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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
Baek, D., Villén, J., Shin, C., Camargo, F. D., Gygi, S. P., & Bartel, D. P. (2008) · Nature · doi:10.1038/nature07242 · Cited by 3,592
Widespread changes in protein synthesis induced by microRNAs
Selbach, M., Schwanhäusser, B., Thierfelder, N., Fang, Z., Khanin, R., & Rajewsky, N. (2008) · Nature · doi:10.1038/nature07228 · Cited by 3,429 · cited 1×
“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
Vasudevan, S., Tong, Y., & STEITZ, J. A. (2007) · Science · doi:10.1126/science.1149460 · Cited by 2,911 · cited 1×
“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
Vattem, K. M., & Wek, R. C. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0400541101 · Cited by 1,696
Specificity of microRNA target selection in translational repressionPreprint
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Absence of S6K1 protects against age- and diet-induced obesity while enhancing insulin sensitivity
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A microRNA in a Multiple-Turnover RNAi Enzyme Complex
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Argonaute2, a Link Between Genetic and Biochemical Analyses of RNAi
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Single-Stranded Antisense siRNAs Guide Target RNA Cleavage in RNAi
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Broad-Spectrum Antivirals Derived from Natural Products
Tian, W.-J., & Wang, X. (2023) · Viruses · doi:10.3390/v15051100 · Cited by 24
“The initiation beginning with eIF4F, consisting of eIF4A, eIF4E, and eIF4G, binds to the m7GTP residue at the 5′- untranslated region (5′UTR) of mRNA for capdependent translation [60,61].”
BackgroundADP enhances the allosteric activation of eukaryotic elongation factor 2 kinase by calmodulin
Piserchio, A., Long, K., Browning, L. S., Bohanon, A. L., Isiorho, E., Dalby, K., & Ghose, R. (2023) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.2300902120 · Cited by 16
“While the regulation of initiation, the first of three broad stages of protein synthesis (2), has been studied extensively (3, 4), there is a growing appreciation that the second stage, elongation, which involves the sequential incorporation of amino acids into a lengthening polypeptide chain, is…”
BackgroundGuo, Y., Zhou, D., Li, W., & Cao, J. (2022) · Expert Systems with Applications · doi:10.1016/j.eswa.2022.118004 · Cited by 15
EPI-Mind: Identifying Enhancer–Promoter Interactions Based on Transformer Mechanism
Ni, Y., Fan, L.-P., Wang, M., Zhang, N., Zuo, Y.-C., & Liao, M. (2022) · Interdisciplinary Sciences Computational Life Sciences · doi:10.1007/s12539-022-00525-z · Cited by 16
Not1 and Not4 inversely determine mRNA solubility that sets the dynamics of co-translational events
Allen, G., Weiss, B., Panasenko, O., Huch, S., Villányi, Z., Albert, B., Dilg, D., Zagatti, M., Schaughency, P. M., Liao, S. E., et al. (2022) · bioRxiv · doi:10.1186/s13059-023-02871-7 · Cited by 16
“Repression of translation initiation, the major rate-limiting step of translation, for instance, plays a key role in cellular responses to nutrient levels and stresses (5-7).”
BackgroundLane, S., Yeomans, A., & Shakir, S. (2022) · BMJ Open · doi:10.1136/bmjopen-2021-060425 · Cited by 16
“Thus the sequence of the ssRNA in the mRNA vaccine will determine the likelihood of complementarity (to itself, other mRNAs or microRNAs) to generate dsRNA which could then trigger immune responses via Toll-like Receptors (TLRs) (22) as well as alter mRNA translation mechanisms (21).”
BackgroundShao, L., Fingerhut, J. M., Falk, B. L., Han, H., Maldonado, G., Qiao, Y.-M., Lee, V., Hall, E., Chen, L., Polevoy, G., et al. (2021) · bioRxiv · doi:10.1101/2021.12.19.473358 · Cited by 16
“Protein synthesis can be divided into three steps (initiation, elongation, termination), yet much of the regulation occurs at the first step (Hershey et al., 2018; Pelletier and Sonenberg, 2019; Sonenberg and Hinnebusch, 2009).”
BackgroundDysregulation of Translation Factors EIF2S1, EIF5A and EIF6 in Intestinal-Type Adenocarcinoma (ITAC)
Schatz, C., Sprung, S., Schartinger, V., Codina-Martínez, H., Lechner, M., Hermsen, M., & Haybaeck, J. (2021) · Cancers · doi:10.3390/cancers13225649 · Cited by 16
“Hence, we focused on these translational factors and in view of a special expertise in our laboratory, we focused on EIF5A, EIF6 and EIF2S1, proteins mainly playing a role in the initiation phase of the translational process [13].”
