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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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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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Birth and death view of DNA, RNA, and Proteins.
Kumari, P., & Bhavesh, N. S. (2023) · Gene · doi:10.1016/j.gene.2023.147672 · Cited by 5
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“Because STR_13795 was in the 3 ′ UTR of cls-2 , the 17-bp deletion associated with expression of cls-2 might affect the targeting by miRNAs (Sonenberg and Hinnebusch 2009; Jan et al. 2011).”
BackgroundVisualization of translation reorganization upon persistent collision stress in mammalian cells
Fedry, J., Silva, J., Vanević, M., Fronik, S., Mechulam, Y., Schmitt, E., Georges, A. D., Faller, W., & Förster, F. (2023) · bioRxiv · doi:10.1101/2023.03.23.533914 · Cited by 5
HLA-I and HLA-II Peptidomes of SARS-CoV-2: A Review
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“Third, models of bioinformatics prediction do not justify the manipulation ways of viruses to cellular processes, which affect antigen presentation [32,33].”
MethodIRES-mediated translation in bacteria
Takallou, S., Puchacz, N., Allard, D., Said, K. B., Nokhbeh, R., Samanfar, B., & Golshani, A. (2022) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2022.12.022 · Cited by 7
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N6-Adenosine Methylation of a Single Site in SARS-CoV-2 5′-UTR Promotes TranslationPreprint
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“Translating proteins from mRNAs requires three steps: initiation, elongation, and termination [3,4].”
MethodMartínez‐Alonso, E., Guerra‐Pérez, N., Escobar-Peso, A., Peracho, L., Lechuga, R. V., Cruz-Culebras, A., Masjuán, J., & Alcázar, A. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23031830 · Cited by 7
“The initiation step is a highly regulated mechanism with an important checkpoint in the 40S ribosomal subunit recruitment to the 5′ end of a specific mRNA [13,14].”
BackgroundBerger, C. A., Ward, C. P., Karchner, S. I., Nelson, R. K., Reddy, C. M., Hahn, M. E., & Tarrant, A. M. (2022) · Marine Environmental Research · doi:10.1016/j.marenvres.2022.105569 · Cited by 10
Clarke-Whittet, M., Rocco, A., & Gerber, A. P. (2022) · Microorganisms · doi:10.3390/microorganisms10020340 · Cited by 6
“Numerous proteins integrate cellular homeostatic and sensory signals, by gatekeeping of mRNA access for translation on a global or specific basis [2].”
BackgroundModeling the ribosomal small subunit dynamic in Saccharomyces cerevisiae based on TCP-seq data
Neumann, T., & Tuller, T. (2022) · Nucleic Acids Research · doi:10.1093/nar/gkac021 · Cited by 7
“The scan, which begins in the 5′cap and moves forward in the 3′ direction until the detection of the AUG start codon, is accompanied by different initiation factors (5,57), resulting in footprints that have dependency both on the location of the SSU in the 5′UTR and on footprint length (Figure 1A).”
BackgroundDong, Y., Tong, H., Hu, Q., & Dong, X.-Z. (2021) · Microbiology spectrum · doi:10.1128/spectrum.01167-21 · Cited by 5
Wei, S.-S., Guo, W., Qian, Y., Xiang, J., Liu, K., Gao, X.-J., Gao, X.-W., & Chen, Y.-C. (2021) · Aging · doi:10.18632/aging.203606 · Cited by 5
Unconventional translation initiation factor EIF2A is required for Drosophila spermatogenesis
Lowe, D., & Montell, D. J. (2021) · bioRxiv · doi:10.1002/dvdy.403 · Cited by 5
Tools for Assessing Translation in Cryptococcus neoformans
Knowles, C. M., McIntyre, K. M., & Panepinto, J. C. (2021) · Journal of Fungi · doi:10.3390/jof7030159 · Cited by 9
“The eukaryotic elongation factor 1A (eEF1A) directs aminoacyl t-tRNAs into the A site in a GTP-dependent manner and upon pairing of the correct tRNA, eIF1A triggers the hydrolysis of GTP allowing the aminoacyl-tRNA to enter the empty A site (Reviewed in [4,5]).”
