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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.
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“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]
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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
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
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
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
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
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
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
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
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
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
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Ben‐Sahra, I., & Manning, B. D. (2017) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2017.02.012 · Cited by 668
“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 379
“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
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BackgroundMolecular logic of mTORC1 signalling as a metabolic rheostat
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“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
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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
“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
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“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).”
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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
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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 145
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
“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.”
BackgroundThe ribosome, (slow) beating heart of cancer (stem) cell
Bastide, A., & David, A. (2018) · Oncogenesis · doi:10.1038/s41389-018-0044-8 · Cited by 125
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 126
Self-citationLiu, R., & Proud, C. G. (2016) · Acta Pharmacologica Sinica · doi:10.1038/aps.2015.123 · Cited by 117
Self-citationAntignano, I., Liu, Y., Offermann, N., & Capasso, M. (2023) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-023-04775-y · Cited by 117
Signaling, 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 126
“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 116
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BackgroundRegulation of rDNA transcription in response to growth factors, nutrients and energy
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“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
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“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.”
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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 85
“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 80
“…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…”
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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
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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 60
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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
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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
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Maekawa, S., Ishida, T., & Yanagisawa, S. (2017) · The Plant Cell · doi:10.1105/tpc.17.00778 · Cited by 45
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“regulation of translation (27), and we therefore analyzed whether mTORC1 activity was reduced in cells that remained proliferative during chronic palbociclib treatment.”
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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 40
“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.”
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Lessard, F., Brakier‐Gingras, L., & Ferbeyre, G. (2019) · BioEssays · doi:10.1002/bies.201800183 · Cited by 40
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
Exploiting cancer vulnerabilities: mTOR, autophagy, and homeostatic imbalance
Johnson, C. E., & Tee, A. R. (2017) · Essays in Biochemistry · doi:10.1042/ebc20170056 · Cited by 40
“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 40
“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 43
“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 39
“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
“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 42
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 38
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
“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
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
“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 31
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 36
“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
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
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 31
“…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
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
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 33
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 32
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 28
“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 26
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 30
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
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 27
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
“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. C., & Laiho, M. (2022) · Cancers · doi:10.3390/cancers14235776 · Cited by 33
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 26
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 28
“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 28
“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
“TOP motifs are found mainly in mRNAs that encode r-proteins and translation factors (Fonseca et al., 2014; Iadevaia et al., 2014).”
Background
Metadata
- 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
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