) · Journal of Neuroscience · doi:10.1523/jneurosci.3294-12.2013 · Cited by 145
Purine Nucleotide Availability Regulates mTORC1 Activity through the Rheb GTPase
Emmanuel, N., Ragunathan, S., Shan, Q., Wang, F., Giannakou, A., Huser, N. H., Jin, G., Myers, J. S., Abraham, R. T., & Ünsal-Kaçmaz, K. (2017) · Cell Reports · doi:10.1016/j.celrep.2017.05.043 · Cited by 145
mTORC1 Promotes Metabolic Reprogramming by the Suppression of GSK3-dependent Foxk1 Phosphorylation
He, L., Gomes, A. P., Wang, X., Yoon, S. O., Lee, G., Nagiec, M. J., Cho, S., Chavez, A., Islam, T., Yu, Y., et al. (2018) · Molecular Cell · doi:10.1016/j.molcel.2018.04.024 · Cited by 145
A recollection of mTOR signaling in learning and memoryPreprint
Graber, T. E., McCamphill, P. K., & Sossin, W. S. (2013) · Learning & Memory · doi:10.1101/lm.027664.112 · Cited by 143
The tumor suppressor FLCN mediates an alternate mTOR pathway to regulate browning of adipose tissuePreprint
Wada, S., Neinast, M. D., Jang, C., Ibrahim, Y. H., Lee, G., Babu, A., Li, J., Hoshino, A., Rowe, G. C., Rhee, J., et al. (2016) · Genes & Development · doi:10.1101/gad.287953.116 · Cited by 141
Cryo-EM structure of human mTOR complex 2
Chen, X., Liu, M., Tian, Y., Li, J., Qi, Y., Zhao, D., Wu, Z., Huang, M., Wong, C. C. L., Wang, H., et al. (2018) · Cell Research · doi:10.1038/s41422-018-0029-3 · Cited by 138
Intermittent Administration of Rapamycin Extends the Life Span of Female C57BL/6J Mice
Apelo, S. I. A., Pumper, C. P., Baar, E. L., Richardson, N. E., & Lamming, D. W. (2016) · The Journals of Gerontology Series A · doi:10.1093/gerona/glw064 · Cited by 136
Puffenberger, E. G., Strauss, K. A., Ramsey, K. M., Craig, D. W., Stephan, D. A., Robinson, D. L., Hendrickson, C., Gottlieb, S., Ramsay, D. A., Siu, V. M., et al. (2007) · Brain · doi:10.1093/brain/awm100 · Cited by 131
Urano, J., Tabancay, A. P., Yang, W., & Tamanoi, F. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.15.11198 · Cited by 128
EPRS is a critical mTORC1–S6K1 effector that influences adiposity in mice
Arif, A., Terenzi, F., Potdar, A. A., Jia, J., Sacks, J., China, A., Halawani, D., Vasu, K., Li, X., Brown, J. M., et al. (2017) · Nature · doi:10.1038/nature21380 · Cited by 128
Lipid sensing by mTOR complexes via de novo synthesis of phosphatidic acid
Menon, D., Salloum, D., Bernfeld, E., Sher, E. F., Akselrod, A., Frías, M. A., Sudderth, J., Chen, P.-H., DeBerardinis, R. J., & Foster, D. A. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.772988 · Cited by 127
Dynamics of mTORC1 activation in response to amino acids
Manifava, M., Smith, M. D., Rotondo, S., Walker, S. A., Niewczas, I. S., Zoncu, R., Clark, J. P., & Ktistakis, N. T. (2016) · eLife · doi:10.7554/elife.19960 · Cited by 123
Raptor/mTORC1 loss in adipocytes causes progressive lipodystrophy and fatty liver disease
Lee, P. L., Tang, Y., Li, H., & Guertin, D. A. (2016) · Molecular Metabolism · doi:10.1016/j.molmet.2016.04.001 · Cited by 118
Yuskaitis, C. J., Jones, B. M., Wolfson, R. L., Super, C. E., Dhamne, S. C., Rotenberg, A., Sabatini, D. M., Şahin, M., & Poduri, A. (2017) · Neurobiology of Disease · doi:10.1016/j.nbd.2017.12.010 · Cited by 116
Self-citationAn mTORC1-to-CDK1 Switch Maintains Autophagy Suppression during Mitosis
Odle, R., Walker, S. A., Oxley, D., Kidger, A. M., Balmanno, K., Gilley, R., Okkenhaug, H., Florey, O., Ktistakis, N. T., & Cook, S. J. (2019) · Molecular Cell · doi:10.1016/j.molcel.2019.10.016 · Cited by 113
Lysosomal Signaling Licenses Embryonic Stem Cell Differentiation via Inactivation of Tfe3
Villegas, F., Lehalle, D., Mayer, D., Rittirsch, M., Stadler, M. B., Zinner, M., Olivieri, D., Vabres, P., Duplomb-Jego, L., De Bont, E. S. J. M., et al. (2019) · Cell Stem Cell · doi:10.1016/j.stem.2018.11.021 · Cited by 110