Quantification of mRNA cap-modifications by means of LC-QqQ-MS
Muthmann, N., Špaček, P., Reichert, D., van Dülmen, M., & Rentmeister, A. (2021) · Methods · doi:10.1016/j.ymeth.2021.05.018 · Cited by 19
Ding, Z., Lamb, T. M., Boukhris, A., Porter, R. L., & Bell-Pedersen, D. (2021) · mBio · doi:10.1128/mbio.00871-21 · Cited by 16
“contains initiation factor eIF2, composed of a, b and g subunits, Met-tRNAi and GTP (32, 33).”
BackgroundInfluentialIron in Translation: From the Beginning to the End
Romero, A. M., Martínez‐Pastor, M. T., & Puig, S. (2021) · Microorganisms · doi:10.3390/microorganisms9051058 · Cited by 20
“In eukaryotes, the rate-limiting step in translation is the initiation step [37].”
BackgroundHe, Z., Wang, M.-H., Zhao, Q., Li, X., Liu, P., Ren, B., Wu, C., Du, X., Li, N., & Liu, Q. (2020) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2020.111073 · Cited by 18
The mRNA-Based Innovative Strategy: Progress and Challenges
Zhou, H., Wei, D., Chen, Z., Chen, H., Dong, C., Cai, W., Wang, J., Liu, X., Li, Y., Yang, Y., et al. (2026) · Nano-Micro Letters · doi:10.1007/s40820-025-01906-x · Cited by 17
“The translation of mRNA cannot proceed unless the eukaryotic translation initiation factors recognize 5’cap [38].”
Ribosome Biogenesis and Function in Cancer: From Mechanisms to Therapy
Gitareja, K., Chelliah, S. S., Sanij, E., Sandhu, S. K., Kang, J., & Khot, A. S. (2025) · Cancers · doi:10.3390/cancers17152534 · Cited by 20
“Phosphorylation of S6K1 stimulates translation initiation through RPS6 phosphorylation, eIF4B activation, and programmed cell death 4 (PDCD4) inhibition, thereby stimulating the mRNA helicase activity of eIF4A during translation initiation [148,149].”
Exploring the Potential and Advancements of Circular RNA Therapeutics
Wang, L., Wang, L., Dong, C., Liu, J., Cui, G., Gao, S., & Liu, Z. (2025) · Exploration · doi:10.1002/exp.20240044 · Cited by 15
“Additionally, compared with cap-dependent translation, IRES-based circRNA translation is less affected by cancer cell state and types, ensuring relatively consistent therapeutic protein expression and efficacy across different cancers [113].”
Protein Synthesis and Metabolism in T Cells
Sinclair, L. V., & Cantrell, D. A. (2025) · Annual Review of Immunology · doi:10.1146/annurev-immunol-082323-035253 · Cited by 19
A highly optimized human in vitro translation system
Bothe, A., & Ban, N. (2024) · Cell Reports Methods · doi:10.1016/j.crmeth.2024.100755 · Cited by 15
“32,33 By in - vitro -trans- lating reporter mRNAs with or without a cap and poly(A) tail, we could confirm the synergistic roles of the 5 0 cap and 3 0 poly(A) tail to promote efficient translation (Figure 3A), confirming that our system enables efficient canonical cap-dependent initiation.”
Devarkar, S., Vetick, M. B., Balaji, S., Lomakin, I., Yang, L.-J., Jin, D., Gilbert, W. V., Chen, S.-D., & Xiong, Y. (2023) · Cell Reports · doi:10.1016/j.celrep.2023.113156 · Cited by 15
“These results suggest that the interaction between the CTD of MERS-CoV Nsp1 and the 40S ribosomal subunit is critical for its translation inhibition activity.”
Cooperative activation of PDK1 and AKT by MAPK4 enhances cancer growth and resistance to therapy
Han, D., Wang, W., Jeon, J. H., Shen, T., Huang, X., Yi, P., Dong, B., & Yang, F. (2023) · PLoS Biology · doi:10.1371/journal.pbio.3002227 · Cited by 13
Kim, S., Choi, J., Marsal-García, L., Amiri, M., Yanagiya, A., & Sonenberg, N. (2023) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2300008120 · Cited by 14
Self-citationTranslational Regulation by eIFs and RNA Modifications in Cancer
Zhang, L., Zhang, Y., Zhang, S., Qiu, L., Zhang, Y., Zhou, Y., Han, J., & Xie, J. (2022) · Genes · doi:10.3390/genes13112050 · Cited by 18
Inhibition of the AKT/mTOR pathway negatively regulates PTEN expression via miRNAs
Wan, L., Wang, Y., Li, J., Wang, Y., & Zhang, H. (2022) · Acta Biochimica et Biophysica Sinica · doi:10.3724/abbs.2022159 · Cited by 15
“processes, most regulation is exerted at the initiation stage [17].”
