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Regulation of Translation Initiation in Eukaryotes: Mechanisms and Biological Targets
Open accessAbstract
Translational control in eukaryotic cells is critical for gene regulation during nutrient deprivation and stress, development and differentiation, nervous system function, aging, and disease. We describe recent advances in our understanding of the molecular structures and biochemical functions of the translation initiation machinery and summarize key strategies that mediate general or gene-specific translational control, particularly in mammalian systems.
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“Both transcription and translation are strongly affected by exact DNA and mRNA sequences, respectively, as well as their cellular environments (Sonenberg and Hinnebusch, 2009; Alpert et al., 2017).”
From Evaluating Efficiencies of Dual AAV Approaches for Retinal Targeting (2017) · cites this paper as Sonenberg and Hinnebusch, 2009
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“Translation of a uORFs can modulate the expression of the downstream protein-coding gene in response to global (Sonenberg and Hinnebusch, 2009) or gene-specific regulatory signals (Medenbach et al., 2011).”
From Ribosome Profiling of Mouse Embryonic Stem Cells Reveals the Complexity and Dynamics of Mammalian Proteomes (2011) · cites this paper as Sonenberg and Hinnebusch, 2009
In the citing paper
“which, like NIBAN1, phosphorylates EIF4EBP1 to allow assembly of the initiation complex23”
From NEAT-seq: simultaneous profiling of intra-nuclear proteins, chromatin accessibility and gene expression in single cells (2022) · cites this paper as [23]
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“Even for those studies concluding that inhibition occurs at the level of translation initiation, the data are conflicting as in some studies translation inhibition was cap dependent and mediated by eIF4F, whereas in others it was cap independent and mediated via eIF6 (Filipowicz et al., 2008).”
Self-citationThe impact of microRNAs on protein output
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Widespread changes in protein synthesis induced by microRNAs
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“It is noteworthy that recent large-scale studies in cells demonstrated that the magnitude of translation inhibition of most mRNAs is moderate (~2-fold) (Baek et al., 2008; Selbach et al., 2008), and that similar results were obtained in cell-free translation extracts.”
Switching from Repression to Activation: MicroRNAs Can Up-Regulate Translation
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“Surprisingly, it was reported recently that miRNAs can also stimulate rather than inhibit translation when cells enter quiescence (Vasudevan et al., 2007).”
Reinitiation involving upstream ORFs regulates ATF4 mRNA translation in mammalian cells
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Multiple Roles of the Stress Sensor GCN2 in Immune Cells
Zhao, C., Guo, H., Hou, Y., Tong, L., Wei, D., & Zhao, Y. X. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24054285 · Cited by 42
“In yeast, phosphorylation of eIF-2α by phosphorylated GCN2 decreases eIF-2-GTP levels and eliminates the (ternary complex) TC’s inhibitory effects of the upstream open reading frames (uORFs) of GCN4 mRNA, thereby promoting GCN4 translation and blocking general translation [61].”
BackgroundRegulation and outcomes of localized RNA translation
Gasparski, A. N., Mason, D. E., Moissoglu, K., & Mili, S. (2022) · Wiley Interdisciplinary Reviews - RNA · doi:10.1002/wrna.1721 · Cited by 33
“Phosphorylation of eIF2α is a key regulatory mechanism for adjusting protein synthesis in response to internal or external cues (Sonenberg & Hinnebusch, 2009). eIF2a phosphorylation is carried out by one of four members of the eIF2α kinase family leading to a decrease in global protein synthesis…”
BackgroundRegulation of cancer progression by circRNA and functional proteins
Chen, J., Gu, J., Tang, M., Liao, Z., Tang, R., Zhou, L., Su, M., Jiang, J., Hu, Y., Chen, Y., et al. (2021) · Journal of Cellular Physiology · doi:10.1002/jcp.30608 · Cited by 55
“…m6A reader YTH N6‐methyladenosine RNA binding protein 3 (YTHDF3), and is enhanced by methyltransferase like 3/methyltransferase like 14 (METTL3/14), inhibited by demethylase fat mass and obesity associated (FTO) (Liu et al., 2014; Ping et al., 2014; Sonenberg & Hinnebusch, 2009; Wang et al., 2014).”
BackgroundTissue- and stage-specific landscape of the mouse translatome
Wang, H., Wang, Y., Yang, J., Zhao, Q. C., Tang, N., Chen, C., Li, H., Cheng, C., Xie, M., Yang, Y., et al. (2021) · Nucleic Acids Research · doi:10.1093/nar/gkab482 · Cited by 44
“Not present in any of the analyzed tissues (under cutoff) Group-enriched At least five-fold higher expression in a group of tissues (2-5)”
BackgroundAngiogenin (ANG)—Ribonuclease Inhibitor (RNH1) System in Protein Synthesis and Disease
Sarangdhar, M. A., & Allam, R. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22031287 · Cited by 41
“Interestingly, during evolution, from bacteria to mammals, a cell has minimally evolved its core translational machinery, however, the regulatory mechanisms to control protein translation are increasingly advanced [7].”
