mTORC1 signaling controls multiple steps in ribosome biogenesis
Abstract
Ribosome biogenesis is critical for cells to generate the ribosomes they need for protein synthesis in order to survive, grow and proliferate. It is a complex process, involving the coordinated production of four different RNA species and about 80 proteins, as well as their assembly into functional ribosomal subunits. Given its high demand for amino acids and nucleotides, it is also a metabolically expensive process for the cell. The mammalian target of rapamycin complex 1 (mTORC1) is a protein kinases which is activated by nutrients, anabolic hormones and oncogenic signaling pathways. mTORC1 positively regulates several steps in ribosome biogenesis, including ribosomal RNA transcription, the synthesis of ribosomal proteins and other components required for ribosome assembly. mTORC1 can thus coordinate stimuli which promote ribosome production with the various steps involved in this process. Although important advances have been made in our understanding of mTORC1 signaling, major questions remain about the molecular mechanisms by which it regulates ribosome biogenesis.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
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?
mTORC1 increases ribosomal biogenesis.
“However, mTORC1 increases not only protein synthesis from existing ribosomes but also the synthesis of more ribosomes, a process known as ribosomal biogenesis [176].”
From Effects of Skeletal Muscle Hypertrophy on Fat Mass and Glucose Homeostasis in Humans and Animals: A Narrative Review with Systematic Literature Search (2025) · cites this paper as [176]
Cites
TSC2 Mediates Cellular Energy Response to Control Cell Growth and Survival
Inoki, K., Zhu, T., & Guan, K.-L. (2003) · Cell · doi:10.1016/s0092-8674(03)00929-2 · Cited by 3,914 · see citing works
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 · see citing works
eIF4 Initiation Factors: Effectors of mRNA Recruitment to Ribosomes and Regulators of Translation
Gingras, A., Raught, B., & Sonenberg, N. (1999) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.68.1.913 · Cited by 2,103 · see citing works
A unifying model for mTORC1-mediated regulation of mRNA translation
Thoreen, C. C., Chantranupong, L., Keys, H. R., Wang, T., Gray, N. S., & Sabatini, D. M. (2012) · Nature · doi:10.1038/nature11083 · Cited by 1,477 · see citing works
MicroRNA-10a binds the 5’UTR of ribosomal protein mRNAs and enhances their translation
Ørom, U. A., Nielsen, F. C., & Lund, A. H. (2008) · Molecular Cell · doi:10.1016/j.molcel.2008.05.001 · Cited by 1,384 · see citing works
Inoki, K., Ouyang, H., Zhu, T., Lindvall, C., Wang, Y., Zhang, X., Yang, Q., Bennett, C., Harada, Y., Stankunas, K., et al. (2006) · Cell · doi:10.1016/j.cell.2006.06.055 · Cited by 1,377 · see citing works
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 · see citing works
The translational landscape of mTOR signalling steers cancer initiation and metastasis
Hsieh, A. C., Liu, Y., Edlind, M. P., Ingolia, N. T., Janes, M. R., Sher, A., Shi, E. Y., Stumpf, C. R., Christensen, C., Bonham, M. J., et al. (2012) · Nature · doi:10.1038/nature10912 · Cited by 1,313 · see citing works
Rapamycin suppresses 5′TOP mRNA translation through inhibition of p70s6k
Jefferies, H. B. J., Fumagalli, S., Dennis, P. B., Reinhard, C., Pearson, R. B., & Thomas, G. (1997) · The EMBO Journal · doi:10.1093/emboj/16.12.3693 · Cited by 934 · see citing works
Regulation of elongation factor 2 kinase by p90RSK1 and p70 S6 kinase
Wang, X.-M., Li, W., Williams, M. R., Terada, N., Alessi, D., & Proud, C. G. (2001) · EMBO Journal · doi:10.1093/emboj/20.16.4370 · Cited by 862 · see citing works
Self-citationRoux, P. P., Ballif, B. A., Anjum, R., Gygi, S. P., & Blenis, J. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0405659101 · Cited by 750 · see citing works
Pende, M., Um, S. H., Mieulet, V., Sticker, M., Goss, V. L., Mestan, J., Mueller, M., Fumagalli, S., Kozma, S. C., & Thomas, G. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.8.3112-3124.2004 · Cited by 743 · see citing works
Stimulation of de novo pyrimidine synthesis by growth signaling through mTOR and S6K1
Ben-Sahra, I., Howell, J. J., Asara, J. M., & Manning, B. D. (2013) · Science · doi:10.1126/science.1228792 · Cited by 739 · see citing works
Activation of mTORC2 by Association with the Ribosome
Zinzalla, V., Stracka, D., Oppliger, W., & Hall, M. N. (2011) · Cell · doi:10.1016/j.cell.2011.02.014 · Cited by 648 · see citing works
Ribosomal protein S6 phosphorylation is a determinant of cell size and glucose homeostasisPreprint
Ruvinsky, I., Sharon, N., Lerer, T., Cohen, H., Stolovich-Rain, M., Nir, T., Dor, Y., Zisman, P., & Meyuhas, O. (2005) · Genes & Development · doi:10.1101/gad.351605 · Cited by 640 · see citing works
Feng, Z., Hu, W., de Stanchina, E., Teresky, A. K., Jin, S., Lowe, S., & Levine, A. J. (2007) · Cancer Research · doi:10.1158/0008-5472.can-06-4149 · Cited by 633 · see citing works
Regulation of HDM2 activity by the ribosomal protein L11
Lohrum, M. A. E., Ludwig, R. L., Kubbutat, M. H. G., Hanlon, M., & Vousden, K. H. (2003) · Cancer Cell · doi:10.1016/s1535-6108(03)00134-x · Cited by 626 · see citing works
Rapamycin selectively represses translation of the "polypyrimidine tract" mRNA family.
Jefferies, H. B. J., Reinhard, C., Kozma, S. C., & Thomas, G. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.10.4441 · Cited by 623 · see citing works
An Emerging Role of mTOR in Lipid Biosynthesis
Laplante, M., & Sabatini, D. M. (2009) · Current Biology · doi:10.1016/j.cub.2009.09.058 · Cited by 614 · see citing works
Mayer, C., & Grummt, I. (2006) · Oncogene · doi:10.1038/sj.onc.1209883 · Cited by 568 · see citing works
Bywater, M. J., Poortinga, G., Sanij, E., Hein, N., Peck, A., Cullinane, C. M., Wall, M., Cluse, L. A., Drygin, D., Anderes, K. L., et al. (2012) · Cancer Cell · doi:10.1016/j.ccr.2012.05.019 · Cited by 561 · see citing works
How Cells Coordinate Growth and Division
Jorgensen, P., & Tyers, M. (2004) · Current Biology · doi:10.1016/j.cub.2004.11.027 · Cited by 559 · see citing works
Zhang, Y., Wolf, G. W., Bhat, K., Jin, A., Allio, T., Burkhart, W., & Xiong, Y. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.23.8902-8912.2003 · Cited by 556 · see citing works
Powers, T., & Walter, P. (1999) · Molecular Biology of the Cell · doi:10.1091/mbc.10.4.987 · Cited by 540 · see citing works
Inhibition of MDM2-mediated p53 Ubiquitination and Degradation by Ribosomal Protein L5
Dai, M., & Lu, H. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m403722200 · Cited by 536 · see citing works
Quantitative Phosphoproteomics Reveal mTORC1 Activates de Novo Pyrimidine Synthesis
Robitaille, A. M., Christen, S., Shimobayashi, M., Cornu, M., Fava, L. L., Moes, S., Prescianotto-Baschong, C., Sauer, U., Jenoe, P., & Hall, M. N. (2013) · Science · doi:10.1126/science.1228771 · Cited by 525 · see citing works
TOS Motif-Mediated Raptor Binding Regulates 4E-BP1 Multisite Phosphorylation and Function
Schalm, S. S., Fingar, D. C., Sabatini, D. M., & Blenis, J. (2003) · Current Biology · doi:10.1016/s0960-9822(03)00329-4 · Cited by 512 · see citing works
Identification of a conserved motif required for mTOR signaling.