BackgroundProteomic elucidation of the targets and primary functions of the picornavirus 2A protease
Serganov, A. A., Udi, Y., Stein, M. E., Patel, V., Fridy, P. C., Rice, C. M., Saeed, M., Jacobs, E. Y., Chait, B. T., & Rout, M. P. (2022) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2022.101882 · Cited by 31
Mubarak, G., & Zahir, F. (2022) · Journal of Personalized Medicine · doi:10.3390/jpm12020199 · Cited by 22
“For a full review of all rRNA classes see [21,22].”
BackgroundSelection of Cashmere Fineness Functional Genes by Translatomics
Zhang, Y., Zhang, D., Xu, Y., Qin, Y., Gu, M., Cai, W., Bai, Z., Zhang, X., Chen, R., Sun, Y., et al. (2022) · Frontiers in Genetics · doi:10.3389/fgene.2021.775499 · Cited by 15
“Therefore, protein abundance seems to be mainly regulated by ribosomes, highlighting the importance of translation control (Gebauer and Hentze, 2004; Sonenberg and Hinnebusch, 2009).”
BackgroundmTOR-dependent translation amplifies microglia priming in aging mice.
Keane, L., Antignano, I., Riechers, S.-P., Zollinger, R., Dumas, A., Offermann, N., Bernis, M. E., Russ, J., Graelmann, F., Mccormick, P., et al. (2021) · Journal of Clinical Investigation · doi:10.1172/jci155208 · Cited by 15
“Originally, a long 5′-UTR, rich in secondary structures, was thought to confer mTORC1 specificity (79, 80); however, more recently, it has emerged that translation of mRNAs without a long 5′-UTR can still be sensitive to eIF4E (42, 82).”
Deficiency of eIF4B Increases Mouse Mortality and Impairs Antiviral Immunity
Chen, B., Chen, Y., Rai, K. R., Wang, X., Liu, S., Li, Y., Xiao, M., Ma, Y., Wang, G., Guo, G., et al. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.723885 · Cited by 16
“Translation of messenger RNA (mRNA) is initiated by the assembly of eukaryotic translation initiation factor (eIF) 4F (eIF4F) complex (5, 6), which contains three key initiation factors: eIF4E (recognizing and binding the mRNA 5’ cap structures) (7, 8), eIF4A (functioning as the ATP-dependent RNA helicase) (9, 10), an…”
BackgroundTian, H., Lin, L., Ba, Z., Xue, F., Li, Y.-Z., & Zeng, W. (2021) · Chinese Chemical Letters · doi:10.1016/j.cclet.2021.05.070 · Cited by 15
Wei, C. Y., Zhang, J., Yuan, X., He, Z., Liu, G., & Wu, J. (2020) · Knowledge-Based Systems · doi:10.1016/j.knosys.2020.106459 · Cited by 20
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“Additionally, translation elongation factors could regulate the initial stages of protein synthesis [58].”
BackgroundThomas-Jardin, S. E., Suresh, S., Arce, A., Novaresi, N., Deng, Q., Stein, E., Thomas, L., Lewis, C. M., Ahn, C. W., Evers, B. M., et al. (2025) · Cancer Research · doi:10.1158/0008-5472.can-24-3844 · Cited by 13
“Mechanistically, ISR activation has been shown to induce the translation of specific mRNAs that harbor inhibitory uORFs, including canonical ISR response transcripts such as ATF4 , GADD34 , and GCN4 (16, 39, 40).”
Ji, F., Zhang, J., Mao, L., Tan, Y., Ye, M., He, X., Zhao, Y., Liu, J., Zhang, Y., Zhang, N., et al. (2025) · Nature Communications · doi:10.1038/s41467-024-55745-2 · Cited by 13
“These antibodies included anti-PGRMC1 (Cat#12990-1-AP, Proteintech, 1:1,000), anti-Flag-M2 (Cat#F3165, Sigma, 1:1,000), anti-c-Myc (Cat#ab32072, Abcam, 1:1,000), anti-HA (Cat#AE008, Abclonal, 1:1,000), anti-PERK (Cat#3192S, CST, 1:1,000), anti-p-PERK (T980, Cat#MA5-15033, Thermo, 1:1,000), anti-eIF2 α (S51; Cat#ab3215…”
Herrmannová, A., Jelínek, J., Pospíšilová, K., Kerényi, F., Vomastek, T., Watt, K., Brábek, J., Mohammad, M. P., Wagner, S., Topisirovic, I., et al. (2024) · bioRxiv · doi:10.1101/2023.06.29.547003 · Cited by 14
Transcriptional programming of translation by BCL6 controls skeletal muscle proteostasis
Ramachandran, K., Futtner, C. R., Sommars, M. A., Quattrocelli, M., Omura, Y., Fruzyna, E., Wang, J. C., Waldeck, N. J., Senagolage, M. D., Telles, C. G., et al. (2024) · Nature Metabolism · doi:10.1038/s42255-024-00983-3 · Cited by 20
“8) 54 .”