BackgroundKirby, T. J. (2019) · Journal of Applied Physiology · doi:10.1152/japplphysiol.01031.2018 · Cited by 37
Song, J., Li, H., Liu, Y., Li, X., Shi, Q., Lei, Q., Hu, W., Huang, S., Chen, Z., & He, X. (2023) · Advanced Science · doi:10.1002/advs.202302425 · Cited by 37
Protein translation paradox: Implications in translational regulation of aging
Kim, H. S., & Pickering, A. M. (2023) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2023.1129281 · Cited by 43
“The first initiation phase of protein translation is a rate limiting step, where most regulations are exerted (Gebauer and Hentze 2004; Sonenberg and Hinnebusch 2009; Jackson et al., 2010).”
BackgroundInfluentialImaging translational control by Argonaute with single-molecule resolution in live cells
Cialek, C. A., Galindo, G., Morisaki, T., Zhao, N., Montgomery, T. A., & Stasevich, T. J. (2022) · Nature Communications · doi:10.1038/s41467-022-30976-3 · Cited by 37
Ricciardi, A., Bennuru, S., Tariq, S., Kaur, S., Wu, W., ELKAHLOUN, A. G., Arakelyan, A., Shaik, J. S., Dorward, D. W., Nutman, T. B., et al. (2021) · PLoS neglected tropical diseases · doi:10.1371/journal.pntd.0008884 · Cited by 45
“mTORC1 regulates mRNA synthesis and protein translation as two of its main downstream targets include ribosomal subunit p70S6 kinase 1 (S6K) and eukaryotic initiation factor 4E-binding protein (4E-BP) [18].”
BackgroundFreitas-de-Sousa, L. A., Nachtigall, P. G., Portes-Junior, J. A., Holding, M. L., Nystrom, G. S., Ellsworth, S. A., Guimarães, N. D. C., Tioyama, E. C., Ortiz, F. R., Silva, B. R., et al. (2020) · Toxins · doi:10.3390/toxins12120791 · Cited by 44
“Translation initiation factors enhance translation by stabilizing mRNA and ribosomal complexes and may act as a translational regulatory mechanism [63], while microRNAs play important roles in regulating gene expression by interacting with the 3′ untranslated region of target mRNAs, inducing mRNA degradation and trans…”
BackgroundEmerging translation strategies during virus–host interaction
Hoang, H., Neault, S., Pelin, A., & Alain, T. (2020) · Wiley Interdisciplinary Reviews - RNA · doi:10.1002/wrna.1619 · Cited by 39
“The eIFs are then released and the 60S ribosomal subunit is recruited to the 40S ribosomal subunit, forming an elongation competent 80S monosome (Jackson, Hellen, & Pestova, 2010; Sonenberg & Hinnebusch, 2009).”
BackgroundEmerging Roles of Gemin5: From snRNPs Assembly to Translation Control
Martínez-Salas, E., Embarc-Buh, A., & Francisco-Velilla, R. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21113868 · Cited by 37
Svitkin, Y. V., Gingras, A., & Sonenberg, N. (2021) · Nucleic Acids Research · doi:10.1093/nar/gkab1241 · Cited by 38
“PKR, among other cellular functions, represses translation under conditions of cellular stress or virus infection by phosphorylating the (cid:2) -subunit of translation initiation factor 2 (eIF2 (cid:2) ) (16,17). eIF2, which is composed of three subunits (cid:2) , (cid”
Self-citationT cells at work: How post‐transcriptional mechanisms control T cell homeostasis and activation
Jurgens, A. P., Popović, B., & Wolkers, M. C. (2021) · European Journal of Immunology · doi:10.1002/eji.202049055 · Cited by 42
Roles of HIF and 2-Oxoglutarate-Dependent Dioxygenases in Controlling Gene Expression in Hypoxia
Frost, J., Frost, M. G., Batie, M., Jiang, H., & Rocha, S. (2021) · Cancers · doi:10.3390/cancers13020350 · Cited by 47
“mTOR inhibition also causes hypophosphorylation of Eukaryotic Translation Initiation Factor (eIF) 4E Binding Protein 1 (eIF4EBP1), allowing the sequestering of eIF4E and decrease of 5’cap-dependent initiation [246,247].”