BackgroundInferring translational heterogeneity from Saccharomyces cerevisiae ribosome profiling
Bordignon, P. D. C., & Pechmann, S. (2021) · FEBS Journal · doi:10.1111/febs.15748 · Cited by 6
Translational Regulation by Upstream Open Reading Frames and Its Relevance to Human Genetic Disease
Fernandes, R. O., & Romão, L. (2020) · Wiley eBooks · doi:10.1002/9780470015902.a0029194 · Cited by 5
Green, S. R., Al-attar, R., McKechnie, A. E., Naidoo, S., & Storey, K. B. (2020) · Cellular Signalling · doi:10.1016/j.cellsig.2020.109763 · Cited by 7
“eIF2a is needed for translation since it enables the GTP-dependent transfer of the first methionine-bearing tRNA to the ribosome and it can be inhibited by various protein kinases phosphorylating on S51 [56].”
BackgroundInfluentialMachado, F. C., Bittencourt-Cunha, P., Malvezzi, A., Árico, M., Radio, S., Smircich, P., Zoltner, M., Field, M. C., & Schenkman, S. (2020) · Cellular Microbiology · doi:10.1111/cmi.13243 · Cited by 5
“…transcription factor 4 (ATF4), C/EBP homologous protein (CHOP) and a regulatory subunit of protein phosphatase 1, which can dephosphorylate eIF2α (Sonenberg & Hinnebusch, 2009). eIF2α phosphorylation at T169 in T. cruzi epimastigotes is induced by nutritional stress and mutation to alanine…”
BackgroundMultiplexed photo-activation of mRNA with single-cell resolution
Zhang, D.-Y., Jin, S., Piao, X.-J., & Devaraj, N. (2020) · bioRxiv · doi:10.1101/2020.03.19.999631 · Cited by 5
“[30] Moreover, in-vitro transcribed mRNA (IVT-mRNA) is only transiently active in cytosol and is completely degraded via cellular metabolism, typically within 24 hours.”
BackgroundChaudhury, A., Kongchan, N., Massey, S., Sharma, R., Pal, R., Zhao, N., Tsoi, P. S., Zhu, Y., Olokpa, E., Mao, S., et al. (2026) · Nucleic Acids Research · doi:10.1093/nar/gkag123 · Cited by 6
“…(PIC) comprised of eIF1, eIF1a, eIF5, and the (small) 40S ribosomal subunit bound by the eIF2-GTP-Met-tRNAi ternary complex, to form the 48S PIC [ 16 ]. eIF4G1’s role is so central to cap-dependent translational initiation that cleavage of this protein in virally infected cells is sufficient to…”
GCN2 monitors mRNA translation termination
Worner, K., Maschhoff, K. R., Schuh, G. M., & Hu, W. (2025) · Molecular Cell · doi:10.1016/j.molcel.2025.11.015 · Cited by 6
Roles of RNA Structures in the Genome Translation of (+) Sense RNA Viruses
Lu, G., Beyene, B. G., Camacho, J. M., & Koirala, D. (2025) · Viruses · doi:10.3390/v17111404 · Cited by 4
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Ponti, R. D., Vandelli, A., Broglia, L., & Tartaglia, G. G. (2025) · Biology Direct · doi:10.1186/s13062-025-00706-y · Cited by 3
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“As the initial step of protein synthesis, there are a variety of translation initiation cytokines involved in the process of translation [9].”
Filipović, D., & Turck, C. W. (2025) · Molecular Neurobiology · doi:10.1007/s12035-025-05013-1 · Cited by 3
“…regulation is crucial for fine-tuning gene expression and is vital for processes such as synaptic plasticity, as well as memory and learning [94] Taken together, the decline in vesicle-and synapse-associated proteins following CSIS may impair synaptic vesicle recycling and retrieval,…”
Rodriguez-Martinez, A., & Young-Baird, S. K. (2025) · Molecular Biology of the Cell · doi:10.1091/mbc.e24-08-0341 · Cited by 11
“As the final step in the central dogma, translation control plays critical roles in cell homeostasis, proliferation, and growth (Gebauer and Hentze, 2004; Sonenberg and Hinnebusch, 2009; Hershey et al. , 2012).”