Schalm, S., & Blenis, J. (2002) · Current Biology · doi:10.1016/s0960-9822(02)00762-5 · Cited by 507 · see citing works
Mayer, C., Zhao, J., Yuan, X., & Grummt, I. (2004) · Genes & Development · doi:10.1101/gad.285504 · Cited by 506 · see citing works
Rheb fills a GAP between TSC and TOR
Manning, B. (2003) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2003.09.003 · Cited by 483 · see citing works
Hannan, K., Brandenburger, Y., Jenkins, A., Sharkey, K., Cavanaugh, A., Rothblum, L., Moss, T., Poortinga, G., McArthur, G., Pearson, R., et al. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.23.8862-8877.2003 · Cited by 473 · see citing works
The RNA Polymerase I Transcription Machinery: An Emerging Target for the Treatment of Cancer
Drygin, D., Rice, W. G., & Grummt, I. (2010) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pharmtox.010909.105844 · Cited by 419 · see citing works
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 407 · see citing works
Analysis of Nucleolar Protein Dynamics Reveals the Nuclear Degradation of Ribosomal Proteins
Lam, Y. W., Lamond, A. I., Mann, M., & Andersen, J. S. (2007) · Current Biology · doi:10.1016/j.cub.2007.03.064 · Cited by 369 · see citing works
Functions and regulation of the 70 kDa ribosomal S6 kinases
Fenton, T. R., & Gout, I. T. (2010) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2010.09.018 · Cited by 338 · see citing works
Huber, A., Bodenmiller, B., Uotila, A., Ståhl, M., Wanka, S., Gerrits, B., Aebersold, R. H., & Loewith, R. (2009) · Genes & Development · doi:10.1101/gad.532109 · Cited by 334 · see citing works
Oh, W. J., Wu, C. C., Kim, S. J., Facchinetti, V., Julien, L.-A., Finlan, M., Roux, P. P., Su, B., & Jacinto, E. (2010) · The EMBO Journal · doi:10.1038/emboj.2010.271 · Cited by 333 · see citing works
Nutrient regulates Tor1 nuclear localization and association with rDNA promoter
Li, H., Tsang, C. K., Watkins, M. P., Bertram, P. G., & Zheng, X.-F. (2006) · Nature · doi:10.1038/nature05020 · Cited by 299 · see citing works
Ribosomal protein S6 kinase activity controls the ribosome biogenesis transcriptional program
Chauvin, C., Koka, V., Nouschi, A., Mieulet, V., Hoareau‐Aveilla, C., Dreazen, A., Cagnard, N., Carpentier, W., Kiss, T., Meyuhas, O., et al. (2013) · Oncogene · doi:10.1038/onc.2012.606 · Cited by 279 · see citing works
ERK1/2 Phosphorylate Raptor to Promote Ras-dependent Activation of mTOR Complex 1 (mTORC1)
Carriere, A., Romeo, Y., Acosta-Jaquez, H. A., Moreau, J., Bonneil, E., Thibault, P., Fingar, D. C., & Roux, P. P. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.159046 · Cited by 268 · see citing works
Donati, G., Peddigari, S., Mercer, C. A., & Thomas, G. (2013) · Cell Reports · doi:10.1016/j.celrep.2013.05.045 · Cited by 263 · see citing works
The role of human ribosomal proteins in the maturation of rRNA and ribosome production
Robledo, S. M., Idol, R. A., Crimmins, D. L., Ladenson, J. H., Mason, P. J., & Bessler, M. (2008) · RNA · doi:10.1261/rna.1132008 · Cited by 261 · see citing works
Zhao, J., Yuan, X., Frödin, M., & Grummt, I. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00036-4 · Cited by 259 · see citing works
Tcherkezian, J., Cargnello, M., Roméo, Y., Huttlin, E. L., Lavoie, G., Gygi, S. P., & Roux, P. P. (2014) · Genes & Development · doi:10.1101/gad.231407.113 · Cited by 255 · see citing works
Epigenetic Activation of a Subset of mRNAs by eIF4E Explains Its Effects on Cell Proliferation
Mamane, Y., Petroulakis, E., Martineau, Y., Sato, T.-A., Larsson, O., Rajasekhar, V., & Sonenberg, N. (2007) · PLoS ONE · doi:10.1371/journal.pone.0000242 · Cited by 237 · see citing works
mTOR associates with TFIIIC, is found at tRNA and 5S rRNA genes, and targets their repressor Maf1
Kantidakis, T., Ramsbottom, B. A., Birch, J. L., Dowding, S. N., & White, R. J. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1005188107 · Cited by 218 · see citing works
Translational coregulation of 5′TOP mRNAs by TIA-1 and TIARPreprint
Damgaard, C. K., & Lykke‐Andersen, J. (2011) · Genes & Development · doi:10.1101/gad.17355911 · Cited by 214 · see citing works
Hölzel, M., Michaela, R., Schlee, M., Thomas, G., Thomas, H., Anastassia, M., Anita, G.-E., Kremmer, E., Hiddemann, W., Bornkamm, G. W., et al. (2005) · The Journal of Cell Biology · doi:10.1083/jcb.200501141 · Cited by 205 · see citing works
Voit, R., Schnapp, A., Kuhn, A., Rosenbauer, H., Hirschmann, P., Stunnenberg, H. G., & Grummt, I. (1992) · The EMBO Journal · doi:10.1002/j.1460-2075.1992.tb05280.x · Cited by 199 · see citing works
Basic mechanisms in RNA polymerase i transcription of the ribosomal RNA genes
Goodfellow, S. J., & Zomerdijk, J. C. B. M. (2013) · Subcellular Biochemistry · doi:10.1007/978-94-007-4525-4_10 · Cited by 197 · see citing works
Strezoska, Ž., Pestov, D. G., & Lau, L. F. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.15.5516-5528.2000 · Cited by 185 · see citing works
mTORC1 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 182 · see citing works
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 182 · see citing works
Rouquette, J., Choesmel, V., & Gleizes, P. (2005) · The EMBO Journal · doi:10.1038/sj.emboj.7600752 · Cited by 180 · see citing works
Claypool, J. A., French, S. L., Johzuka, K., Eliason, K., Vũ, L., Dodd, J. A., Beyer, A. L., & Nomura, M. (2003) · Molecular Biology of the Cell · doi:10.1091/mbc.e03-08-0594 · Cited by 171 · see citing works
mTOR binds to the promoters of RNA polymerase I- and III-transcribed genes
Tsang, C. K., Liu, H., & Zheng, X.-F. (2010) · Cell Cycle · doi:10.4161/cc.9.5.10876 · Cited by 157 · see citing works
Mechanisms of regulation of RNA polymerase III‐dependent transcription by TORC1
Wei, Y., Tsang, C. K., & Zheng, X.-F. (2009) · The EMBO Journal · doi:10.1038/emboj.2009.179 · Cited by 156 · see citing works
Amino acid starvation affects the initiation frequency of nucleolar RNA polymerase
Grummt, I., Smith, V. A., & Grummt, F. (1976) · Cell · doi:10.1016/0092-8674(76)90174-4 · Cited by 150 · see citing works
Regulation of Ribosomal Protein mRNA Content and Translation in Growth-Stimulated Mouse Fibroblasts
Geyer, P., Meyuhas, O., Perry, R. P., & Johnson, L. F. (1982) · Molecular and Cellular Biology · doi:10.1128/mcb.2.6.685-693.1982 · Cited by 144 · see citing works
Michaela, R., Hölzel, M., Thomas, G., Anastassia, M., Thomas, H., Orban, M., Pfisterer, I., Anita, G.-E., Kremmer, E., & Eick, D. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.00172-07 · Cited by 139 · see citing works