BackgroundFatal attraction: The roles of ribosomal proteins in the viral life cycle
Miller, C. M., Selvam, S., & Fuchs, G. (2020) · Wiley Interdisciplinary Reviews - RNA · doi:10.1002/wrna.1613 · Cited by 36
“Translation of eukaryotic messenger RNAs (mRNAs) has been very well reviewed elsewhere and is only briefly recapped here (Hershey, Sonenberg, & Mathews, 2018; Sonenberg & Hinnebusch, 2009).”
BackgroundMethodNon-canonical mRNA translation initiation in cell stress and cancer
Mahé, M., Rios-Fuller, T. J., Katsara, O., & Schneider, R. J. (2024) · NAR Cancer · doi:10.1093/narcan/zcae026 · Cited by 37
Translation machinery: the basis of translational control
Shu, Y., Zhou, G., & Xu, G. (2023) · Journal of genetics and genomics/Journal of Genetics and Genomics · doi:10.1016/j.jgg.2023.07.009 · Cited by 50
Long noncoding RNAs in cardiovascular disease
Kohlmaier, A., Holdt, L. M., & Teupser, D. (2023) · Current Opinion in Cardiology · doi:10.1097/hco.0000000000001041 · Cited by 39
Dang, T. T., Kim, M., Lee, Y. Y., Le, H. T., Kim, K. H., Nam, S., Hyun, S. H., Kim, H. L., Chung, S. W., Chung, H., et al. (2023) · Autophagy · doi:10.1080/15548627.2023.2173900 · Cited by 42
“ATF6[1-373]-expressing adenoviruses for 24 h were treated with DMSO or Tm (1 μg/mL) for 24 h.”
BackgroundMethodInfluentialCPEB3 functions as a tumor suppressor in colorectal cancer via JAK/STAT signaling
Fang, Y., Zhong, Q., Wang, Y., Gu, C.-C., Liu, S., Li, A., & Yan, Q. (2020) · Aging · doi:10.18632/aging.103893 · Cited by 44
“Data accumulated in recent years support the role of post-transcriptional regulation in cancer oncogenesis [14].”
BackgroundJeevakumar, V., Sardar, A. K. A., Mohamed, F., Smithhart, C. M., Price, T. J., & Dussor, G. O. (2020) · Journal of Neurophysiology · doi:10.1152/jn.00188.2020 · Cited by 40
Optimization of the 5ʹ untranslated region of mRNA vaccines
Ma, Q., Zhang, X., Yang, J., Li, H., Hao, Y., & Feng, X. (2024) · Scientific Reports · doi:10.1038/s41598-024-70792-x · Cited by 30
Inyang, K. E., Evans, C. M., Heussner, M., Petroff, M. G., Reimers, M., Vermeer, P. D., Tykocki, N. R., Folger, J. K., & Laumet, G. O. (2022) · Pain · doi:10.1097/j.pain.0000000000003045 · Cited by 39
Fakih, Z., Plourde, M. B., & Germain, H. (2023) · Biomolecules · doi:10.3390/biom13071160 · Cited by 33
“It has been shown that translational regulation mainly takes place during the initiation steps [85].”
BackgroundUncovering the Underlying Mechanisms of Ketamine as a Novel Antidepressant
Xu, S., Yao, X., Li, B., Cui, R., Zhu, C., Wang, Y., & Yang, W. (2022) · Frontiers in Pharmacology · doi:10.3389/fphar.2021.740996 · Cited by 53
“mTORC1 participates in cap-dependent initiation of mRNA translation via its downstream target 4E-BPs (Sonenberg and Hinnebusch, 2009).”
BackgroundKawa, A. B., Hwang, E.-K., Funke, J. R., Zhou, H., Costa‐Mattioli, M., & Wolf, M. E. (2022) · Biological Psychiatry · doi:10.1016/j.biopsych.2022.05.008 · Cited by 29
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“considered a more rapid and direct strategy for environmental response [42].”
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“During eukaryotic translation initiation, Met-tRNAi is recruited by eIF2, a heterotrimeric factor that binds the tRNA in a GTP-dependent manner (Hinnebusch et al., 2007; Sonenberg and Hinnebusch, 2009).”
Barrado-Gil, L., del Puerto, A., Muñoz-Moreno, R., Galindo, I., Cuesta-Geijo, M. A., Urquiza, J., Nistal-Villán, E., de Motes, C. M., & Alonso, C. (2020) · Frontiers in Microbiology · doi:10.3389/fmicb.2020.622907 · Cited by 32
“The eIF4E-binding proteins (4E-BPs) are well-known translational repressors of the cap-dependent translation (Sonenberg and Hinnebusch, 2009).”
BackgroundNutrient Control of mRNA Translation
Shu, X. E., Swanda, R. V., & Qian, S. (2020) · Annual Review of Nutrition · doi:10.1146/annurev-nutr-120919-041411 · Cited by 39
“It is becoming increasingly evident that the regulation of translation provides the cell with the plasticity to respond to rapid changes in the environment (149).”