Fernández-García, L., & García-Blanco, M. A. (2025) · Antiviral Research · doi:10.1016/j.antiviral.2025.106142 · Cited by 4
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The Proteins Diversity of the eIF4E Family in the eIF4F Complex
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“The initiation complex stops at the start codon, which is followed by dissociation of the translation initiation factors, as well as addition of the 60S ribosomal subunit resulting in formation of the 80S ribosome [31, 27].”
β2-integrins control HIF1α activation in human neutrophils
Kling, L., Eulenberg-Gustavus, C., Jerke, U., Rousselle, A., Eckardt, K., Schreiber, A., & Kettritz, R. (2024) · Frontiers in Immunology · doi:10.3389/fimmu.2024.1406967 · Cited by 4
Genomic factors associated with substance use disorder relapse: A critical review
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“Initiation is a rate limiting step and there are several mechanisms involved in controlling this phase (Buffington et al., 2014; Sonenberg & Hinnebusch, 2009).”
Li, J., Chen, Y., Yang, Y., Yang, Y., & Wu, Z. (2024) · Animal nutrition · doi:10.1016/j.aninu.2024.06.008 · Cited by 8
RNA-binding proteins in bone pathophysiology
Maroni, P., Pesce, N. A., & Lombardi, G. (2024) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2024.1412268 · Cited by 4
Yulyaningsih, E., Suh, J. H., Fanok, M. H., Chau, R., Solanoy, H., Takahashi, R. H., Bakardjiev, A., Becerra, I., Benitez, N. B., Chiu, C.-L., et al. (2024) · bioRxiv · doi:10.1101/2023.08.21.554203 · Cited by 4
“Upon recognition of the start codon, GTP is hydrolyzed, and the resulting eIF2-GDP dissociates from the complex (Gebauer and Hentze 2004, Sonenberg and Hinnebusch 2009).”
BackgroundGuo, H., Lv, J., Su, X.-W., Chen, L., Ren, J.-S., Liu, L., Ren, M., Liu, S., Dai, M., Ren, G., et al. (2024) · Frontiers in Plant Science · doi:10.3389/fpls.2024.1366986 · Cited by 4
“Protein synthesis is a complex process that can be categorized into four distinct stages: initiation, elongation, termination, and ribosome recycling (Sonenberg and Hinnebusch, 2009).”
BackgroundChen, Z.-Q., Wang, F., Chen, B., Wu, G.-W., Tian, D.-G., Yuan, Q., Qiu, S., Zhai, Y.-S., Chen, J.-P., Zheng, H.-Y., et al. (2024) · Molecular plant pathology · doi:10.1111/mpp.13434 · Cited by 4
“On the other hand, many host defences limit viral translation by selectively or globally impairing the translation machinery (Machado et al., 2017 ; Sonenberg & Hinnebusch, 2009).”
BackgroundThe p30 protein of the African swine fever virus behaves as an RNase.
Nandy, S., Bora, N. R., Gaurav, S., & Kumar, S. (2023) · Virology · doi:10.1016/j.virol.2023.109967 · Cited by 4
JUN mRNA Translation Regulation is Mediated by Multiple 5’ UTR and Start Codon Features
González-Sánchez, A. M., Castellanos-Silva, E. A., Díaz-Figueroa, G., & Cate, J. H. D. (2023) · bioRxiv · doi:10.1101/2023.11.17.567602 · Cited by 4
“Protein translation is one of the most energetically expensive cellular processes and is highly regulated, especially during translation initiation (Buttgereit and Brand 1995; Sonenberg and Hinnebusch 2009; Topisirovic and Sonenberg 2011; Hershey et al. 2012; Leibovitch and Topisirovic 2018).”
BackgroundGeng, G., Yu, C., Xiangdong, L., Shi, K., & Yuan, X. (2023) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2023.128062 · Cited by 4
Translatomics to explore dynamic differences in immunocytes in the tumor microenvironment
Guo, Y., Yan, S., & Zhang, W. (2023) · Molecular Therapy — Nucleic Acids · doi:10.1016/j.omtn.2023.102037 · Cited by 4
“It is well known that mammalian target of rapamycin (mTOR)- related pathways are the main regulatory factors of cell metabolism, 88,89 translation initiation and elongation, 90,91 and the biological function and metabolism of T cells.”
