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Nutrient sensing and TOR signaling in yeast and mammals
Open accessAbstract
Coordinating cell growth with nutrient availability is critical for cell survival. The evolutionarily conserved TOR (target of rapamycin) controls cell growth in response to nutrients, in particular amino acids. As a central controller of cell growth, mTOR (mammalian TOR ) is implicated in several disorders, including cancer, obesity, and diabetes. Here, we review how nutrient availability is sensed and transduced to TOR in budding yeast and mammals. A better understanding of how nutrient availability is transduced to TOR may allow novel strategies in the treatment for mTOR ‐related diseases.
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Citations
Cites
AMPK: a nutrient and energy sensor that maintains energy homeostasis
Hardie, D. G., Ross, F. A., & Hawley, S. A. (2012) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3311 · Cited by 4,602
AMPK Phosphorylation of Raptor Mediates a Metabolic Checkpoint
Gwinn, D. M., Shackelford, D. B., Egan, D. F., Mihaylova, M. M., Mery, A., Vasquez, D. S., Turk, B. E., & Shaw, R. J. (2008) · Molecular Cell · doi:10.1016/j.molcel.2008.03.003 · Cited by 3,849
TSC2 is phosphorylated and inhibited by Akt and suppresses mTOR signalling
Inoki, K., Li, Y., Zhu, T., Wu, J., & Guan, K.-L. (2002) · Nature Cell Biology · doi:10.1038/ncb839 · Cited by 3,083
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
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 · cited 7×
“In yeast, the EGO (Ego1 – Ego2 – Ego3) ternary complex, the ortholog of RAGULATOR, tethers Gtr1/2 to the vacuole (the yeast equivalent of the lysosome) (Kogan et al , 2010; Zhang et al , 2012; Levine et al , 2013; Powis et al , 2015).”
InfluentialRheb 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
Loewith, R., Jacinto, E., Wullschleger, S., Lorberg, A., Crespo, J. L., Bonenfant, D., Oppliger, W., Jenoe, P., & Hall, M. N. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00636-6 · Cited by 1,886
Self-citationZoncu, R., Bar-Peled, L., Efeyan, A., Wang, S., Sancak, Y., & Sabatini, D. M. (2011) · Science · doi:10.1126/science.1207056 · Cited by 1,673
Regulation of TORC1 by Rag GTPases in nutrient response
Kim, E., Goraksha-Hicks, P., Li, L., Neufeld, T. P., & Guan, K.-L. (2008) · Nature Cell Biology · doi:10.1038/ncb1753 · Cited by 1,349
p53 Target Genes Sestrin1 and Sestrin2 Connect Genotoxic Stress and mTOR Signaling
Budanov, A. V., & Karin, M. (2008) · Cell · doi:10.1016/j.cell.2008.06.028 · Cited by 1,326 · cited 1×
“…proposed to repress mTORC1 through at least three different mechanisms: (i) by activating AMPK (AMP-activated protein kinase) and the TSC complex (Budanov & Karin, 2008), (ii) by acting as a GDI (guanosine dissociation inhibitor) to prevent GDP dissociation from RAGA/B (Peng et al , 2014), and…”
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
The nuts and bolts of AGC protein kinases
Pearce, L. R., Komander, D., & Alessi, D. R. (2010) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2822 · Cited by 1,294
The eIF2α/ATF4 pathway is essential for stress-induced autophagy gene expression
B’chir, W., Maurin, A.-C., Carraro, V., Averous, J., Jousse, C., Muranishi, Y., Parry, L., Stepien, G., Fafournoux, P., & Bruhat, A. (2013) · Nucleic Acids Research · doi:10.1093/nar/gkt563 · Cited by 1,162
Bar-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 · cited 9×
“GATOR1 is composed of DEPDC5 (DEP domain-containing protein 5), NPRL2 (nitrogen permease regulator 2-like protein), and NPRL3 where DEPDC5 is thought to possess the GAP activity toward RAGA/B (Bar-Peled et al , 2013; Panchaud et al , 2013a).”
InfluentialMaking 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
Ragulator 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 · cited 10×
“GATOR1 is composed of DEPDC5 (DEP domain-containing protein 5), NPRL2 (nitrogen permease regulator 2-like protein), and NPRL3 where DEPDC5 is thought to possess the GAP activity toward RAGA/B (Bar-Peled et al , 2013; Panchaud et al , 2013a).”