BackgroundBlanco, N., Williams, A. J., Tang, D., Zhan, D., Misaghi, S., Kelley, R. F., & Simmons, L. C. (2020) · Biotechnology and Bioengineering · doi:10.1002/bit.27347 · Cited by 32
“…the Kozak sequence affect translation initiation both in higher (Kozak, 1986) and lower (Dvir et al., 2013; Wallace et al., 2020) eukaryotes and have been associated with the development of human diseases, including cancer, and metabolic disorders (Mohan et al., 2014; Sonenberg & Hinnebusch, 2009).”
BackgroundThe mTORC1/S6K/PDCD4/eIF4A Axis Determines Outcome of Mitotic Arrest
Moustafa-Kamal, M., Kucharski, T. J., El-Assaad, W., Abbas, Y. M., Gandin, V., Nagar, B., Pelletier, J., Topisirovic, I., & Teodoro, J. G. (2020) · Cell Reports · doi:10.1016/j.celrep.2020.108230 · Cited by 31
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“Then, the assembled 80S elongating ribosome synthesizes a new protein before terminating at a stop codon 18,19 .”
Saaoud, F., Lu, Y., Xu, K., Shao, Y., Praticò, D., Vázquez-Padrón, R. I., Wang, H., & Yang, X. (2024) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2024.108604 · Cited by 33
Bile proteome reveals biliary regeneration during normothermic preservation of human donor livers
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“Speci fi cally, upregulation of eukaryote initiation factors (EIFs), implicated in ribosomal complex formation necessary for protein synthesis, suggest compensatory mechanisms as a suboptimal cellular repair response to biliary injury 35 .”
Moya‐Alvarado, G., Guerra, M. V., Tiburcio, R., Bravo, E., & Bronfman, F. C. (2022) · Neurobiology of Disease · doi:10.1016/j.nbd.2022.105796 · Cited by 32
“mTOR forms part of the TORC1 complex that coordinates CAP-dependent mRNA translation by phosphorylating components of the translational machinery (Foster and Fingar, 2010; Oh and Jacinto, 2011; Sonenberg and Hinnebusch, 2009) and its activity has been located to late endosomes and lysosome (Fig.”
De, S., & Mühlemann, O. (2022) · RNA Biology · doi:10.1080/15476286.2022.2065116 · Cited by 35
mCherry contains a fluorescent protein isoform that interferes with its reporter function
Fages-Lartaud, M., Tietze, L., Elie, F., Lale, R., & Hohmann-Marriott, M. F. (2021) · bioRxiv · doi:10.3389/fbioe.2022.892138 · Cited by 31
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Spatiotemporal regulation of maternal mRNAs during vertebrate oocyte meiotic maturation
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CRAFT: a bioinformatics software for custom prediction of circular RNA functions
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“In brief, eIF2 delivers the initiator methionyl tRNA (Met‐tRNAiMet) to the 40S subunit of the ribosome to form the 43S complex, permitting subsequent translation (67).”
BackgroundHan, S., Wang, X., Guan, J., Wu, J., Zhang, Y., Li, P., Liu, Z., Abdullah, S. W., Zhang, Z., Ye, J., et al. (2021) · Journal of Virology · doi:10.1128/jvi.00238-21 · Cited by 29
“In eukaryotic cells, translation initiation occurs through two alternative mechanisms, a classical cap-dependent mechanism for most eukaryotic mRNAs and a 59-end-independent mechanism driven by internal ribosome entry site (IRES) elements (1, 2).”
BackgroundmTORC2 Assembly Is Regulated by USP9X-Mediated Deubiquitination of RICTOR.
Wrobel, L., Siddiqi, F. H., Hill, S. M., Son, S.-M., Karabiyik, C., Kim, H., & Rubinsztein, D. (2020) · Cell Reports · doi:10.1016/j.celrep.2020.108564 · Cited by 30
Making ends meet: New functions of mRNA secondary structure
Ermolenko, D. N., & Mathews, D. H. (2020) · Wiley Interdisciplinary Reviews - RNA · doi:10.1002/wrna.1611 · Cited by 28
“CPEB•Maskin binds to eIF4E•5’ cap and displaces eIF4G (Sonenberg & Hinnebusch, 2009).”
BackgroundLaila, U. E., An, W., & Xu, Z.-X. (2024) · Frontiers in Immunology · doi:10.3389/fimmu.2024.1448489 · Cited by 34
Zaid, A. K. M. A., & Ariel, A. (2024) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2024.115204 · Cited by 35
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“9 However, for stress-responsive transcripts containing upstream open reading frames (uORFs), a reduction in the available eIF2 complex allows the initiation complex to bypass the uORF inhibition and translate the main ORFs (mORFs).”