Dysregulation of RNA polymerase I transcription during disease
Hannan, K. M., Sanij, E., Rothblum, L. I., Hannan, R. D., & Pearson, R. B. (2012) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2012.10.014 · Cited by 137 · see citing works
Physical and Functional Interaction between Pes1 and Bop1 in Mammalian Ribosome Biogenesis
Lapik, Y. R., Fernandes, C. J., Lau, L. F., & Pestov, D. G. (2004) · Molecular Cell · doi:10.1016/j.molcel.2004.05.020 · Cited by 129 · see citing works
The role of UBF in regulating the structure and dynamics of transcriptionally active rDNA chromatin
Sanij, E., & Hannan, R. D. (2009) · Epigenetics · doi:10.4161/epi.4.6.9449 · Cited by 129 · see citing works
Regulation of pol III transcription by nutrient and stress signaling pathways
Moir, R. D., & Willis, I. M. (2012) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2012.11.001 · Cited by 121 · see citing works
UBF activates RNA polymerase I transcription by stimulating promoter escape
Panov, K. I., Friedrich, J. K., Russell, J., & Zomerdijk, J. C. B. M. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7601221 · Cited by 121 · see citing works
Lee, J. H., Moir, R. D., & Willis, I. M. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.c900020200 · Cited by 117 · see citing works
Transcription of mouse rDNA is regulated by an activated subform of RNA polymerase I
Tower, J., & Sollner-Webb, B. (1987) · Cell · doi:10.1016/0092-8674(87)90514-9 · Cited by 116 · see citing works
James, M., & Zomerdijk, J. C. B. M. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m307735200 · Cited by 113 · see citing works
Strezoska, Z., Pestov, D. G., & Lau, L. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m204381200 · Cited by 109 · see citing works
Growth control and ribosomopathies
Teng, T., Thomas, G., & Mercer, C. A. (2013) · Current Opinion in Genetics & Development · doi:10.1016/j.gde.2013.02.001 · Cited by 106 · see citing works
Quality control mechanisms during ribosome maturation
Karbstein, K. (2013) · Trends in Cell Biology · doi:10.1016/j.tcb.2013.01.004 · Cited by 104 · see citing works
Pellizzoni, L., Lotti, F., Maras, B., & Pierandrei‐Amaldi, P. (1997) · Journal of Molecular Biology · doi:10.1006/jmbi.1996.0888 · Cited by 103 · see citing works
mTOR signaling regulates the processing of pre-rRNA in human cells
Iadevaia, V., Zhang, Z., Jan, E., & Proud, C. G. (2011) · Nucleic Acids Research · doi:10.1093/nar/gkr1040 · Cited by 102 · see citing works
Self-citationCoactivator and Promoter-Selective Properties of RNA Polymerase I TAFs
Beckmann, H., Chen, J., O’Brien, T., & Tjian, R. (1995) · Science · doi:10.1126/science.270.5241.1506 · Cited by 98 · see citing works
The many faces of small nucleolar RNAs
Bratkovič, T., & Rogelj, B. (2014) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2014.04.009 · Cited by 97 · see citing works
La protein has a positive effect on the translation of TOP mRNAs in vivo
Crosio, C. (2000) · Nucleic Acids Research · doi:10.1093/nar/28.15.2927 · Cited by 96 · see citing works
Grewal, S. S., Evans, J. R., & Edgar, B. A. (2007) · The Journal of Cell Biology · doi:10.1083/jcb.200709044 · Cited by 95 · see citing works
Modulation of transcription of rRNA genes by rapamycin
Mahajan, P. B. (1994) · International Journal of Immunopharmacology · doi:10.1016/0192-0561(94)90091-4 · Cited by 93 · see citing works
Hmo1 Is Required for TOR-Dependent Regulation of Ribosomal Protein Gene Transcription
Berger, A. B., Decourty, L., Badis, G., Nehrbass, U., Jacquier, A., & Gadal, O. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.01102-07 · Cited by 92 · see citing works
Tuan, J., Zhai, W., & Comai, L. (1999) · Molecular and Cellular Biology · doi:10.1128/mcb.19.4.2872 · Cited by 91 · see citing works
Miloslavski, R., Cohen, E., Avraham, A., Iluz, Y., Hayouka, Z., Kasir, J., Mudhasani, R., Jones, S. N., Cybulski, N., Rüegg, M. A., et al. (2014) · Journal of Molecular Cell Biology · doi:10.1093/jmcb/mju008 · Cited by 87 · see citing works
Huo, Y., Iadevaia, V., Yao, Z., Kelly, I., Cosulich, S., Guichard, S., Foster, L., & Proud, C. (2012) · Biochemical Journal · doi:10.1042/bj20112107 · Cited by 79 · see citing works
Self-citationLa Protein Is Associated with Terminal Oligopyrimidine mRNAs in Actively Translating Polysomes
Cardinali, B., Carissimi, C., Gravina, P., & Pierandrei‐Amaldi, P. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m300722200 · Cited by 73 · see citing works
Matthew, E. M., Hart, L. S., Astrinidis, A., Navaraj, A., Dolloff, N. G., Dicker, D. T., Henske, E. P., & El-Deiry, W. S. (2009) · Cell Cycle · doi:10.4161/cc.8.24.10800 · Cited by 67 · see citing works
Havel, J. J., Li, Z., Cheng, D., Peng, J., & Fu, H. (2014) · Oncogene · doi:10.1038/onc.2014.91 · Cited by 57 · see citing works
Shama, S., Avni, D., Frederickson, R., Sonenberg, N., & Meyuhas, O. (1995) · Europe PMC (PubMed Central) · Cited by 55 · see citing works
The Species-Specific RNA Polymerase I Transcription Factor SL-1 Binds to Upstream Binding Factor
Hempel, W. M., Cavanaugh, A. H., Hannan, R. D., Taylor, L. J., & Rothblum, L. I. (1996) · Molecular and Cellular Biology · doi:10.1128/mcb.16.2.557 · Cited by 54 · see citing works
Loreni, F., Thomas, G., & Amaldi, F. (2000) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.2000.01753.x · Cited by 50 · see citing works
Transcription from the rat 45S ribosomal DNA promoter does not require the factor UBF.
Sd, S., O’Mahony, D. J., Kinsella, B. T., & Li, R. (1993) · Europe PMC (PubMed Central) · Cited by 46 · see citing works
Fonseca, B. D., Alain, T., Finestone, L. K., Huang, B., Rolfe, M. J., Jiang, T., Yao, Z., Hernández, G., Bennett, C. F., & Proud, C. G. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.260794 · Cited by 45 · see citing works
Self-citationLiu, R., Iadevaia, V., Avérous, J., Taylor, P. M., Zhang, Z., & Proud, C. G. (2014) · Nucleic Acids Research · doi:10.1093/nar/gku130 · Cited by 44 · see citing works
Self-citationCaldarola, S., Amaldi, F., Proud, C. G., & Loreni, F. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m310574200 · Cited by 36 · see citing works
Self-citationExpression of yeast high mobility group protein HMO1 is regulated by TOR signaling
Xiao, L., Kamau, E. T., Donze, D., & Grove, A. (2011) · Gene · doi:10.1016/j.gene.2011.08.017 · Cited by 29 · see citing works
Flagged first, then by citations
2 of the 95 references couldn’t be matched to a known paper.