Li, N., Duan, Y., Ye, Q., Ma, Y., Ma, R., Zhao, L., Zhu, S., Yu, F., Qi, S., & Wang, Y. (2023) · New Phytologist · doi:10.1111/nph.19129 · Cited by 17
Advances in Polysaccharide Production Based on the Co-Culture of Microbes
Peng, W., Guo, X., Xu, X., Zou, D., Zou, H., & Yang, X. (2023) · Polymers · doi:10.3390/polym15132847 · Cited by 14
“Proteins are important components of the bacterial structure and are involved in the catalysis of many biochemical reactions and bacterial metabolism [75]; based on this, antimicrobial activity was previously assessed using Cordyceps polysaccharides [76].”
A highly efficient human cell-free translation system
Aleksashin, N., Chang, S. T.-L., & Cate, J. (2023) · bioRxiv · doi:10.1101/2023.02.09.527910 · Cited by 14
“During stress, eIF2α may also be phosphorylated by PKR-like endoplasmic reticulum kinase (PERK), general control non-derepressible-2 (GCN2) kinase, and heme-regulated HRI kinase (14) (Fig.”
An, Z., Chen, F.-Y., Hao, H., Xiong, M., Peng, H., Sun, H., & Wang, K.-J. (2023) · Fish and Shellfish Immunology · doi:10.1016/j.fsi.2023.108649 · Cited by 14
Castillo, K., Wu, C., Ding, Z., Lopez-Garcia, O. K., Rowlinson, E., Sachs, M. S., & Bell‐Pedersen, D. (2022) · Cell Reports · doi:10.1016/j.celrep.2022.111879 · Cited by 19
Circadian Governance of Cardiac Growth
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“The latter phosphorylation event inhibits the formation of the eIF2-GTP-methionyl-tRNA complex that is required for translation initiation of the majority of mRNA-encoded proteins [61].”
BackgroundAlves, A. N., Sgrò, C., Piper, M. W. D., & Mirth, C. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.822685 · Cited by 14
“GCN2 is a ubiquitous protein kinase activated in the presence of uncharged tRNAs, which occurs when there is an insufficiency of amino acids (Sonenberg and Hinnebusch, 2009; Armstrong et al., 2014).”
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Willems, P., Ndah, E., Jonckheere, V., Breusegem, F. V., & Damme, P. V. (2022) · Frontiers in Plant Science · doi:10.3389/fpls.2021.778804 · Cited by 14
“Of these phases, translation initiation forms a major rate-limiting step that is strongly regulated in eukaryotes (Sonenberg and Hinnebusch, 2009; Shah et al., 2013).”
BackgroundG-Quadruplex Regulation of VEGFA mRNA Translation by RBM4
Niu, K., Zhang, X., Song, Q., & Feng, Q. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23020743 · Cited by 19
“The mRNA translation is mediated in either a cap-dependent or cap-independent manner [2,3].”
BackgroundAnticancer Effects of I-BET151, an Inhibitor of Bromodomain and Extra-Terminal Domain Proteins
Lai, J., Liu, Z., Zhao, Y., Ma, C., & Huang, H. (2021) · Frontiers in Oncology · doi:10.3389/fonc.2021.716830 · Cited by 15
A role for translational regulation by S6 kinase and a downstream target in inflammatory pain
de la Peña, J. B., Kunder, N., Lou, T., Chase, R., Stanowick, A. D., Barragán‐Iglesias, P., Pancrazio, J. J., & Campbell, Z. T. (2021) · British Journal of Pharmacology · doi:10.1111/bph.15646 · Cited by 16
“…activity of eukaryotic initiation factor 4A (eIF4A) and plays a key role in initiation by recruiting of the small ribosomal subunit to mRNA (Sonenberg & Hinnebusch, 2009). eEF2K controls translation elongation as it phosphorylates and inactivates eukaryotic elongation factor 2 (eEF2)…”
BackgroundHooshmandi, M., Truong, V. T., Fields, E., Thomas, R. E., Wong, C., Sharma, V. K., Gantois, I., Roque, P. S., Chalkiadaki, K., Wu, N., et al. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.109036 · Cited by 14
Self-citationCollins, K. S., Eadon, M. T., Cheng, Y.-H., Barwinska, D., Ferreira, R. M., McCarthy, T. W., Janosevic, D., Syed, F., Maier, B., El-Achkar, T. M., et al. (2021) · bioRxiv · doi:10.3390/cells11071166 · Cited by 14
“There is growing evidence that altered translation, the fundamental step in gene expression that creates functional proteins, is important in both responding and contributing to cell stress [9,10].”