Rubio, A., Garland, G. D., Sfakianos, A., Harvey, R. F., & Willis, A. E. (2022) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2022.04.006 · Cited by 35
Targeting translation: a promising strategy for anticancer metallodrugs
Ortega, E., Vigueras, G., Ballester, F. J., & Ruiz, J. (2021) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2021.214129 · Cited by 44
mTORC1 Crosstalk With Stress Granules in Aging and Age-Related Diseases
Sandoval, M. C., Heberle, A. M., Rehbein, U., Barile, C., Pittol, J. M. R., & Thedieck, K. (2021) · Frontiers in Aging · doi:10.3389/fragi.2021.761333 · Cited by 30
Tumor suppressor p53 restrains cancer cell dissemination by modulating mitochondrial dynamics
Phan, T. T. T., Lin, Y., Chou, Y., Wu, C., & Lin, L. (2022) · Oncogenesis · doi:10.1038/s41389-022-00401-x · Cited by 34
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Reciprocal control of translation and transcription in autism spectrum disorder
Longo, F., & Klann, E. (2021) · EMBO Reports · doi:10.15252/embr.202052110 · Cited by 29
“…(mammalian/ mechanistic target of rapamycin complex 1) and ERK (extracellular signal-regulated kinase) are dysregulated in several types of ASD (Sonenberg & Hinnebusch, 2009; Darnell & Klann, 2013), resulting in increased net de novo protein synthesis, which in turn leads to altered synaptic…”
Arthropods Under Pressure: Stress Responses and Immunity at the Pathogen-Vector Interface
Rosche, K. L., Sidak‐Loftis, L. C., Hurtado, J., Fisk, E. A., & Shaw, D. K. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2020.629777 · Cited by 40
microRNA-induced translational control of antiviral immunity by the cap-binding protein 4EHP
Zhang, X., Chapat, C., Wang, P., Choi, J., Li, Q., Luo, J., Wiebe, S. A., Kim, S., Robichaud, N., Karam, I. F., et al. (2021) · Molecular Cell · doi:10.1016/j.molcel.2021.01.030 · Cited by 30
Self-citationMNK2 governs the macrophage antiinflammatory phenotype
Bartish, M., Tong, D., Pan, Y., Wallerius, M., Liu, H., Ristau, J., Ferreira, S. D. S., Wallmann, T., van Hoef, V., Masvidal, L., et al. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1920377117 · Cited by 34
“The eukaryotic initiation factor (eIF) 4F (eIF4F) complex, whose activity is primarily regulated via its 5′ mRNA cap-binding subunit eIF4E, is a central node controlling initiation of translation (18).”
BackgroundBuoso, E., Masi, M., Long, A., Chiappini, C., Travelli, C., Govoni, S., & Racchi, M. (2020) · British Journal of Pharmacology · doi:10.1111/bph.15218 · Cited by 29
“…represents 10% of total translation but becomes the main translation mechanism for some mRNA under stress conditions, including proliferative disorders, viral infection, and mitosis, in order to allow protein synthesis when the cap-dependent pathway is inhibited (Sonenberg & Hinnebusch, 2009).”
BackgroundeIF4F is a thermo-sensing regulatory node in the translational heat shock response.
Altamirano, C. D., Kang, M.-K., Jordan, M. A., Borianne, T., Dilmen, I., Gnädig, M., von Appen, A., Honigmann, A., Franzmann, T. M., & Alberti, S. (2024) · Molecules and Cells · doi:10.1016/j.molcel.2024.02.038 · Cited by 28
Dong, J.-N., Zhao, Z.-K., Wang, Z., Li, S., Zhang, Y.-P., Sun, Z., Qin, G.-X., Zhang, X.-F., Zhao, W., Aschalew, N. D., et al. (2023) · Journal of Hazardous Materials · doi:10.1016/j.jhazmat.2023.133376 · Cited by 28
Fujii, K., Zhulyn, O., Byeon, G. W., Genuth, N. R., Kerr, C. H., Walsh, E. M., & Barna, M. (2021) · Developmental Cell · doi:10.1016/j.devcel.2021.10.009 · Cited by 30
A (dis)integrated stress response: Genetic diseases of eIF2α regulators
English, A. M., Green, K. M., & Moon, S. L. (2021) · Wiley Interdisciplinary Reviews - RNA · doi:10.1002/wrna.1689 · Cited by 33
“In addition to phosphorylation of 4E-BPs, another key way that translation initiation is regulated is by the phosphorylation of the α subunit of eIF2 at serine 51 during the ISR (Hershey et al., 2019; Sonenberg & Hinnebusch, 2009).”