Saha, B., Bhardwaj, U., & Goss, D. (2023) · Biochemistry · doi:10.1021/acs.biochem.3c00125 · Cited by 4
Expression of Eukaryotic Translation Initiation Factors in the Urothelial Carcinoma of the Bladder
Luzha, J., Nass, N., Czapiewski, P., Schroeder, N., Kalinski, T., Schostak, M., Schatz, C., Jandrig, B., & Haybaeck, J. (2023) · Anticancer Research · doi:10.21873/anticanres.16292 · Cited by 4
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“Meanwhile, up-regulated translation pathways, including cytoplasmic translation and ribonucleoprotein complex biogenesis [39], maybe a potential therapeutic target in AML, confirming previous studies that translational control can play a critical role in modulating gene expression [40,41].”
Dev, G., Chawla, A. S., Gupta, S., Bal, V., George, A., Rath, S., & Arimbasseri, G. A. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232416017 · Cited by 5
“Several external and internal stimuli and pathways upregulate protein synthesis in eukaryotic cells [2,3].”
BackgroundTian, Y., Liu, Q., Zhou, Y.-F., Chen, X.-Y., Pan, Y.-C., Xu, H.-W., & Yang, Z.-Y. (2022) · Frontiers in Bioengineering and Biotechnology · doi:10.3389/fbioe.2022.901452 · Cited by 4
“Defects in any of these five subunits impair protein synthesis by reducing eIF2B activity (Pavitt et al., 1997; Kimball et al., 1998; Sonenberg and Hinnebusch, 2009; Elsby et al., 2011).”
BackgroundDysregulated Gene Expression in Lymphoblasts from Parkinson’s Disease
Annesley, S., Allan, C., Sanislav, O., Evans, A., & Fisher, P. (2022) · Proteomes · doi:10.3390/proteomes10020020 · Cited by 4
“activated themselves by mTOR—are known to inactivate eukaryotic initiation factors, thereby reducing translation rates [26].”
BackgroundKhan, M. A., Kumar, P., Akif, M., & Miyoshi, H. (2021) · PLoS ONE · doi:10.1371/journal.pone.0259688 · Cited by 4
Moriwaki, C., Tanigaki, R., Miyake, Y., Vo, N., Nguyen, M. T., Nguyen, N., Do, T. N. V., Nguyen, H. X., & Kataoka, T. (2021) · The biochemist · doi:10.3390/biochem1030014 · Cited by 4
“eIF2 plays an essential role in the transport and entry of Met-tRNAiMet to the ribosome small subunit during the initiation of translation [45,46].”
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Expression of Phosphodiesterase (PDE) Isoenzymes in the Human Male and Female Urethra
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Light-control of cap methylation and mRNA translation via genetic code expansion of Ecm1
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Visualizing lncRNA and mRNA structure models within the Integrative Genomics Viewer
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4Ei-10 interdiction of oncogenic cap-mediated translation as therapy for non-small cell lung cancer
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“eIF4E binds to the cap while eIF4G stabilizes the capmRNA interaction while RNA helicase eIF4A unwinds the secondary structure of the mRNA permitting access for the 43S pre-initiation complex to scan for the AUG start codon [1].”
BackgroundRodríguez-Pereira, C., Lagunas, A., Casanellas, I., Vida, Y., Pérez-Inestrosa, E., Andrades, J., Becerra, J., Samitier, J., Blanco, F., & Magalhães, J. (2020) · Materials · doi:10.3390/ma13102247 · Cited by 4
“As mRNA is prone to degradation, it is possible that mRNA has a rapid turnover while its protein has a higher half-life and remains accumulated [27].”
BackgroundToyoshima, Y., Yoshizawa, F., Tokita, R., Taguchi, Y., Takahashi, S.-I., Kato, H., & Minami, S. (2020) · American Journal of Physiology. Endocrinology and Metabolism · doi:10.1152/ajpendo.00464.2019 · Cited by 4
mTORC1 and nuclear ERK spatially control translation in cardiomyocytes through 4EBP1 phosphorylation
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Bridging technical innovation and computational advances in studies of RNA–protein assemblies
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“Ribosome engagement during translation further decompacts messenger RNPs, and nuclear cap-binding complex and PABPN1 are exchanged for cytoplasmic EIF4E and PABPC1, respectively 58 .”