BackgroundGindina, S., Botsford, B. W., Cowansage, K. K., LeDoux, J. E., Klann, E., Hoeffer, C. A., & Ostroff, L. E. (2021) · The Journal of Comparative Neurology · doi:10.1002/cne.25158 · Cited by 16
“The two major targets of regulation are eIF4E, whose availability to bind to eIF4G is controlled by repressor proteins, and the activity of eIF2, which is controlled by phosphorylation of its α subunit (Borden & Volpon, 2020; Groppo & Richter, 2009; Sonenberg & Hinnebusch, 2009).”
BackgroundMethyladenosine Modification in RNAs: Classification and Roles in Gastrointestinal Cancers
Li, Q., He, W., & Wan, G. (2021) · Frontiers in Oncology · doi:10.3389/fonc.2020.586789 · Cited by 18
Qin, S., Ye, L., Zheng, Y., & Gao, J. (2020) · FEBS Letters · doi:10.1002/1873-3468.14030 · Cited by 14
Zhang, M., Zhao, J., Li, W., Wen, S., Huang, H., Dong, J., Liu, B., Zhang, G., Wang, H., Shen, Y., et al. (2020) · Environmental and Experimental Botany · doi:10.1016/j.envexpbot.2020.104350 · Cited by 16
Translation initiation and its relevance in colorectal cancer
Minnee, E., & Faller, W. J. (2020) · FEBS Journal · doi:10.1111/febs.15690 · Cited by 20
PKZ, a Fish-Unique eIF2α Kinase Involved in Innate Immune Response
Wu, C., Zhang, Y.-B., & Hu, C.-Y. (2020) · Frontiers in Immunology · doi:10.3389/fimmu.2020.00585 · Cited by 14
Strayer, E. C., Gopinath, S. K., Lee, H., Vejnar, C. E., Neuenkirchen, N., Gupta, A., Beaudoin, J.-D., & Giráldez, A. J. (2024) · Nature Communications · doi:10.1038/s41467-024-55274-y · Cited by 17
Understanding neurotropic enteric viruses: routes of infection and mechanisms of attenuation
Lulla, V., & Sridhar, A. (2024) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-024-05450-6 · Cited by 13
“Translation initiation is tightly regulated in a cell-and tissue-specific manner for both cap-and IRES-dependent mRNAs [88].”
BackgroundWallace, C., Oliveros, G., Xie, L., Serrano, P. A., Rockwell, P., & Figueiredo-Pereira, M. (2024) · Scientific Reports · doi:10.1038/s41598-024-54156-z · Cited by 13
Impact of eIF2α phosphorylation on the translational landscape of mouse embryonic stem cells
Amiri, M., Kiniry, S. J., Possemato, A. P., Mahmood, N., Basiri, T., Dufour, C. R., Tabatabaei, N., Deng, Q., Bellucci, M. A., Harwalkar, K., et al. (2023) · Cell Reports · doi:10.1016/j.celrep.2023.113615 · Cited by 21
Self-citationWu, C., Wang, S., Cao, T., Huang, T., Xu, L., Wang, J., Li, Q., Wang, Y., Qian, L., Xu, L., et al. (2023) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.17751 · Cited by 15
Ribosome changes reprogram translation for chemosurvival in G0 leukemic cells
Datta, C., Truesdell, S. S., Wu, K. Q., Bukhari, S. I. A., Ngue, H., Buchanan, B., Tonquèze, O. L., Lee, S., Kollu, S., Granovetter, M. A., et al. (2022) · Science Advances · doi:10.1126/sciadv.abo1304 · Cited by 15
“With eIF2 phosphorylation, stringent use of conventional Kozak start sites for initiator tRNA recruitment (3) is reduced—and can permit translation of specific mRNAs such as those with complex 5′UTRs, unconventional non-AUG start sites, or AUGs in poor Kozak start sites that would normally be poorly translated (47).”