BackgroundInfluentialLiu, T., Yang, D., Wei, Q., Wang, Y., Tian, L., Liu, X., Yang, Y., Luo, Q.-Y., Xu, J., Liu, Y., et al. (2025) · Molecules and Cells · doi:10.1016/j.molcel.2025.05.015 · Cited by 27
Decoding biology with massively parallel reporter assays and machine learningPreprint
Fleur, A. L., Shi, Y., & Seelig, G. (2024) · Genes & Development · doi:10.1101/gad.351800.124 · Cited by 29
“The PIC then scans the 5 ′ UTR until it encounters a start codon, commonly AUG, where ribosome assembly is finished (Sonenberg and Hinnebusch 2009).”
MethodBharti, N., Santos, L. A., Davyt, M., Behrmann, S., Eichholtz, M., Jiménez‐Sánchez, A., Hong, J. S., Rab, A., Sorscher, E. J., Albers, S., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-47258-9 · Cited by 27
“ZNF598 depletion leads to defective resolution of stalled ribosomes (PMID: 28132843), resulting in an elevation of general collisions (those collisions are also detected in our system, Fig.”
Regulation of stress granule formation in human oligodendrocytes
Pernin, F., Cui, Q., Mohammadnia, A., Fernandes, M. G. F., Hall, J. A., Srour, M., Dudley, R., Zandee, S., Klément, W., Prat, A., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-45746-6 · Cited by 31
“The phosphorylation of 4E-BP1 leads to its dissociation from the translation initiation factor eIF4E, allowing the formation of the initiation complex at the 5 ′ -cap of mRNAs resulting in protein translation 54,55 .”
Schaeffer, J., Vilallongue, N., Decourt, C., Blot, B., Bakdouri, N. E., Plissonnier, E., Excoffier, B., Paccard, A., Diaz, J., Humbert, S., et al. (2023) · Neuron · doi:10.1016/j.neuron.2023.06.005 · Cited by 30
“…initiation (harringtonin treat-ment), the blockage of translation elongation (puromycin treat-ment), and RNA degradation (RNase I treatment) (Figures S3D and S3E). mRNA is necessary for the formation of active 80S ribosomes, 31 and the degradation of ribosomal RNA (rRNA) can dissociate ribosomes.”
Pitera, A. P., Szaruga, M., Peak‐Chew, S., Wingett, S., & Bertolotti, A. (2022) · The EMBO Journal · doi:10.15252/embj.2021109985 · Cited by 28
“The kinase GCN2 is activated by amino acid shortage, PKR by double-stranded RNA during viral infections, HRI by heme deficiency and PERK (or PEK) by accumulation of misfolded proteins in the endoplasmic reticulum (Sonenberg & Hinnebusch, 2009; Wek, 2018).”
Morozov, D., Mironov, V., Moryachkov, R., Shchugoreva, I., Artyushenko, P., Zamay, G., Kolovskaya, O., Zamay, T., Krat, A., Molodenskiy, D., et al. (2021) · Molecular Therapy: Nucleic Acids · doi:10.1016/j.omtn.2021.07.015 · Cited by 27
Sun, L.-P., Liu, S.-G., Wang, X., Zheng, X., Chen, Y. C., & Shen, H. (2020) · Journal of Translational Medicine · doi:10.1186/s12967-021-02877-4 · Cited by 27
“eIFs play important roles in controlling the translation of proteins regulating cell growth, apoptosis, and malignant transformation [35, 36].”
BackgroundProtein Stability Buffers the Cost of Translation Attenuation following eIF2α Phosphorylation
Schneider, K., Nelson, G. M., Watson, J. L., Morf, J., Dalglish, M. M., Luh, L. M., Weber, A., & Bertolotti, A. (2020) · Cell Reports · doi:10.1016/j.celrep.2020.108154 · Cited by 29
Golob-Schwarzl, N., Puchas, P., Gogg-Kamerer, M., Weichert, W., Göppert, B., & Haybaeck, J. (2020) · Anticancer Research · doi:10.21873/anticanres.14292 · Cited by 27
Haji, N., Riebe, I., Aguilar‐Valles, A., Artinian, J., Laplante, I., & Lacaille, J. (2020) · Molecular Autism · doi:10.1186/s13229-020-00340-7 · Cited by 31
“TSC1 and TSC2 are repressors of the mechanistic target of rapamycin complex 1 (mTORC1), a signaling pathway crucial in the control of neuronal protein synthesis [3, 4].”