McKenney, K. M., Hernandez-Perez, C., Dunshee, E. B., Pum, J. M., DesMarais, A. J., Connacher, R. P., & Goldstrohm, A. C. (2026) · Nucleic Acids Research · doi:10.1093/nar/gkag075 · Cited by 3
“The poly(A) tail is bound by cytoplasmic poly(A)-binding proteins (PABPCs) that enhance translation and mRNA stability [ 1 –4 ] by interacting with translation initiation factor eIF4G, which in turn binds to 5 (cid”
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“[53, 54].”
Gao, F., Yang, X., Yang, Z., Yu, D., Zhang, B., Wang, Y., Yao, Z., Chen, J., Liao, Q., Li, L., et al. (2025) · Research · doi:10.34133/research.1032 · Cited by 2
“As a competitive binding factor of eIF4E, 4E-BP can bind eIF4E with strong affinity in the non-phosphorylated state, thereby inhibiting the overall protein synthesis [ 56 ].”
Termination of the integrated stress response
de Miguel, C., Thorkelsson, S. R., Fatalska, A., Hodgson, G., Dalglish, M., Wang, C., & Bertolotti, A. (2025) · Science · doi:10.1126/science.adw5137 · Cited by 3
Fordjour, G. N. R., Ghosh, A., Ferry, J. G., Armache, J., Bevilacqua, P. C., & Murakami, K. S. (2025) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2025.110686 · Cited by 2
“It is proposed that such thermophilic adaptations of ribosomes using extra r-proteins and these extra proteins may have been used during eukaryotic ribosome evolution for translation regulation or ribosome localization (56, 57).”
Zhao, C.-S., Liu, S., Li, Z., Chen, J.-Y., & Xiong, X. (2025) · Cells · doi:10.3390/cells14131032 · Cited by 3
“The phosphorylated eIF2 α inhibits eIF2B activity and consequently reduces global translation [74,75].”
Regulation of Protein Synthesis at the Translational Level: Novel Findings in Cardiovascular Biology
Tsoy, S., & Liu, J. (2025) · Biomolecules · doi:10.3390/biom15050692 · Cited by 3
“This interaction between eIF4G and PABPC1 (Figure 2A) is necessary for the formation of a stable, looped mRNP complex, which stimulates cap-dependent translation while protecting the mRNA from exonucleases [31].”
Graphene Oxide-Modified Resin for Selective dsRNA Removal from In Vitro-Transcribed mRNA
Ryu, J., Namgung, J., Jang, J., Lee, G., Yoo, K., Jun, B., & Kim, D. (2025) · ACS Applied Bio Materials · doi:10.1021/acsabm.5c00320 · Cited by 3
Optimizing Human Cell-Free System for Efficient Protein Production
Mansour, A., Kipper, K., & Pulk, A. (2025) · Journal of Microbiology and Biotechnology · doi:10.4014/jmb.2410.10026 · Cited by 3
“We employed GADD34 and K3L to enhance CFPS activity [22, 23, 34, 48, 49].”
Preh, E. O., Ramirez, M. A., Mohan, S., Guy, C. R., & Bell‐Pedersen, D. (2025) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2411916122 · Cited by 2
Translational regulation of SND1 governs endothelial homeostasis during stress
Han, Z., Yan, G., Jousma, J., Nukala, S. B., Amiri, M., Kiniry, S. J., Tabatabaei, N., Kwon, Y., Zhang, S., Rehman, J., et al. (2025) · Journal of Clinical Investigation · doi:10.1172/jci168730 · Cited by 3
“Activation of mTORC1 phosphorylates the translation repressor eukaryotic translation initiation factor 4E–binding proteins (4E-BPs), releasing them from eukaryotic translation initiation factor 4E (eIF4E) to allow cap-dependent translation to proceed (45, 46).”