BackgroundStem cell-derived exosomal transcriptomes for wound healing
Chen, G., Chen, H., Xiang, Z., & Zhu, W. Z. (2022) · Frontiers in Surgery · doi:10.3389/fsurg.2022.933781 · Cited by 13
Tandem repeats ubiquitously flank and contribute to translation initiation sites
Maddi, A. M. A., Kavousi, K., Arabfard, M., Ohadi, H., & Ohadi, M. (2022) · BMC Genomic Data · doi:10.1186/s12863-022-01075-5 · Cited by 18
“Introduction Translational regulation can be global or gene-specific, and most instances of translational regulation affect the rate-limiting initiation step [1, 2].”
BackgroundNoncanonical metabolite RNA caps: Classification, quantification, (de)capping, and function
Mattay, J. (2022) · Wiley Interdisciplinary Reviews - RNA · doi:10.1002/wrna.1730 · Cited by 16
“2022;13:e1730. wires.wiley.com/rna 1 of 23 https://doi.org/10.1002/wrna.1730 for nuclear export (Lewis & Izaurralde, 1997), and mediates translation (Sonenberg et al., 1978; Sonenberg & Hinnebusch, 2009).”
InfluentialAnomalous HIV-1 RNA, How Cap-Methylation Segregates Viral Transcripts by Form and Function
Boris‐Lawrie, K., Singh, G., Osmer, P. S., Zucko, D., Staller, S., & Heng, X. (2022) · Viruses · doi:10.3390/v14050935 · Cited by 15
The role of altered translation in intellectual disability and epilepsy
Malone, T. J., & Kaczmarek, L. K. (2022) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2022.102267 · Cited by 12
Microtubule and Actin Cytoskeletal Dynamics in Male Meiotic Cells of Drosophila melanogaster
Frappaolo, A., Piergentili, R., & Giansanti, M. G. (2022) · Cells · doi:10.3390/cells11040695 · Cited by 25
“This complex, which consists of the capbinding protein eIF4E, the RNA helicase eIF4A and the scaffolding protein eIF4G, binds the poly(A)-binding protein to promote circularization of mRNAs and ribosome 40S subunit recruitment [27].”
BackgroundNoh, B., Blasco-Conesa, M. P., Lai, Y., Ganesh, B. P., Urayama, A., Moreno‐González, I., Marrelli, S. P., McCullough, L. D., & Moruno-Manchon, J. F. (2022) · Frontiers in Aging · doi:10.3389/fragi.2021.797562 · Cited by 12
Zhu, T., Jiang, X., Xin, H., Zheng, X., Xue, X., Chen, J.-L., & Qi, B.-M. (2021) · Veterinary Research · doi:10.1186/s13567-021-01018-5 · Cited by 13
“When bound to GTP, the eIF2 complex recruits Met-tRNAi and the 40S ribosomal subunit to initiate mRNA translation [3, 4].”
BackgroundFan, X., Bao, T., Yi, H., Zhang, Z., Zhang, K., Liu, X., Lin, X., Zhang, Z., & Feng, Z. (2021) · Frontiers in Microbiology · doi:10.3389/fmicb.2021.781454 · Cited by 14
Modulation of AggR levels reveals features of virulence regulation in enteroaggregative E. coli
Prieto, A., Bernabeu, M., Sánchez-Herrero, J., Pérez-Bosque, A., Miró, L., Bäuerl, C., Collado, C., Hüttener, M., & Juárez, A. (2021) · Communications Biology · doi:10.1038/s42003-021-02820-9 · Cited by 13
Esteves, A. D., Koyuncu, O. Ö., & Enquist, L. W. (2022) · Journal of Virology · doi:10.1128/jvi.01752-21 · Cited by 14
Annexin A2 binds the internal ribosomal entry site of c-myc mRNA and regulates its translation
Strand, E., Hollås, H., Sakya, S. A., Romanyuk, S. A., Saraste, M. E. V., Grindheim, A. K., Patil, S. S., & Vedeler, A. (2021) · RNA Biology · doi:10.1080/15476286.2021.1947648 · Cited by 14
“It is difficult to achieve a detailed understanding regarding the molecular mechanisms of cellular IRESs, since no in vitro system totally recapitulates the function of these elements [91].”
BackgroundThe Interplay of Tumor Stroma and Translational Factors in Endometrial Cancer
Sobočan, M., Smolle, M., Schatz, C., & Haybaeck, J. (2020) · Cancers · doi:10.3390/cancers12082074 · Cited by 13
“, the formation of the multifactorial 43S preinitiation complex, and the assembly of the eIF4F complex on the mRNA cap [12].”