BackgroundWang, M.-F., Yang, C.-Q., Liu, X.-B., Zheng, J., Xue, Y.-X., Ruan, X., Shen, S., Wang, D., Li, Z., Cai, H., et al. (2020) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.15217 · Cited by 27
ncRFP: A Novel end-to-end Method for Non-Coding RNAs Family Prediction Based on Deep Learning
Wang, L., Zheng, S.-P., Zhang, H., Qiu, Z.-Y., Zhong, X., Liuliu, H., & Liu, Y.-N. (2020) · IEEE/ACM Transactions on Computational Biology & Bioinformatics · doi:10.1109/tcbb.2020.2982873 · Cited by 27
“…RNAs (tRNAs) and ribosomal RNAs (rRNAs). tRNAs, which include the highly conserved secondary structure of the ‘cloverleaf model’, are mainly responsible for the transportation of amino acids in the course of translation [6], and rRNAs mainly take charge of the synthesis of peptide chains [7].”
BackgroundKim, Y. S., Kimball, S. R., Piskounova, E., Begley, T. J., & Hempel, N. (2024) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2317846121 · Cited by 24
“10 and 11 .”
No country for old methods: New tools for studying microproteins
Valdivia-Francia, F., & Sendoel, A. (2024) · iScience · doi:10.1016/j.isci.2024.108972 · Cited by 38
“106–108 It begins with the formation of the ternary complex (eIF2-GTP-Met-tRNAi), which assembles with the 40S ribosomal subunit to form the preinitiation complex (PIC) to scan the 5 0 untranslated region (5 0 UTR).”
BackgroundFAM69C functions as a kinase for eIF2α and promotes stress granule assembly
Wu, Z., Mei, F., Gan, Y., Liu, A., Hu, J., Jin, Y., & Yin, Y. (2023) · EMBO Reports · doi:10.15252/embr.202255641 · Cited by 28
“Translational control in eukaryotic cells is critical for cell survival during stress responses (Sonenberg & Hinnebusch, 2009).”
Liu, B., Zhang, J., Meng, X. Z., Xie, S. M., Liu, F., Chen, H., Yao, D., Li, M., Guo, M., Shen, H., et al. (2023) · Oncogene · doi:10.1038/s41388-023-02641-6 · Cited by 30
“mTORC1 is the major pathway mediating translational control by phosphorylating the eukaryotic initiation factor 4E-binding proteins (4E-BPs) and p70 S6 kinase 1 (S6K1) [7].”
BackgroundTasak, M., & Phizicky, E. (2022) · PLoS Genetics · doi:10.1371/journal.pgen.1010215 · Cited by 26
Advances in the study of RNA-binding proteins in diabetic complications
Chen, X., Wu, J., Li, Z., Han, J., Xia, P., Shen, Y., Ma, J., Liu, X., Zhang, J., & Yu, P. (2022) · Molecular Metabolism · doi:10.1016/j.molmet.2022.101515 · Cited by 27
Pajot, A., Lavaud, J., Carrier, G., Garnier, M., Saint‐Jean, B., Rabilloud, N., Baroukh, C., Bérard, J., Olivier Bernard, A., Marchal, L., et al. (2022) · Frontiers in Plant Science · doi:10.3389/fpls.2022.830069 · Cited by 33
“These results are to be carefully considered, because transcripts could be regulated before translation into proteins (Sonenberg and Hinnebusch, 2009).”
BackgroundPlant Long Noncoding RNAs: New Players in the Field of Post-Transcriptional Regulations
Fonouni‐Farde, C., Ariel, F., & Crespi, M. D. (2021) · Non-Coding RNA · doi:10.3390/ncrna7010012 · Cited by 51
“The regulation of translation, so-called translational control, is a mechanism that allows a rapid modulation of gene expression through the activation or repression of pre-synthesized mRNA translation without requiring de novo transcription [62,63].”
BackgroundCoding potential of circRNAs: new discoveries and challenges
Miao, Q., Ni, B., & Tang, J. (2021) · PeerJ · doi:10.7287/peerj.10718v0.1/reviews/1 · Cited by 26
“…mechanism 115 during cell stress, ensuring basic protein needs are met(Lang et al. 2002; Riley et al. 2010); as such, this 116 mechanism is often triggered in conditions of viral invasion, tumor or other human diseases(Faye & Holcik 117 2015; Holcik & Sonenberg 2005; Sonenberg & Hinnebusch 2009).”
BackgroundHofmann, C., Serafin, A., Schwerdt, O. M., Fischer, J., Sicklinger, F., Younesi, F., Byrne, N. J., Meyer, I. S., Malovrh, E., Sandmann, C., et al. (2024) · Circulation · doi:10.1161/circulationaha.123.067479 · Cited by 25
“11 For the majority of transcripts, mRNAs selected for translation initiation are activated by the binding of the eIF (eukaryotic initiation factor) 4F, a heterotrimeric protein complex, consisting of eIF4E, eIF4G, and eIF4A that bind the 5’ cap of mRNAs to promote translation.”