Ribosomal rodeo: wrangling translational machinery in gynecologic tumors
Filipek, K., & Penzo, M. (2024) · Cancer and Metastasis Reviews · doi:10.1007/s10555-024-10234-2 · Cited by 3
“The translational machinery encompasses a complex sys-tem of cellular components responsible for protein synthesis, including ribosomes, messenger RNA (mRNA), transfer RNA, (tRNA), translational factors, and regulatory proteins [1].”
Exploring the dynamics of messenger ribonucleoprotein-mediated translation repression
Meyer, J., Payr, M., Duss, O., & Hennig, J. (2024) · Biochemical Society Transactions · doi:10.1042/bst20231240 · Cited by 4
Zhu, J., Wu, R., Yang, T., Yuan, Y., Liu, G., Chen, S., Chen, Z., Liu, S., Wang, S., Li, D., et al. (2024) · Hepatology · doi:10.1097/hep.0000000000001101 · Cited by 4
“[38] Upon invasion of the virus into a host cell, the cell initiates mechanisms such as protein kinase R-eIF2 α pathways to hinder the early stage of protein translation, thereby restricting the synthesis of viral proteins and the generation of viral particles.”
Diet induced insulin resistance is due to induction of PTEN expressionPreprint
Rosen, N., Mukherjee, R., Pancholi, P., Sharma, M., Solomon, H., Timaul, M. N., Thant, C., Mcgriskin, R., Hayatt, O., Markov, V., et al. (2024) · Research Square · doi:10.21203/rs.3.rs-4021885/v1 · Cited by 3
The human eIF4E:4E-BP2 complex structure for studying hyperphosphorylation.
Zeng, J., Lu, C., Huang, X., & Li, Y. (2024) · Physical Chemistry, Chemical Physics - PCCP · doi:10.1039/d3cp05736d · Cited by 3
Fernández-García, L., Ahumada-Marchant, C., Lobos-Ávila, P., Brauer, B., Bustos, F. J., & Arriagada, G. (2024) · Viruses · doi:10.3390/v16030403 · Cited by 4
“The canonical or cap-dependent translation mechanism relies on the recognition of the 5 ′ cap structure, and the recruitment of the translation machinery is dependent on this event [15].”
BackgroundJoshi, K., Luisi, B., Wunderlin, G., Saleh, S., Lilly, A. C., Okusolubo, T., & Farabaugh, P. J. (2024) · Nucleic Acids Research · doi:10.1093/nar/gkae053 · Cited by 3
“Phosphorylation of translation factors can directly reduce or increase their intrinsic activity or indirectly regulate their association with inhibitory factors ( 24 ,25 ).”
BackgroundDuan, M.-T., Dev, I., Lu, A., You, M.-Y., & Shapiro, M. (2023) · bioRxiv · doi:10.1101/2023.05.26.541240 · Cited by 3
D’Agostino, S., Tettey‐Matey, A., Volpe, M., Pierattini, B., Ansaloni, F., Lau, P., Bon, C., Peruzzo, O., Braccia, C., Armirotti, A., et al. (2023) · Research Square · doi:10.1101/2023.05.25.542260 · Cited by 3
“This hypothesis would be, indeed, consistent with what was observed in both cap-dependent or –independent translation initiation, where the ability of the poly(A) binding proteins to interact with cap or IRES-binding proteins can mediate circularization of the mRNA by linking the 5’ and 3’UTRs in a closed loop [53,54].”
ResultProteomic profiling of eIF3a conditional knockout mice
Zhuo, W., Chen, J., Jiang, S.-L., Zheng, J., Huang, H.-X., Xie, P., Li, W., Lei, M., Yin, J., Gao, Y., et al. (2023) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2023.1160063 · Cited by 3
“translation is rate-limiting during protein synthesis (Sonenberg and Hinnebusch, 2009).”