Cited by
Sorted by citations
The PI3K–AKT network at the interface of oncogenic signalling and cancer metabolism
Hoxhaj, G., & Manning, B. D. (2020) · Nature Reviews Cancer · doi:10.1038/s41568-019-0216-7 · Cited by 2,137 · see citing works
Targeting mTOR for cancer therapy
Hua, H., Kong, Q.-B., Zhang, H., Wang, J., Luo, T., & Jiang, Y.-F. (2019) · Journal of Hematology & Oncology · doi:10.1186/s13045-019-0754-1 · Cited by 772 · see citing works
Ribosome biogenesis in cancer: new players and therapeutic avenues
Pelletier, J., Thomas, G., & Volarević, S. (2017) · Nature reviews. Cancer · doi:10.1038/nrc.2017.104 · Cited by 802 · see citing works
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 641 · see citing works
“Enhancing ribosome biogenesis is a major function of mTORC1 [33].”
BackgroundmTOR in Brain Physiology and Pathologies
Bockaert, J., & Marin, P. (2015) · Physiological Reviews · doi:10.1152/physrev.00038.2014 · Cited by 360 · see citing works
“In addition, mTORC1, via S6K1, promotes the expression of ribosomal RNA (rRNA), the transcription of 5S rRNA, and transfer RNA (tRNA) and thereby contributes to ribosome biogenesis (109).”
BackgroundStepanenko, A. A., & Dmitrenko, V. V. (2015) · Gene · doi:10.1016/j.gene.2015.08.009 · Cited by 321 · see citing works
Ribosome biogenesis in disease: new players and therapeutic targets
Jiao, L., Liu, Y., Yu, X., Pan, X., Zhang, Y., Tu, J., Song, Y., & Li, Y. (2023) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-022-01285-4 · Cited by 317 · see citing works
“2).(22) Ribosomal protein S6 kinase 1 (S6K1) is under the control of mTORC1 signaling.”
BackgroundMolecular logic of mTORC1 signalling as a metabolic rheostat
Valvezan, A. J., & Manning, B. D. (2019) · Nature Metabolism · doi:10.1038/s42255-019-0038-7 · Cited by 295 · see citing works
Drosophila as a model for ageing
Piper, M. D. W., & Partridge, L. (2018) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2017.09.016 · Cited by 273 · see citing works
“In addition to its effects on translation and autophagy, mTOR signals to control other cellular functions, including transcription, through all three RNA polymerases (Ghosh et al., 2014; Iadevaia et al., 2014; Marshall et al., 2012).”
BackgroundMTOR inhibitors in cancer therapy
Xie, J., Wang, X., & Proud, C. G. (2016) · F1000Research · doi:10.12688/f1000research.9207.1 · Cited by 266 · see citing works
The mTORC1 signaling network senses changes in cellular purine nucleotide levels
Hoxhaj, G., Hughes-Hallett, J., Timson, R. C., Ilagan, E., Yuan, M., Asara, J., Ben-Sahra, I., & Manning, B. (2017) · Cell Reports · doi:10.1016/j.celrep.2017.10.029 · Cited by 184 · see citing works
“As part of its program to stimulate ribosome biogenesis, mTORC1 has been found to promote the action of both Pol I and Pol III, the RNA polymerases that transcribe rRNA (Iadevaia et al., 2014).”
BackgroundGene expression hallmarks of cellular ageing
Frenk, S., & Houseley, J. M. (2018) · Biogerontology · doi:10.1007/s10522-018-9750-z · Cited by 180 · see citing works
“In fact, accumulation of ribosomal proteins is a predictor of shortened lifespan in yeast (Janssens et al. 2015; Janssens and Veenhoff 2016) and fibroblasts derived from Hutchinson–Gilford progeria syndrome (HGPS) patients show unusually high ribosome synthesis (Buchwalter and Hetzer 2017), while…”
BackgroundRegulation of ribosomal protein genes: An ordered anarchy
Petibon, C., Ghulam, M. M., Catala, M., & Elela, S. A. (2020) · Wiley Interdisciplinary Reviews - RNA · doi:10.1002/wrna.1632 · Cited by 164 · see citing works
“The most studied mechanism of translation regulation is that controlled by the TOR pathway, which links translation to nutrients availability, cell size, and cell division (Caron et al., 2010; Gingras et al., 2004; Iadevaia et al., 2014; Masvidal et al., 2017; Mayer & Grummt, 2006).”
BackgroundMethodThe Lysosome Signaling Platform: Adapting With the Times
Inpanathan, S., & Botelho, R. J. (2019) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2019.00113 · Cited by 157 · see citing works
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 160 · see citing works
“also stimulates rRNA synthesis through coordinated regulation of three essential RNA polymerase I (Pol I)-specific transcription factors, UBF, SL1, and TIF1A, and by relieving MAF1-mediated inhibition of RNA polymerase III (Pol III) transcription (Iadevaia et al., 2014; Mayer and Grummt, 2006; Michels et al., 2010; Sh…”
BackgroundInfluentialLysosomal quality control of cell fate: a novel therapeutic target for human diseases
Zhu, S.-Y., Yao, R.-Q., Li, Y., Zhao, P.-Y., Ren, C., Du, X.-H., & Yao, Y.-M. (2020) · Cell Death and Disease · doi:10.1038/s41419-020-03032-5 · Cited by 124 · see citing works
mTOR Cross-Talk in Cancer and Potential for Combination Therapy
Conciatori, F., Ciuffreda, L., Bazzichetto, C., Falcone, I., Pilotto, S., Bria, E., Cognetti, F., & Milella, M. (2018) · Cancers · doi:10.3390/cancers10010023 · Cited by 140 · see citing works
Ribosome biogenesis adaptation in resistance training-induced human skeletal muscle hypertrophy
Figueiredo, V. C., Caldow, M. K., Massie, V., Markworth, J. F., Cameron-Smith, D., & Blazevich, A. J. (2015) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00050.2015 · Cited by 133 · see citing works
“In fact, ribosomal content dictates the upper limit of protein synthesis of a cell (12), and thus it may be speculated that RE not only activates translational initiation but also increases the total muscle capacity for protein synthesis through de novo ribosome biogenesis.”
BackgroundAntignano, I., Liu, Y., Offermann, N., & Capasso, M. (2023) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-023-04775-y · Cited by 117 · see citing works
The ribosome, (slow) beating heart of cancer (stem) cell
Bastide, A., & David, A. (2018) · Oncogenesis · doi:10.1038/s41389-018-0044-8 · Cited by 119 · see citing works
Phosphorylation and Signal Transduction Pathways in Translational ControlPreprint
Proud, C. G. (2018) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a033050 · Cited by 121 · see citing works
Self-citationLiu, R., & Proud, C. G. (2016) · Acta Pharmacologica Sinica · doi:10.1038/aps.2015.123 · Cited by 117 · see citing works
Self-citationSignaling, metabolism, and cancer: An important relationship for therapeutic intervention
Vaghari‐Tabari, M., Ferns, G. A., Qujeq, D., Andevari, A. N., Sabahi, Z., & Moein, S. (2021) · Journal of Cellular Physiology · doi:10.1002/jcp.30276 · Cited by 117 · see citing works
“acids, so that by stimulating the biogenesis of ribosomes, it increases protein synthesis (Bar‐Peled & Sabatini, 2014; Iadevaia et al., 2014).”