BackgroundJungers, C. F., Elliff, J. M., Masson‐Meyers, D. S., Phiel, C. J., & Origanti, S. S. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.ra120.013324 · Cited by 21
Hwang, H. S., Lee, M. H., & Kim, H. (2020) · The FASEB Journal · doi:10.1096/fj.201903003r · Cited by 20
The autism susceptibility kinase, TAOK2, phosphorylates eEF2 and modulates translation
Henis, M., Rücker, T., Scharrenberg, R., Richter, M., Baltussen, L., Hong, S., Meka, D. P., Schwanke, B., Neelagandan, N., Daaboul, D., et al. (2024) · Science Advances · doi:10.1126/sciadv.adf7001 · Cited by 13
“…ternary complex formation (eIF2- GTP-tRNAiMet) required for start codon recognition and delivering the first methionine amino acid to the ribosome ( 6 ). eIF2 α phosphorylation leads to general down-regulation of most translation, but paradoxically up-regulates proteins encoded by mRNAs with…”
Gong, X., Feng, S.-H., Wang, J.-H., Gao, B., Xue, W.-X., Chu, H.-Y., Fang, S., Yuan, Y.-M., Cheng, Y.-Q., Liao, M., et al. (2025) · PLoS Pathogens · doi:10.1371/journal.ppat.1012987 · Cited by 12
“Following the delivery of mRNA-TC to ribosomes, PABPC1 dissociates and can associate with the importin α/β complex, facilitating the nuclear import of PABPC1 [81,89–91].”
Therapeutic potential of Parkin and its regulation in Parkinson’s disease
Safreena, N., Nair, I. C., & Chandra, G. (2024) · Biochemical Pharmacology · doi:10.1016/j.bcp.2024.116600 · Cited by 11
Fang, L., Gu, W., Li, R., Chen, C., Cai, S., Luozhong, S., Chen, M., Hsu, A., Tsai, Y.-C., Londhe, K., et al. (2024) · ACS Nano · doi:10.1021/acsnano.4c07530 · Cited by 11
eIF4F complex dynamics are important for the activation of the integrated stress response
Kim, K. Q., Urs, A. N. N., Lasehinde, V., Greenlaw, A. C., Hudson, B. H., & Zaher, H. S. (2024) · Molecular Cell · doi:10.1016/j.molcel.2024.04.016 · Cited by 13
“3,4,69 On the other hand, while canonical initiation is responsible for translating the majority of mRNAs, evidence increasingly supports the notion that cap-independent mechanisms play critical roles in health and disease.”
BackgroundHost-like RNA Elements Regulate Virus Translation
Khan, D., & Fox, P. L. (2024) · Viruses · doi:10.3390/v16030468 · Cited by 14
“Translation initiation is generally the rate-limiting step in protein synthesis and is exquisitely regulated by a variety of mechanisms [1,2,4].”
BackgroundCrystal structure of a cap-independent translation enhancer RNA
Lewicka, A., Roman, C., Jones, S., Disare, M. T., Rice, P. A., & Piccirilli, J. A. (2023) · Nucleic Acids Research · doi:10.1093/nar/gkad649 · Cited by 12
Xue, M.-G., Cong, F., Zheng, W.-L., Xu, R.-Q., Liu, X., Bao, H., Sung, Y., Xi, Y.-M., He, F., Ma, J., et al. (2023) · Cell Death Discovery · doi:10.1038/s41420-023-01587-8 · Cited by 12
He, X., Sun, Y., Lu, J., Naz, F., Ma, S., & Liu, J. (2023) · Frontiers in Immunology · doi:10.3389/fimmu.2023.1117760 · Cited by 14
Feng, L., Lin, X., Fu, B., Xiong, Y., Zaky, M. Y., & Wu, H. (2023) · Life Sciences · doi:10.1016/j.lfs.2023.121374 · Cited by 12
“These changes may not induce a complete and effective immune response, and HLA-I monitoring is also [121,122]”
Diverse roles of heterogeneous nuclear ribonucleoproteins in viral life cycle
Bhattarai, K., & Holčı́k, M. (2022) · Frontiers in Virology · doi:10.3389/fviro.2022.1044652 · Cited by 14
Evolving understandings for the roles of non-coding RNAs in autoimmunity and autoimmune disease
Cheng, Z., Hou, G., & Shen, N. (2022) · Journal of Autoimmunity · doi:10.1016/j.jaut.2022.102948 · Cited by 15
Inhibition of eIF6 Activity Reduces Hepatocellular Carcinoma Growth: An In Vivo and In Vitro Study
Scagliola, A., Miluzio, A., Mori, G., Ricciardi, S., Oliveto, S., Manfrini, N., & Biffo, S. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23147720 · Cited by 14
“These eIFs are regulated by signaling pathways and stimulate the translation of specific mRNAs by interacting with 5′UTR sequences of mRNAs [6,7].”