Quantification of elongation stalls and impact on gene expression in yeast
Hou, W.-F., Harjono, V., Harvey, A. T., Subramaniam, A. R., & Zid, B. M. (2023) · bioRxiv · doi:10.1101/2023.03.19.533377 · Cited by 3
Regulation of the interactions between human eIF5 and eIF1A by the CK2 kinase
Gamble, N. K., Paul, E., Anand, B., & Marintchev, A. (2022) · Current Research in Structural Biology · doi:10.1016/j.crstbi.2022.09.003 · Cited by 3
“eIF5 has an N-terminal domain (NTD), which performs the GAP function, and a Cterminal domain (CTD), which is responsible for most of the proteinprotein interactions, including with the N-terminal tail of the β subunit of eIF2 (eIF2β-NTT) (reviewed in (Hinnebusch, 2014; Jackson et al., 2010; Marintchev and Wagner, 2004…”
BackgroundKaur, H., & Moreau, R. (2022) · Life Science · doi:10.1016/j.lfs.2022.120989 · Cited by 3
Shi, J., Cao, Y., Lang, Q.-H., Dong, Y., Huang, L., Yang, L., Li, J.-J., Zhang, X., & Wang, D. (2022) · Plant Reproduction · doi:10.1007/s00497-022-00442-7 · Cited by 4
“Regulation of translation is exerted mainly at translation initiation (Sonenberg and Hinnebusch 2009).”
BackgroundLoss of 4E-BP Converts Cerebellar Long-Term Depression to Long-Term Potentiation
Saviuk, N., Chong, Y., Wang, P., Bermudez, S., Zhao, Z., Bhaskaran, A. A., Bowie, D., Sonenberg, N., Cooper, E., & Haghighi, A. P. (2021) · Cell Reports · doi:10.1016/j.celrep.2022.110911 · Cited by 4
Self-citationKoromilas, A. E. (2022) · BioEssays · doi:10.1002/bies.202200026 · Cited by 5
Fan, X., Zhang, K., Zhang, Z., Zhang, Z., Lin, X., Liu, X., Feng, Z., & Yi, H. (2022) · Foods · doi:10.3390/foods11101411 · Cited by 4
“These results indicate that translational regulation can be a more rapid and direct means of acid stress response compared to transcriptional regulation, because no new mRNA needs to be produced [27].”
BackgroundSatoh, K. (2022) · Analytical Biochemistry · doi:10.1016/j.ab.2021.114542 · Cited by 3
Evolutionarily divergent mTOR remodels the translatome to drive rapid wound closure and regenerationPreprint
Zhulyn, O., Rosenblatt, H. D., Shokat, L., Dai, S.-Z. A., Kuzuoglu-Ozturk, D., Zhang, Z.-J., Ruggero, D., Shokat, K., & Barna, M. (2021) · bioRxiv · doi:10.1101/2021.10.28.465024 · Cited by 3
“−2 −4 −6 −8 log10 (padj) no change response to virus (35) regulation of protein modification process (120) activation of immune response (41) response to lipopolysaccharide (32) response to bacterium (44) defense response to other organism (47)”
BackgroundShi, B., Song, Q., Luo, X., Song, J., Xia, D., Xia, Z., Liu, M., Wang, W., Wang, R., Du, H., et al. (2021) · Archives of Virology · doi:10.1007/s00705-021-05209-5 · Cited by 4
Translation Initiation Factor eIF2Bε Promotes Stemness of Intestinal Epithelial Cells
Smit, W. L., de Boer, R. J., Meijer, B. J., Spaan, C. N., van Roest, M., Koelink, P. J., Köster, J., Dekker, E., Abbink, T. E. M., van der Knaap, M. S., et al. (2020) · Stem Cell Research · doi:10.1016/j.scr.2021.102499 · Cited by 4
Translational regulation in pathogenic and beneficial plant-microbe interactions.
Traubenik, S., Ferrari, M., Blanco, F., & Zanetti, M. (2021) · Biochemical Journal · doi:10.1042/bcj20210066 · Cited by 3
Babaei, G., Massah, A., & Habibi, M. K. (2021) · Virology Journal · doi:10.1186/s12985-021-01601-4 · Cited by 3
“IRES-based alternative translation strategy can be adopted by cellular mRNA independent from cap-dependent translation [12, 33, 38, 39].”
BackgroundToribio, R., Muñoz, A., Sánchez, F., Ponz, F., & Castellano, M. M. (2021) · The Plant Journal · doi:10.1111/tpj.15290 · Cited by 4
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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