BackgroundDiverse Regulators of Human Ribosome Biogenesis Discovered by Changes in Nucleolar Number
Farley‐Barnes, K. I., McCann, K. L., Ogawa, L. M., Merkel, J., Surovtseva, Y. V., & Baserga, S. J. (2018) · Cell Reports · doi:10.1016/j.celrep.2018.01.056 · Cited by 115 · see citing works
“This process is subject to complex regulation because it must be highly responsive to various cellular stimuli, such as nutrient availability (Iadevaia et al., 2014; Jastrzebski et al., 2007; Mitchell et al., 2015).”
mTORC1 and PKB/Akt control the muscle response to denervation by regulating autophagy and HDAC4
Castets, P., Rion, N., Théodore, M., Falcetta, D., Lin, S., Reischl, M., Wild, F., Guérard, L., Eickhorst, C., Brockhoff, M., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-11227-4 · Cited by 112 · see citing works
The DDX5/Dbp2 subfamily of DEAD‐box RNA helicases
Xing, Z., Ma, W. K., & Tran, E. J. (2018) · Wiley Interdisciplinary Reviews - RNA · doi:10.1002/wrna.1519 · Cited by 108 · see citing works
Ribosomal biogenesis as an emerging target of neurodevelopmental pathologies
Hetman, M., & Słomnicki, Ł. P. (2018) · Journal of Neurochemistry · doi:10.1111/jnc.14576 · Cited by 110 · see citing works
Coupling of Ribosome Synthesis and Translational Capacity with Cell Growth
Dai, X., & Zhu, M. (2020) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2020.04.010 · Cited by 110 · see citing works
Ribosome biogenesis restricts innate immune responses to virus infection and DNA
Bianco, C., & Mohr, I. (2019) · eLife · doi:10.7554/elife.49551 · Cited by 101 · see citing works
“Introduction The minting of ribosomes, the molecular machines that synthesize polypeptides, is subject to stringent controls that coordinate demand for ribosomes with intracellular processes and environmental cues, including nutritional status and responses to physiological stress (Iadevaia et al., 2014).”
BackgroundIntrinsic Age-Dependent Changes and Cell-Cell Contacts Regulate Nephron Progenitor Lifespan
Chen, S., Brunskill, E. W., Potter, S. S., Dexheimer, P. J., Salomonis, N., Aronow, B. J., Hong, C. I., Zhang, T., & Kopan, R. (2015) · Developmental Cell · doi:10.1016/j.devcel.2015.09.009 · Cited by 98 · see citing works
Regulation of CD8+ T memory and exhaustion by the mTOR signals
Chen, Y., Xu, Z., Sun, H., Ouyang, X.-X., Han, Y.-H., Yu, H., Wu, N.-B., Xie, Y., & Su, B. (2023) · Cellular & Molecular Immunology · doi:10.1038/s41423-023-01064-3 · Cited by 91 · see citing works
“Over several decades of research, mTOR has been characterized as a key regulator of multiple metabolic processes, including ribosome biogenesis [160], protein [161]/ nucleotide [162, 163]/fatty acid/lipid [164] synthesis and negative regulation of autophagy [165]. mTOR forms at least two distinct…”
BackgroundRegulation of rDNA transcription in response to growth factors, nutrients and energy
Kusnadi, E. P., Hannan, K. M., Hicks, R. J., Hannan, R. D., Pearson, R. B., & Kang, J. (2014) · Gene · doi:10.1016/j.gene.2014.11.010 · Cited by 95 · see citing works
PI3K/Akt/mTOR Signaling Pathway and the Biphasic Effect of Arsenic in Carcinogenesis
Chen, Q. Y., & Costa, M. (2018) · Molecular Pharmacology · doi:10.1124/mol.118.112268 · Cited by 92 · see citing works
“through an increased number of ribosomes and accelerated protein translation (Iadevaia et al., 2014).”
BackgroundA non-canonical role for a small nucleolar RNA in ribosome biogenesis and senescence
Cheng, Y., Wang, S., Zhang, H., Lee, J.-S., Ni, C., Guo, J., Chen, E., Wang, S., Acharya, A., Chang, T.-C., et al. (2024) · Cell · doi:10.1016/j.cell.2024.06.019 · Cited by 92 · see citing works
“51 Additionally, EPB41L4A-AS1 , the SNORA13 host gene, was reported to be strongly induced in human fibroblasts upon serum starvation or contact-induced growth arrest, conditions where SNORA13-mediated inhibition of ribosome biogenesis might be advantageous.”
Exaptive Evolution of Target of Rapamycin Signaling in Multicellular Eukaryotes
Brunkard, J. O. (2020) · Developmental Cell · doi:10.1016/j.devcel.2020.06.022 · Cited by 84 · see citing works
“…monomeric metabolites required for ribosome synthesis (amino acids and nucleotides) and the energy stores required to transcribe, translate, and assemble ribosomes, to ensure that ribosome production does not deplete available resources (Figure 1) (Iadevaia et al., 2014; Pelletier et al., 2018).”
BackgroundmTORC Inhibitors as Broad-Spectrum Therapeutics for Age-Related Diseases
Walters, H. E., & Cox, L. S. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19082325 · Cited by 85 · see citing works
“Ribosomal biogenesis (and hence subsequent protein synthesis) requires the coordination of transcription of ribosomal RNAs (rRNA) within the nucleolus by RNA polymerase I, protein-encoding messenger RNAs (mRNA) by RNA polymerase II and transfer RNAs (tRNA) and a further 5S ribosomal RNA by RNA polymerase III, and is p…”
BackgroundThe homeostatic regulation of ribosome biogenesis
Ni, C., & Buszczak, M. (2022) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2022.03.043 · Cited by 82 · see citing works
Monocytes present age-related changes in phospholipid concentration and decreased energy metabolism
Saare, M., Tserel, L., Haljasmägi, L., Taalberg, E., Peet, N., Eimre, M., Vetik, R., Kingo, K., Saks, K., Tamm, R., et al. (2020) · Aging Cell · doi:10.1111/acel.13127 · Cited by 79 · see citing works
Emerging Role of Eukaryote Ribosomes in Translational Control
Venezia, N. D., Vincent, A., Marcel, V., Catez, F., & Diaz, J. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20051226 · Cited by 77 · see citing works
“Since all of the mRNAs coding for RPs contain a 5′-TOP, mTOR positively regulates synthesis of RPs allowing a coordinated synthesis of the different components of the ribosome [51].”
BackgroundYu, P., Qu, N., Zhu, R., Hu, J., Han, P., Wu, J., Tan, L., Gan, H., He, C., Fang, C., et al. (2023) · Science Advances · doi:10.1126/sciadv.adg7125 · Cited by 79 · see citing works
“5) ( 42 ).”
Szaflarski, W., Leśniczak-Staszak, M., Sowiński, M., Ojha, S., Aulas, A., Dave, D., Malla, S., Anderson, P., Ivanov, P. V., & Lyons, S. M. (2021) · Nucleic Acids Research · doi:10.1093/nar/gkab1231 · Cited by 78 · see citing works
“…synthesis. mTOR integrates multiple aspects of ribosome biogenesis to allow for coordinative regulation of different components [Reviewed in (72)]. mTOR inactivation represses ribosomal protein synthesis through dephosphorylation of LARP1 (31) and represses the transcription of both 47S and…”
Giguère, V. (2018) · FEBS Journal · doi:10.1111/febs.14384 · Cited by 77 · see citing works
Rad, E., Murray, J. T., & Tee, A. R. (2018) · Cancers · doi:10.3390/cancers10010005 · Cited by 73 · see citing works
Altered ribosomal function and protein synthesis caused by tau
Evans, H. T., Taylor, D. W., Kneynsberg, A., Bodea, L., & Götz, J. (2021) · Acta Neuropathologica Communications · doi:10.1186/s40478-021-01208-4 · Cited by 70 · see citing works
Fyfe, J. J., Bishop, D. J., Bartlett, J. D., Hanson, E. D., Anderson, M. J., Garnham, A. P., & Stepto, N. K. (2018) · Scientific Reports · doi:10.1038/s41598-017-18887-6 · Cited by 69 · see citing works
“In addition to mediating transient changes in translational efficiency, accumulating evidence suggests mTORC1 also plays a key role in regulating ribosome biogenesis (and therefore translational capacity) in skeletal muscle by regulating all three classes of RNA polymerases (RNA Pol-I to -III) 25 .”
