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.
“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
The Introduction (page not available in our copy) explains that mRNA sequences and structures affect translation initiation, while cellular conditions such as starvation or stress can alter translation. It does not establish the corresponding claim that DNA sequence and cellular environment affect transcription. (LLM, conf=0.88)
Experimental — accuracy not yet measuredTranslation of uORFs can regulate expression of the downstream protein-coding gene in response to either global or gene-specific regulatory signals.
“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
NIBAN1 phosphorylates EIF4EBP1 to allow assembly of the initiation complex.
“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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Cites
(2008) · doi:10.1038/nrg2290 · Cited by 5,199 · cited 1× · see citing works
“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 · see citing works
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× · see citing works
“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 2,806 · cited 1× · see citing works
“Surprisingly, it was reported recently that miRNAs can also stimulate rather than inhibit translation when cells enter quiescence (Vasudevan et al., 2007).”
A microRNA in a Multiple-Turnover RNAi Enzyme Complex
Hutvágner, G., & Zamore, P. D. (2002) · Science · doi:10.1126/science.1073827 · Cited by 2,081 · see citing works
Reinitiation involving upstream ORFs regulates <i>ATF4</i> 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 · see citing works
Absence of S6K1 protects against age- and diet-induced obesity while enhancing insulin sensitivity
Um, S. H., Frigerio, F., Watanabe, M., Picard, F., Joaquin, M., Sticker, M., Fumagalli, S., Allegrini, P. R., Kozma, S. C., Auwerx, J., et al. (2004) · Nature · doi:10.1038/nature02866 · Cited by 1,677 · see citing works
Specificity of microRNA target selection in translational repressionPreprint
Doench, J. G., & Sharp, P. A. (2004) · Genes & Development · doi:10.1101/gad.1184404 · Cited by 1,642 · see citing works
Single-stranded antisense siRNAs guide target RNA cleavage in RNAi.
Martı̂nez, J., Patkaniowska, A., Urlaub, H., Lührmann, R., & Tuschl, T. (2002) · Cell · doi:10.1016/s0092-8674(02)00908-x · Cited by 1,550 · cited 1× · see citing works
“Once processed from its primary transcript precursor, an miRNA is then loaded into a protein complex, referred to as an RNA-induced silencing complex (RISC), which targets and inhibits protein expression from specific mRNAs (Hammond et al., 2001; Hutvagner and Zamore, 2002; Martinez et al., 2002).”
Structure of the 70S Ribosome Complexed with mRNA and tRNA
Selmer, M., Dunham, C., Murphy, F., Weixlbaumer, A., Petry, S., Kelley, A. C., Weir, J., & Ramakrishnan, V. (2006) · Science · doi:10.1126/science.1131127 · Cited by 1,352 · cited 1× · see citing works
“The stunning progress on crystal structures of bacterial 70S ribosomes bound to mRNAs and tRNAs (Selmer et al., 2006; Yusupova et al., 2006) has provided atomic details of the path of mRNA and contacts made with tRNAs in the decoding sites.”
P bodies and the control of mRNA translation and degradation
Parker, R., & Sheth, U. (2007) · Molecular Cell · doi:10.1016/j.molcel.2007.02.011 · Cited by 1,335 · cited 2× · see citing works
“These mechanisms might be similar to those by which Dhh1/Pat1 repress general translation in yeast during carbon starvation (Parker and Sheth, 2007).”
RNA regulons: coordination of post-transcriptional events
Keene, J. D. (2007) · Nature Reviews Genetics · doi:10.1038/nrg2111 · Cited by 1,321 · see citing works
Holz, M. K., Ballif, B. A., Gygi, S. P., & Blenis, J. (2005) · Cell · doi:10.1016/j.cell.2005.10.024 · Cited by 1,262 · see citing works
Argonaute2, a Link Between Genetic and Biochemical Analyses of RNAi
Hammond, S. M., Boettcher, S., Caudy, A. A., Kobayashi, R., & Hannon, G. J. (2001) · Science · doi:10.1126/science.1064023 · Cited by 1,261 · see citing works
Stress granules: the Tao of RNA triage.
Anderson, P., & Kedersha, N. (2008) · TIBS -Trends in Biochemical Sciences. Regular ed · doi:10.1016/j.tibs.2007.12.003 · Cited by 1,156 · cited 3× · see citing works
“It is noteworthy that some studies demonstrated the association of P-bodies and stress granules and suggested the possibility of exchange of material between P-bodies and stress granules (Anderson and Kedersha, 2008).”