InfluentialAmino 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
Isolation of a Protein Target of the FKBP12-Rapamycin Complex in Mammalian Cells
Sabers, C. J., Martin, M. M., Brunn, G. J., Williams, J. M., Dumont, F. J., Wiederrecht, G., & Abraham, R. T. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.2.815 · Cited by 887
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
Tee, A. R., Fingar, D. C., Manning, B. D., Kwiatkowski, D. J., Cantley, L. C., & Blenis, J. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.202476899 · Cited by 827 · cited 1×
“…associates with TSC1 and TBC1D7 to form the TSC complex that functions as GAP (GTPase-activating protein) toward lysosomal RHEB (Gao et al , 2002; Kenerson et al , 2002; Kwiatkowski et al , 2002; Onda et al , 2002; Tee et al , 2002; Garami et al , 2003; Inoki et al , 2003a; Dibble et al , 2012).”
mTORC1 induces purine synthesis through control of the mitochondrial tetrahydrofolate cycle
Ben-Sahra, I., Hoxhaj, G., Ricoult, S. J. H., Asara, J. M., & Manning, B. D. (2016) · Science · doi:10.1126/science.aad0489 · Cited by 795
Dever, T. E., Feng, L., Wek, R. C., Cigan, A. M., Donahue, T. F., & Hinnebusch, A. G. (1992) · Cell · doi:10.1016/0092-8674(92)90193-g · Cited by 776
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
SLC38A9 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
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
RAPT1, a mammalian homolog of yeast Tor, interacts with the FKBP12/rapamycin complex.
Chiu, M. I., Katz, H., & Berlin, V (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.26.12574 · Cited by 481
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
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
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 · cited 1×
“Finally, mutations affecting mammalian amino acid sensing components are linked to immunodeficiency, epilepsy, and cancer (Shimobayashi & Hall, 2015), and mTOR is often deregulated in metabolic disorders such as obesity, diabetes, and cancer (Efeyan et al , 2012; Liko & Hall, 2015).”
Recruitment of folliculin to lysosomes supports the amino acid–dependent activation of Rag GTPases
Petit, C. S., Roczniak-Ferguson, A., & Ferguson, S. M. (2013) · Journal of Cell Biology · doi:10.1083/jcb.201307084 · Cited by 355
Rab1A Is an mTORC1 Activator and a Colorectal Oncogene
Thomas, J. D., Zhang, Y.-J., Wei, Y.-H., Cho, J.-H., Morris, L. E., Wang, H.-Y., & Zheng, X. F. S. (2014) · Cancer Cell · doi:10.1016/j.ccell.2014.09.008 · Cited by 278 · cited 3×
“Mechanisti-cally, amino acids promote GTP loading of the small GTPase RAB1A (Ras-related protein RAB-1A) which in turn stimulates mTORC1 interaction with Golgi-resident RHEB (Thomas et al , 2014).”
Amino Acid-Dependent mTORC1 Regulation by the Lysosomal Membrane Protein SLC38A9
Jung, J., Genau, H. M., & Behrends, C. (2015) · Molecular and Cellular Biology · doi:10.1128/mcb.00125-15 · Cited by 266
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
HIF-independent role of prolyl hydroxylases in the cellular response to amino acids
Durán, R. V., MacKenzie, E. D., Boulahbel, H., Frezza, C., Heiserich, L., Tardito, S., Bussolati, O., Rocha, S., Hall, M. N., & Gottlieb, E. (2013) · Oncogene · doi:10.1038/onc.2012.465 · Cited by 139
Self-citationLevine, T. P., Daniels, R. D., Wong, L. H., Gatta, A. T., Gerondopoulos, A., & Barr, F. A. (2013) · Small GTPases · doi:10.4161/sgtp.24262 · Cited by 93 · cited 1×
“In yeast, the EGO (Ego1 – Ego2 – Ego3) ternary complex, the ortholog of RAGULATOR, tethers Gtr1/2 to the vacuole (the yeast equivalent of the lysosome) (Kogan et al , 2010; Zhang et al , 2012; Levine et al , 2013; Powis et al , 2015).”
Powis, K., Zhang, T., Panchaud, N., Wang, R., Virgilio, C. D., & Ding, J. (2015) · Cell Research · doi:10.1038/cr.2015.86 · Cited by 80
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
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mTOR signalling and cellular metabolism are mutual determinants in cancer
Mossmann, D., Park, S., & Hall, M. N. (2018) · Nature reviews. Cancer · doi:10.1038/s41568-018-0074-8 · Cited by 1,088
Self-citationAMPK 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
Self-citationCancer cell metabolism: the essential role of the nonessential amino acid, glutamine
Zhang, J., Pavlova, N. N., & Thompson, C. B. (2017) · The EMBO Journal · doi:10.15252/embj.201696151 · Cited by 651
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Metadata
- Authors
- González, A., & Hall, M. N.
- Venue
- The EMBO Journal
- Published
- 2017-01-17
- Volume
- 36
- Issue
- 4
- Pages
- 397-408
- ISSN
- 0261-4189 (ISSN-L)
- 1460-2075
- OpenAlex
- W2576890255
- Cited by
- 732
- References
- 37
- FWCI
- 27.08
- Type
- journal article
- Language
- en
- Open access
- bronze
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