BackgroundInfluentialWang, H., Shi, X., Gao, Y., Zhang, X., Zhao, H., Wang, L., Zhang, X., & Chen, R. (2022) · Environment International · doi:10.1016/j.envint.2022.107349 · Cited by 69 · see citing works
PHA-4/FoxA senses nucleolar stress to regulate lipid accumulation in Caenorhabditis elegans
Wu, J., Jiang, X., Li, Y., Zhu, T., Zhang, J., Zhang, Z., Zhang, L., Zhang, Y., Wang, Y., Zou, X., et al. (2018) · Nature Communications · doi:10.1038/s41467-018-03531-2 · Cited by 60 · see citing works
Induction of metabolic quiescence defines the transitional to follicular B cell switch
Farmer, J. R., Allard‐Chamard, H., Sun, N., Ahmad, M., Bertocchi, A., Mahajan, V. S., Aicher, T. P., Arnold, J., Benson, M. D., Morningstar, J. E., et al. (2019) · Science Signaling · doi:10.1126/scisignal.aaw5573 · Cited by 62 · see citing works
Synergistic antileukemic therapies in NOTCH1 -induced T-ALL
Sánchez-Martín, M., Ambesi‐Impiombato, A., Qin, Y., Herranz, D., Bansal, M., Girardi, T., Paietta, E. M., Tallman, M. S., Rowe, J. M., Keersmaecker, K. D., et al. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1611831114 · Cited by 61 · see citing works
“Key oncogenes and signaling pathways involved in the pathogenesis of T-ALL, including NOTCH1, MYC, and the PI3K-AKTmTOR pathway, participate in the regulation of ribosome biogenesis and translation (9, 28, 29).”
BackgroundRole of mTORC1 Controlling Proteostasis after Brain Ischemia
Pérez-Álvarez, M. J., Villa-González, M., Benito‐Cuesta, I., & Wandosell, F. G. (2018) · Frontiers in Neuroscience · doi:10.3389/fnins.2018.00060 · Cited by 60 · see citing works
“In addition, mTORC1 upregulates several steps of ribosome biogenesis including transcription of ribosomal RNA and ribosomal protein synthesis (Iadevaia et al., 2014).”
BackgroundRibosome profiling and dynamic regulation of translation in mammals
Gobet, C., & Naef, F. (2017) · Current Opinion in Genetics & Development · doi:10.1016/j.gde.2017.03.005 · Cited by 56 · see citing works
Bora, P., Gahurová, L., Mašek, T., Hauserová, A., Potěšil, D., Jansová, D., Šušor, A., Zdráhal, Z., Ajduk, A., Pospíšek, M., et al. (2021) · Communications Biology · doi:10.1038/s42003-021-02290-z · Cited by 57 · see citing works
Ribosome biogenesis in skeletal muscle: coordination of transcription and translation
von Walden, F. (2019) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00963.2018 · Cited by 57 · see citing works
Yan, H., Zheng, G., Qu, J., Yang, L., Huang, X., Zhang, E., & Cai, Z. (2019) · Journal of Cellular Physiology · doi:10.1002/jcp.28947 · Cited by 56 · see citing works
Rodríguez‐López, M., Gonzalez, S., Hillson, O., Tunnacliffe, E., Codlin, S., Tallada, V. A., Bähler, J., & Rallis, C. (2020) · Cell Reports · doi:10.1016/j.celrep.2020.02.058 · Cited by 55 · see citing works
“Our results reveal a transcription factor that not only controls RNA Pol II-mediated expression of genes functioning in translation- and metabolism-related processes but also globally inhibits RNA Pol III-mediated expression of tRNAs.”
BackgroundInfluentialSingle-cell analyses demonstrate that a heme–GATA1 feedback loop regulates red cell differentiation
Doty, R. T., Yan, X. S., Lausted, C. G., Munday, A. D., Yang, Z., Yi, D., Jabbari, N., Liu, L., Keel, S., Tian, Q., et al. (2018) · Blood · doi:10.1182/blood-2018-05-850412 · Cited by 54 · see citing works
Paul, R., Luo, M., Mo, X., Lu, J. L., Yeo, S. K., & Guan, J. (2020) · Breast Cancer Research · doi:10.1186/s13058-020-01298-3 · Cited by 52 · see citing works
“In addition, mTOR has been indicated to control multiple steps in ribosome biogenesis [44].”
Ravera, S., Dufour, C., Cesaro, S., Bottega, R., Faleschini, M., Cuccarolo, P., Corsolini, F., Usai, C., Columbaro, M., Cipolli, M., et al. (2016) · Scientific Reports · doi:10.1038/srep25441 · Cited by 51 · see citing works
Fine‐Tuning of Cholesterol Homeostasis Controls Erythroid Differentiation
Lu, Z., Huang, L., Li, Y., Xu, Y., Zhang, R., Zhou, Q., Sun, Q., Lu, Y., Chen, J., Shen, Y., et al. (2021) · Advanced Science · doi:10.1002/advs.202102669 · Cited by 47 · see citing works
Zhu, Z., Liu, J., Yang, C., Zhao, M., & Xiong, Z. (2019) · Cell Death and Disease · doi:10.1038/s41419-019-1627-9 · Cited by 45 · see citing works
Translational control by oncogenic signaling pathways.
Gao, B., & Roux, P. P. (2015) · Biochimica et Biophysica Acta · doi:10.1016/j.bbagrm.2014.11.006 · Cited by 48 · see citing works
Dual roles of mTORC1-dependent activation of the ubiquitin-proteasome system in muscle proteostasis
Kaiser, M. S., Milan, G., Ham, D. J., Lin, S., Oliveri, F., Chojnowska, K., Tintignac, L. A. J., Mittal, N., Zimmerli, C. E., Glass, D. J., et al. (2022) · Communications Biology · doi:10.1038/s42003-022-04097-y · Cited by 46 · see citing works
Maekawa, S., Ishida, T., & Yanagisawa, S. (2017) · The Plant Cell · doi:10.1105/tpc.17.00778 · Cited by 45 · see citing works
“…et al., 2008; Ishida et al., 2016), while exogenous sugar application increases the expression levels of a number of genes associated with ribosome biogenesis in Arabidopsis thaliana (Kojima et al., 2007), as well as yeast andmammalian cells (Powers andWalter, 1999; Iadevaia et al., 2014).”
BackgroundAn RNA damage response network mediates the lethality of 5-FU in colorectal cancer
Chen, J.-K., Merrick, K. A., Kong, Y. W., Izrael-Tomasevic, A., Eng, G. M., Handly, E. D., Patterson, J. C., Cannell, I. G., Suárez-López, L., Hosios, A. M., et al. (2024) · Cell Reports Medicine · doi:10.1016/j.xcrm.2024.101778 · Cited by 44 · see citing works
“Conversely, inhibition of mTORC1, a kinase complex that positively regulates ribosome biogenesis, 62 greatly decreased the cytotoxicity to 5-FUR (Figure S7B).”