BackgroundEiermann, N., Stoecklin, G., & Jovanovic, B. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23105600 · Cited by 14
“Third, 4EBP1 was found to be dephosphorylated, which occurred through the inhibition of mTOR signaling and converted 4EBP1 into an inhibitor of cap-dependent translation [38].”
BackgroundAlam, M. M., Shima, H., Matsuo, Y., Long, N. C., Matsumoto, M., Ishii, Y., Sato, N., Sugiyama, T., Nobuta, R., Hashimoto, S., et al. (2022) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2022.102084 · Cited by 16
“The released eukaryotic translation initiation factor 4E then aids the formation of the translation initiation complex at the 50 ends of mRNA, thereby enhancing global translation (9).”
BackgroundSen, N. D., Zhang, H., & Hinnebusch, A. (2021) · Microorganisms · doi:10.3390/microorganisms9122413 · Cited by 12
“Both 43S PIC attachment to mRNA and subsequent scanning are inhibited by secondary structures in the mRNA 5′UTR [3] that are thought to be resolved by DEAD/H-box RNA helicases.”
BackgroundSelf-citationIdentification of an RNA-Binding-Protein-Based Prognostic Model for Ewing Sarcoma
Chen, Y., Su, H., Su, Y., Zhang, Y., Lin, Y., & Haglund, F. (2021) · Cancers · doi:10.3390/cancers13153736 · Cited by 19
Combined Transcriptomic and Proteomic Analysis of Perk Toxicity Pathways
Popovic, R., Celardo, I., Yu, Y.-Z., Costa, A. C., Loh, S. H., & Martins, L. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22094598 · Cited by 12
“Consequently, the cap-dependent translation is inhibited at the initiation step due to the failure of the 80S ribosome complex to assemble (reviewed in [10]).”
BackgroundKameda, T., Asano, K., & Togashi, Y. (2021) · bioRxiv · doi:10.1371/journal.pcbi.1009068 · Cited by 12
“During eukaryotic initiation, the ribosome dissociates into the large (60S) and small (40S) subunits, and the latter binds the methionyl initiator tRNA (Met tRNA i ) and mRNA with the help of eukaryotic initiation factors (eIFs) [3, 4].”
BackgroundBasak, T., Dey, A., Banerjee, R., Paul, S., Maiti, T., & Ain, R. (2020) · Stem Cells · doi:10.1002/stem.3305 · Cited by 12
“Initiation factors define the rate-limiting step of the entire process and serves as a major site of translational control.(39) Of the four initiation”
BackgroundJiang, M., Hu, H., Zhao, K., Di, R., Huang, X., Shi, Y., Yue, Y., Nie, J., Yu, S. L., Wang, W., et al. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.ra120.014948 · Cited by 13
“For instance, most mRNAs are translated by a scanning mechanism wherein the m(7)G cap at the 5’-UTR is bound with the cap-binding complex eIF4F to activate mRNA (11, 12).”
BackgroundLi, Q.-Y., Xu, J.-X., Zhang, D.-D., Zhong, K.-L., Sun, T., Li, X.-P., & Li, J.-R. (2020) · doi:10.1111/jfs.12832 · Cited by 12
Biological functions and prognostic value of RNA Binding Proteins in clear cell Renal Cell Carcinoma
Zhu, Z., He, A., Lin, L., Xu, C., Cai, T., & Lin, J. (2020) · Journal of Cancer · doi:10.7150/jca.49175 · Cited by 13
Fan, X., Chang, T., Chen, C., Hafner, M., & Wang, Z. (2023) · doi:10.1101/2023.07.08.548206 · Cited by 12
“In eukaryotes, translation initiation is generally mediated by the 5 ¢ -cap, which recruits various translation initiation factors and small ribosomal subunit to form preinitiation complex (16).”
Background(2025) · doi:10.1093/nar/gkaf277 · Cited by 12
“In eukaryotes, translation initiation is generally mediated by the 5 (cid:2) -cap, which recruits various translation initiation factors and small ribosomal subunit to form preinitiation complex [ 16 ].”
Therapeutic Application of mRNA for Genetic Diseases
Schürmann, P. J. L., Vriesman, S. V. B., Castro-Alpízar, J., Kooijmans, S. A. A., Nieuwenhuis, E. E. S., Schiffelers, R. M., & Fuchs, S. A. (2025) · Wiley Interdisciplinary Reviews Nanomedicine and Nanobiotechnology · doi:10.1002/wnan.70019 · Cited by 9
“Highly stable secondary structures prevent ribosome recruitment and codon recognition (Asrani et al. 2018; Leppek et al. 2018; Sonenberg and Hinnebusch 2009).”
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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