mTORC2 phosphorylates protein kinase Cζ to regulate its stability and activity
Li, X., & Gao, T. (2013) · EMBO Reports · doi:10.1002/embr.201338119 · Cited by 107
Shen, K., Choe, A., & Sabatini, D. M. (2017) · Molecular Cell · doi:10.1016/j.molcel.2017.09.026 · Cited by 101
Self-citationGhobrial, I. M., Siegel, D. S. D., Vij, R., Berdeja, J. G., Richardson, P. G. G., Neuwirth, R. B., Patel, C. G., Zohren, F., & Wolf, J. L. (2016) · American Journal of Hematology · doi:10.1002/ajh.24300 · Cited by 100
Mieulet, V., Roceri, M., Espeillac, C., Sotiropoulos, A., Ohanna, M., Oorschot, V., Klumperman, J., Sandri, M., & Pende, M. (2007) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00499.2006 · Cited by 99
Hybrid Structure of the RagA/C-Ragulator mTORC1 Activation Complex
Su, M.-Y., Morris, K. L., Kim, D. J., Fu, Y., Lawrence, R. E., Stjepanović, G., Zoncu, R., & Hurley, J. H. (2017) · Molecular Cell · doi:10.1016/j.molcel.2017.10.016 · Cited by 96
Jacobs, B. L., You, J., Frey, J. W., Goodman, C. A., Gundermann, D. M., & Hornberger, T. A. (2013) · The Journal of Physiology · doi:10.1113/jphysiol.2013.256339 · Cited by 91
Hao, F., Kondo, K., Itoh, T., Ikari, S., Nada, S., Okada, M., & Noda, T. (2018) · Journal of Cell Science · doi:10.1242/jcs.208017 · Cited by 91
Naito, T., Kuma, A., & Mizushima, N. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.456228 · Cited by 88
Sestrin modulator NV-5138 produces rapid antidepressant effects via direct mTORC1 activation
Kato, T., Pothula, S., Liu, R.-J., Duman, C. H., Terwilliger, R., Vlasuk, G. P., Saiah, E., Hahm, S., & Duman, R. S. (2019) · Journal of Clinical Investigation · doi:10.1172/jci126859 · Cited by 88
Biallelic SZT2 Mutations Cause Infantile Encephalopathy with Epilepsy and Dysmorphic Corpus Callosum
Basel‐Vanagaite, L., Hershkovitz, T., Heyman, E., Raspall‐Chaure, M., Kakar, N., Smirin‐Yosef, P., Vila‐Pueyo, M., Kornreich, L., Thiele, H., Bode, H., et al. (2013) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2013.07.005 · Cited by 87
Molecular Architecture and Function of the SEA Complex, a Modulator of the TORC1 Pathway
Algret, R., Fernández-Martı́nez, J., Shi, Y., Kim, S. J., Pellarin, R., Cimermančič, P., Cochet, E., Šali, A., Chait, B. T., Rout, M. P., et al. (2014) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m114.039388 · Cited by 87
Architecture of the human mTORC2 core complex
Stuttfeld, E., Aylett, C. H. S., Imseng, S., Boehringer, D., Scaiola, A., Sauer, E., Hall, M. N., Maier, T., & Ban, N. (2018) · eLife · doi:10.7554/elife.33101 · Cited by 86
TORC1‐dependent epilepsy caused by acute biallelic Tsc1 deletion in adult mice
Abs, E., Goorden, S. M. I., Schreiber, J., Overwater, I. E., Hoogeveen‐Westerveld, M., Bruinsma, C. F., Aganović, E., Borgesius, N. Z., Nellist, M. D., & Elgersma, Y. (2013) · Annals of Neurology · doi:10.1002/ana.23943 · Cited by 83
Endoplasmic reticulum stress-mediated induction of SESTRIN 2 potentiates cell survival
Saveljeva, S., Cleary, P., Mnich, K., Ayo, A., Pakos‐Zebrucka, K., Patterson, J. B., Logue, S. E., & Samali, A. (2016) · Oncotarget · doi:10.18632/oncotarget.7601 · Cited by 83
Two distinct mTORC2-dependent pathways converge on Rac1 to drive breast cancer metastasis
Joly, M. M., Williams, M. M., Hicks, D. J., Jones, B. A., Sanchez, V. M., Young, C. D., Sarbassov, D. D., Muller, W. J., Brantley‐Sieders, D. M., & Cook, R. S. (2017) · Breast Cancer Research · doi:10.1186/s13058-017-0868-8 · Cited by 83
Brandt, C., Hillmann, P., Noack, A., Römermann, K., Öhler, L. A., Rageot, D., Beaufils, F., Melone, A., Sele, A., Wymann, M. P., et al. (2018) · Neuropharmacology · doi:10.1016/j.neuropharm.2018.08.002 · Cited by 83