Lim, C., Dismuke, T., Malawsky, D. S., Ramsey, J. D., Hwang, D., Godfrey, V., Kabanov, A. V., Gershon, T. R., & Sokolsky‐Papkov, M. (2022) · Science Advances · doi:10.1126/sciadv.abl5838 · Cited by 41 · see citing works
“regulation of translation (27), and we therefore analyzed whether mTORC1 activity was reduced in cells that remained proliferative during chronic palbociclib treatment.”
Ribosome-Directed Therapies in Cancer
Temaj, G., Chichiarelli, S., Eufemi, M., Fabio Altieri, F., Hadžiselimović, R., Farooqı, A. A., Yaylım, İ., & Saso, L. (2022) · Biomedicines · doi:10.3390/biomedicines10092088 · Cited by 43 · see citing works
Jin, C., Kang, H., Ryu, J. R., Kim, S., Zhang, Y., Lee, Y., Kim, Y., & Han, K. (2018) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2018.00250 · Cited by 41 · see citing works
“Moreover, it was previously reported that neuronal mTORC1 signaling, which regulates ribosome biogenesis and function (Jastrzebski et al., 2007; Iadevaia et al., 2014), can be altered by Shank3 overexpression or knock-down (Bidinosti et al.”
BackgroundSpatial Activation of TORC1 Is Regulated by Hedgehog and E2F1 Signaling in the Drosophila Eye
Kim, W., Jang, Y., Yang, J., & Chung, J. (2017) · Developmental Cell · doi:10.1016/j.devcel.2017.07.020 · Cited by 36 · see citing works
Ribosomal Proteins Control Tumor Suppressor Pathways in Response to Nucleolar Stress
Lessard, F., Brakier‐Gingras, L., & Ferbeyre, G. (2019) · BioEssays · doi:10.1002/bies.201800183 · Cited by 40 · see citing works
Ribosomal proteins: insight into molecular roles and functions in hepatocellular carcinoma
Xie, X., Guo, P., Yu, H., Wang, Y., & Chen, G. (2017) · Oncogene · doi:10.1038/onc.2017.343 · Cited by 39 · see citing works
Exploiting cancer vulnerabilities: mTOR, autophagy, and homeostatic imbalance
Johnson, C. E., & Tee, A. R. (2017) · Essays in Biochemistry · doi:10.1042/ebc20170056 · Cited by 39 · see citing works
“To rapidly increase cellular biomass, mTORC1 promotes ribosomal biogenesis to enhance the cell’s protein translation machinery (reviewed in [1]).”
Zhu, T., Li, L., Feng, L., Mo, H., & Ren, M. (2020) · Frontiers in Genetics · doi:10.3389/fgene.2020.00186 · Cited by 39 · see citing works
“TORC1 positively regulates multiple steps including ribosomal RNAs transcription, the synthesis of ribosomal proteins and other components in ribosome biogenesis (Iadevaia et al., 2014; Kos-Braun and Kos, 2017).”
BackgroundSIRT7: a novel molecular target for personalized cancer treatment?
Ianni, A., Kumari, P., Tarighi, S., Braun, T. W., & Vaquero, A. (2024) · Oncogene · doi:10.1038/s41388-024-02976-8 · Cited by 41 · see citing works
“Given the clear role of mTOR activation in the stimulation of ribosome biogenesis and protein synthesis [65], it is intriguingly to speculate that in this type of malignancy SIRT7 may sustain cancer cells growth by stimulating these functions.”
BackgroundTranslation Stress Regulates Ribosome Synthesis and Cell Proliferation
Gnanasundram, S. V., & Fåhræus, R. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19123757 · Cited by 38 · see citing works
“Although mTORC1 was known to regulate RiBi in most of the cases rather than mTORC2, it was reported that mTORC2 interacts with mature ribosomes and promotes the AKT survival pathway in proliferating cells [13,41] (see reviews [13,40]).”
BackgroundAcetylation-mediated remodeling of the nucleolus regulates cellular acetyl-CoA responses
Houston, R., Sekine, S., Calderon, M. J., Seifuddin, F., Wang, G., Kawagishi, H., Malide, D. A., Li, Y., Guček, M., Pirooznia, M., et al. (2020) · PLoS Biology · doi:10.1371/journal.pbio.3000981 · Cited by 37 · see citing works
“processing are regulated by multiple mechanisms through nutrient signaling pathways to meet the cellular energy demands [52,53].”
BackgroundSolsona, R., Pavlin, L., Bernardi, H., & Sanchez, A. M. J. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22052741 · Cited by 39 · see citing works
Wang, T., Zhang, W., Wang, Z., Wu, Z., Du, B., Li, L., Chen, Y., Yang, X., Hao, X., & Guo, T. (2019) · Cancer Medicine · doi:10.1002/cam4.2810 · Cited by 36 · see citing works
Brook, M. S., Wilkinson, D. J., Mitchell, W. K., Lund, J. L., Phillips, B. E., Szewczyk, N. J., Kainulainen, H., Lensu, S., Koch, L. G., Britton, S. L., et al. (2017) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00157.2017 · Cited by 34 · see citing works
“Once again, RNA 407 synthesis was correlated with MPS which further validates that in muscle, ribosome and 408 protein metabolism are likely to be inextricably related (likely via mTORc1 (18)).”
MethodSyndecan-1 in liver pathophysiology
Reszegi, A., Tátrai, P., Regős, E., Kovalszky, I., & Baghy, K. (2022) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00039.2022 · Cited by 35 · see citing works
TMEM116 is required for lung cancer cell motility and metastasis through PDK1 signaling pathway
Zhang, S., Dai, H., Li, W., Wang, R., Wu, H., Shen, M., Hu, Y., Xie, L., & Xing, Y. (2021) · Cell Death and Disease · doi:10.1038/s41419-021-04369-1 · Cited by 35 · see citing works
“SC79 is a unique specific AKT activator, and directly enhances phosphorylation of all AKT isoforms and increases AKT activity in multiple cell types [30].”
BackgroundMonomethyl branched-chain fatty acid mediates amino acid sensing upstream of mTORC1
Zhu, M., Teng, F., Li, N., Zhang, L., Zhang, S., Xu, F., Shao, J., Sun, H., & Zhu, H. (2021) · Developmental Cell · doi:10.1016/j.devcel.2021.09.010 · Cited by 34 · see citing works
Navigating the Host Cell Response during Entry into Sites of Latent Cytomegalovirus Infection
Murray, M. J., Peters, N., & Reeves, M. B. (2018) · Pathogens · doi:10.3390/pathogens7010030 · Cited by 33 · see citing works
“TSC1/2 inhibits mammalian target of rapamycin complex 1 (mTORC1) function, thereby inhibiting translation of proteins and ribosome biogenesis [91,92].”