BackgroundThe impact of tRNA modifications on translation in cancer: identifying novel therapeutic avenues
Añazco-Guenkova, A. M., Miguel‐López, B., Monteagudo-García, Ó., García-Vílchez, R., & Blanco, S. (2024) · NAR Cancer · doi:10.1093/narcan/zcae012 · Cited by 29
“This non-canonical protein translation is characterized by ribosomal direct recruitment of specific mRNAs that present discrete sequence elements in the 5 (cid:2) -UTR, and whose translation has been described to be induced under stressful situations ( 1 ,2 ).”
BackgroundKobayashi, H., Yoshimoto, C., Matsubara, S., Shigetomi, H., & Imanaka, S. (2023) · Cancer Drug Resistance · doi:10.20517/cdr.2023.49 · Cited by 25
eIF3 mRNA selectivity profiling reveals eIF3k as a cancer‐relevant regulator of ribosome content
Duan, H., Zhang, S., Zarai, Y., Öllinger, R., Wu, Y., Sun, L., Hu, C., He, Y., Tian, G., Rad, R., et al. (2023) · The EMBO Journal · doi:10.15252/embj.2022112362 · Cited by 29
“eIF3 and the 40S ribosome loaded with methionyl-tRNA and additional eIFs (Sonenberg and Hinnebusch, 2009).”
MethodEukaryotic ribosome quality control system: a potential therapeutic target for human diseases
Zhao, P., Yao, R.-Q., Zhang, Z., Zhu, S., Li, Y., Ren, C., Du, X., & Yao, Y.-M. (2022) · International Journal of Biological Sciences · doi:10.7150/ijbs.70955 · Cited by 27
Natural products as drugs and tools for influencing core processes of eukaryotic mRNA translation
Burgers, L. D., & Fürst, R. (2021) · Pharmacological Research · doi:10.1016/j.phrs.2021.105535 · Cited by 29
Atilano, M. L., Grönke, S., Niccoli, T., Kempthorne, L., Hahn, O., Morón-Oset, J., Hendrich, O., Dyson, M. C., Adams, M. L., Hull, A. J., et al. (2021) · eLife · doi:10.7554/elife.58565 · Cited by 27
Goss, K. L., Koppenhafer, S. L., Waters, T. W., Terry, W. W., Wen, K., Wu, M., Ostergaard, J., Gordon, P. M., & Gordon, D. J. (2020) · Oncogene · doi:10.1038/s41388-020-01552-0 · Cited by 28
“The 4E-BP1 protein, which is regulated by the mTOR pathway and highly expressed in Ewing sarcoma tumors, represses protein translation by binding to the m 7 G cap-binding protein eIF4E and preventing the assembly of the eIF4F translation initiation complex (20,34,35).”
Targeting translation regulators improves cancer therapy
Jiang, S., Mo, J.-L., Ji, P., Lei, L., Yin, J., Zhou, H., Liu, Z., & Hong, W. (2020) · Genomics · doi:10.1016/j.ygeno.2020.11.011 · Cited by 28
An integrative view on the cell-type-specific mechanisms of ketamine's antidepressant actions
Lewis, V., Rurak, G. M., Salmaso, N., & Aguilar‐Valles, A. (2024) · Trends in Neurosciences · doi:10.1016/j.tins.2023.12.004 · Cited by 31
Metadata
- Authors
- Sonenberg, N., & Hinnebusch, A. G.
- Affiliations
- McGill University (CA)
- National Institutes of Health (US)
- Corresponding author
- Sonenberg, Nahum
- Hinnebusch, Alan G.
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2009-02
- Volume
- 136
- Issue
- 4
- Pages
- 731-745
- ISSN
- 0092-8674 (ISSN-L)
- PMC
- PMC3610329
- OpenAlex
- W2037313242
- Cited by
- 3,304
- References
- 137
- Citations by year
- 2026: 145 · 2025: 144 · 2024: 166 · 2023: 194 · 2022: 187 · 2021: 219 · 2020: 208 · 2019: 204 · 2018: 211 · 2017: 240 · 2016: 199 · 2015: 188 · 2014: 212 · 2013: 212 · 2012: 222
- FWCI
- 14.67
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Cell (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- eScholarship@McGill (McGill) (submittedVersion, cc-by-nc-nd)
- Funders
- Howard Hughes Medical Institute
- National Institutes of Health (1ziahd001004-27, ZIA HD001004)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
- 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 Research and Splicing
- Keywords
- translation initiation, translational regulation, nutrient deprivation, stress response, nervous system function, aging, disease, mammalian cells
- MeSH terms
- Animals, Gene Expression Regulation, Humans, Models, Molecular, Peptide Chain Initiation, Translational, Peptide Initiation Factors, Ribosomes
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