TOR Signaling in Fission Yeast
Otsubo, Y., & Yamamato, M. (2008) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.1080/10409230802254911 · Cited by 80
Reijnders, M. R. F., Kousi, M., van Woerden, G. M., Klein, M., Bralten, J., Mancini, G. M. S., van Essen, T., Proietti-Onori, M., Smeets, E. E. J., van Gastel, M., et al. (2017) · Nature Communications · doi:10.1038/s41467-017-00933-6 · Cited by 76
Senoo, H., Kamimura, Y., Kimura, R., Nakajima, A., Sawai, S., Sesaki, H., & Iijima, M. (2019) · Nature Cell Biology · doi:10.1038/s41556-019-0348-8 · Cited by 76
Arg-78 of Nprl2 catalyzes GATOR1-stimulated GTP hydrolysis by the Rag GTPases
Shen, K., Valenstein, M. L., Gu, X., & Sabatini, D. M. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ac119.007382 · Cited by 70
Self-citationA role for Raptor phosphorylation in the mechanical activation of mTOR signaling
Frey, J. W., Jacobs, B. L., Goodman, C. A., & Hornberger, T. A. (2013) · Cellular Signalling · doi:10.1016/j.cellsig.2013.11.009 · Cited by 65
Hemolymph Amino Acid Analysis of Individual Drosophila Larvae
Piyankarage, S. C., Augustin, H., Grosjean, Y., Featherstone, D. E., & Shippy, S. A. (2008) · Analytical Chemistry · doi:10.1021/ac701785z · Cited by 64
Crystal structure of arginine-bound lysosomal transporter SLC38A9 in the cytosol-open state
Lei, H., Ma, J., Martinez, S. S., & Gonen, T. (2018) · Nature Structural & Molecular Biology · doi:10.1038/s41594-018-0072-2 · Cited by 63
The SIN1-PH Domain Connects mTORC2 to PI3K
Yuan, H., & Guan, K. (2015) · Cancer Discovery · doi:10.1158/2159-8290.cd-15-1125 · Cited by 57
Henry, F. E., Hockeimer, W., Chen, A., Mysore, S. P., & Sutton, M. A. (2017) · Molecular Brain · doi:10.1186/s13041-017-0330-y · Cited by 56
The small GTPases Ras and Rap1 bind to and control TORC2 activity
Khanna, A., Lotfi, P., Chavan, A. J., Montaño, N. M., Bolourani, P., Weeks, G., Shen, Z., Briggs, S. P., Pots, H., Haastert, P. J. M. V., et al. (2016) · Scientific Reports · doi:10.1038/srep25823 · Cited by 55
Hwang, Y., Kim, L. C., Song, W., Edwards, D. N., Cook, R. S., & Chen, J. (2019) · Cancer Research · doi:10.1158/0008-5472.can-18-3658 · Cited by 54
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Metadata
- Authors
- Liu, G. Y., & Sabatini, D. M.
- Affiliations
- Broad Institute (US)
- Corresponding author
- Sabatini, David M.
- Venue
- Nature Reviews Molecular Cell Biology
- Published
- 2020-01-14
- Volume
- 21
- Issue
- 4
- Pages
- 183-203
- ISSN
- 1471-0072 (ISSN-L)
- 1471-0080
- PMC
- PMC7102936
- OpenAlex
- W2999421965
- Cited by
- 2,737
- References
- 287
- Citations by year
- 2026: 356 · 2025: 469 · 2024: 462 · 2023: 447 · 2022: 436 · 2021: 412 · 2020: 152
- FWCI
- 34.98
- Type
- journal article
- Language
- en
- Update notices
- correction (2020-01-31)
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Nature Reviews Molecular Cell Biology (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- DSpace@MIT (Massachusetts Institute of Technology) (submittedVersion, cc-by-nc-sa)
- Funders
- National Cancer Institute (R01CA103866, R01CA129105, F31CA232340)
- National Institute of General Medical Sciences (T32GM007287)
- National Institute of Allergy and Infectious Diseases (R37AI047389)
- 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
- mTOR signaling, nutrient sensing, cell growth, protein synthesis, autophagy, metabolic homeostasis, aging, neurodegeneration, cancer, metabolic disorders
- MeSH terms
- Aging, Animals, Autophagy, Humans, Metabolic Diseases, Neoplasms, Nutritional Status, Protein Biosynthesis, Signal Transduction, TOR Serine-Threonine Kinases
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