BackgroundTOR mediates the autophagy response to altered nucleotide homeostasis in an RNase mutant
Kazibwe, Z., Soto-Burgos, J., MacIntosh, G. C., & Bassham, D. C. (2020) · Journal of Experimental Botany · doi:10.1093/jxb/eraa410 · Cited by 33 · see citing works
He, J., Yang, Y., Zhang, J., Chen, J.-Z., Wei, X., He, J., & Luo, L. (2017) · Journal of genetics and genomics/Journal of Genetics and Genomics · doi:10.1016/j.jgg.2017.09.013 · Cited by 31 · see citing works
Functional Characterization of Target of Rapamycin Signaling in Verticillium dahliae
Li, L., Zhu, T., Song, Y., Luo, X., Feng, L., Zhuo, F., Li, F., & Ren, M. (2019) · Frontiers in Microbiology · doi:10.3389/fmicb.2019.00501 · Cited by 30 · see citing works
“…TOR) and LST8 (lethal with SEC thirteen 8), which controls cell growth by regulating translation, transcription and autophagy (Wang and Proud, 2009; Iadevaia et al., 2014; Dobrenel et al., 2016); whereas, those of TORC2 are TOR, RICTOR (rapamycininsensitive companion of TOR), SIN1…”
BackgroundShao, J., Shi, T., Yu, H. T., Ding, Y., Li, L., Wang, X., & Wang, X. (2021) · The EMBO Journal · doi:10.15252/embj.2020107480 · Cited by 30 · see citing works
Cytosolic pH regulates proliferation and tumour growth by promoting expression of cyclin D1
Koch, L. M., Birkeland, E. S., Battaglioni, S., Helle, X., Meerang, M., Hiltbrunner, S., Ibáñez, A. J., Peter, M., Fontecedro, A. C., Opitz, I., et al. (2020) · Nature Metabolism · doi:10.1038/s42255-020-00297-0 · Cited by 30 · see citing works
Proteomic landscape of TGF-β1-induced fibrogenesis in renal fibroblasts
Zhou, S., Yin, X., Mayr, M., Noor, M., Hylands, P. J., & Xu, Q. (2020) · Scientific Reports · doi:10.1038/s41598-020-75989-4 · Cited by 30 · see citing works
Glutamine deficiency in solid tumor cells confers resistance to ribosomal RNA synthesis inhibitors
Pan, M., Zorbas, C., Sugaya, M., Ishiguro, K., Kato, M., Nishida, M., Zhang, H., Candeias, M. M., Okamoto, A., Ishikawa, T., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-31418-w · Cited by 30 · see citing works
Self-citationJensen, K. B., Dredge, B. K., Toubia, J., Jin, X., Iadevaia, V., Goodall, G. J., & Proud, C. G. (2021) · Nucleic Acids Research · doi:10.1093/nar/gkab604 · Cited by 27 · see citing works
“This may provide a further way in which mTORC1 signalling promotes ribosome biogenesis (38).”
BackgroundSelf-citationMartin, E. T., Blatt, P., Nguyen, E., Lahr, R. M., Selvam, S., Yoon, H. A. M., Pocchiari, T., Emtenani, S., Siekhaus, D. E., Berman, A. J., et al. (2022) · Developmental Cell · doi:10.1016/j.devcel.2022.03.005 · Cited by 29 · see citing works
KMT2D Deficiency Promotes Myeloid Leukemias which Is Vulnerable to Ribosome Biogenesis Inhibition
Xu, J., Zhong, A., Zhang, S., Chen, M., Zhang, L., Hang, X., Zheng, J., Wu, B., Deng, X., Pan, X., et al. (2023) · Advanced Science · doi:10.1002/advs.202206098 · Cited by 28 · see citing works
TOR signaling regulates liquid phase separation of the SMN complex governing snRNP biogenesis
Schilling, M., Prusty, A. B., Boysen, B. M. M., Oppermann, F. S., Riedel, Y. L., Husedzinovic, A., Rasouli, H., König, A., Ramanathan, P., Reymann, J., et al. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.109277 · Cited by 28 · see citing works
Yang, X., Wang, X., Hu, L.-P., Feng, M., Zhou, Y.-Q., Li, D., Li, J., Miao, X.-C., Zhang, Y., Yao, L.-L., et al. (2023) · Gastroenterology · doi:10.1053/j.gastro.2023.05.029 · Cited by 28 · see citing works
mRNA cap-binding protein eIF4E1 is a novel regulator of Toxoplasma gondii latency
Holmes, M. J., Bastos, M. S. E., Dey, V., Severo, V. R., Wek, R. C., & Sullivan, W. J. (2024) · mBio · doi:10.1128/mbio.02954-23 · Cited by 27 · see citing works
“Conse quently, the expression of these proteins and hence ribosome abundance is correlated with nutrient availability (37).”
BackgroundRegulation of RNA Polymerase I Stability and Function
Pitts, S., & Laiho, M. (2022) · Cancers · doi:10.3390/cancers14235776 · Cited by 22 · see citing works
Liu, L., Xiao, B., Hirukawa, A., Smith, H. W., Zuo, D., Sanguin‐Gendreau, V., McCaffrey, L. M., Nam, A. J., & Muller, W. J. (2023) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2303010120 · Cited by 25 · see citing works
Comprehensive analysis of the ubiquitinome during oncogene-induced senescence in human fibroblasts
Bengsch, F., Tu, Z., Tang, H., Zhu, H., Speicher, D. W., & Zhang, R. (2015) · Cell Cycle · doi:10.1080/15384101.2015.1026492 · Cited by 27 · see citing works
“These effectors control protein synthesis by regulating cap-dependent translation of mRNAs, ribosome biogenesis and tRNA loading.(20,26,27) Since K-e-G-G MS/MS does not discriminate between poly- and monoubiquitinated sites, 17 detection of an enhanced ubiquitination implies either increased degradation of the target…”
BackgroundLoss of REDD1 augments the rate of the overload-induced increase in muscle mass
Gordon, B. S., Liu, C., Steiner, J. L., Nader, G. A., Jefferson, L. S., & Kimball, S. R. (2016) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00159.2016 · Cited by 27 · see citing works
“The ribosome content of a cell has been proposed to impose an upper limit to the rate of protein synthesis (20).”
BackgroundMa, X., Jia, Q., Li, S., Chen, Z., Ming, X., Zhao, Y. J., & Zhou, D. (2023) · Plant Communications · doi:10.1016/j.xplc.2023.100560 · Cited by 26 · see citing works
“TOP motifs are found mainly in mRNAs that encode r-proteins and translation factors (Fonseca et al., 2014; Iadevaia et al., 2014).”
Background
- Authors
- Iadevaia, V., Liu, R., & Proud, C. G.
- Affiliations
- University of Southampton (GB)
- Corresponding author
- Proud, Christopher G.
- Venue
- Seminars in Cell & Developmental Biology
- Publisher
- Elsevier BV
- Published
- 2014-12
- Volume
- 36
- Pages
- 113-120
- ISSN
- 1084-9521 (ISSN-L)
- OpenAlex
- W1965611273
- Cited by
- 248
- References
- 95
- Citations by year
- 2026: 10 · 2025: 25 · 2024: 19 · 2023: 28 · 2022: 29 · 2021: 29 · 2020: 20 · 2019: 21 · 2018: 26 · 2017: 18 · 2016: 11 · 2015: 9 · 2014: 3
- FWCI
- 1.29
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Seminars in Cell and Developmental Biology (publishedVersion)
- PubMed (publishedVersion)
- Open Research (University of Surrey) (submittedVersion)
- Adelaide Research & Scholarship (AR&S) (University of Adelaide) (submittedVersion)
- Surrey Research Insight Open Access (The University of Surrey) (submittedVersion)
- Funders
- Cancer Research UK
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › PI3K/AKT/mTOR signaling in cancer
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Biochemical and Molecular Research
- Keywords
- mTORC1 signaling, ribosome biogenesis, rDNA transcription, ribosomal protein synthesis, ribosome assembly, nutrient signaling, kinase regulation
- MeSH terms
- Mechanistic Target of Rapamycin Complex 1, Humans, Ribosomal Proteins, Ribosomes, RNA Polymerase I, RNA Polymerase III, RNA, Ribosomal, Protein Biosynthesis, Signal Transduction, 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