InfluentialTranslational control of long-lasting synaptic plasticity and memory
Costa-Mattioli, M., Sossin, W. S., Klann, E., & Sonenberg, N. (2009) · Neuron · doi:10.1016/j.neuron.2008.10.055 · Cited by 944 · see citing works
Self-citationLifespan extension by conditions that inhibit translation in Caenorhabditis elegans
Hansen, M., Taubert, S., Crawford, D., Libina, N., Lee, S.-J., & Kenyon, C. (2007) · Aging Cell · doi:10.1111/j.1474-9726.2006.00267.x · Cited by 918 · cited 1× · see citing works
“Studies in the nematode Caenorhabditis elegans demonstrated that inhibition of several components of the eIF4F complex including eIF4E and eIF4G or lowering their levels extends life span (Pan et al., 2007; Syntichaki et al., 2007; Curran and Ruvkun, 2007; Hansen et al., 2007; Henderson et al., 2006).”
Dendritic Protein Synthesis, Synaptic Plasticity, and Memory
Sutton, M. A., & Schuman, E. M. (2006) · Cell · doi:10.1016/j.cell.2006.09.014 · Cited by 894 · see citing works
Translational Control by MAPK Signaling in Long-Term Synaptic Plasticity and Memory
Kelleher, R. J., Govindarajan, A., Jung, H.-Y., Kang, H., & Tonegawa, S. (2004) · Cell · doi:10.1016/s0092-8674(04)00115-1 · Cited by 845 · see citing works
S6K1- and ßTRCP-Mediated Degradation of PDCD4 Promotes Protein Translation and Cell Growth
Dorrello, N. V., Peschiaroli, A., Guardavaccaro, D., Colburn, N. H., Sherman, N. E., & Pagano, M. (2006) · Science · doi:10.1126/science.1130276 · Cited by 731 · cited 1× · see citing works
“Phosphorylation of Pdcd4 leads to its ubiquitination and degradation by the proteasome (Dorrello et al., 2006).”
Spatial regulation of β-actin translation by Src-dependent phosphorylation of ZBP1
Hüttelmaier, S., Zenklusen, D., Lederer, M., Dictenberg, J., Lorenz, M., Meng, X.-H., Bassell, G., Condeelis, J., & Singer, R. (2005) · Nature · doi:10.1038/nature04115 · Cited by 681 · cited 1× · see citing works
“ZBP1 blocks 60S joining to the 43S PIC (Huttelmaier et al., 2005).”
Gerber, A. P., Herschlag, D., & Brown, P. O. (2004) · PLoS Biology · doi:10.1371/journal.pbio.0020079 · Cited by 651 · cited 1× · see citing works
“The precedents for coordinate regulation of classes of mRNAs at the translational level have already been documented in yeast via Puf RNA-binding proteins (Gerber et al., 2004) and in mammalian systems where the coordinately expressed mRNAs were called “RNA operons” (reviewed in Keene, 2007).”
MicroRNA Inhibition of Translation Initiation in Vitro by Targeting the Cap-Binding Complex eIF4F
Mathonnet, G., Fabian, M., Svitkin, Y., Parsyan, A., Huck, L., Murata, T., Biffo, S., Merrick, W., Darżynkiewicz, E., Pillai, R., et al. (2007) · Science · doi:10.1126/science.1146067 · Cited by 636 · cited 1× · see citing works
“In contrast to the disparate results obtained from studies in cells, in vitro experiments in cell-free translation extracts prepared from mammalian or Drosophila embryos all indicated that miRNAs suppress cap-dependent but not IRES-mediated translation (Mathonnet et al., 2007; Thermann and Hentze, 2007; Wakiyama et al…”
Self-citationThe Fragile X Syndrome Protein Represses Activity-Dependent Translation through CYFIP1, a New 4E-BP
Napoli, I., Mercaldo, V., Boyl, P. P., Eleuteri, B., Zalfa, F., De Rubeis, S., Di Marino, D., Mohr, E., Massimi, M., Falconi, M., et al. (2008) · Cell · doi:10.1016/j.cell.2008.07.031 · Cited by 609 · cited 1× · see citing works
“Although several conflicting models have been proposed to explain the mechanism of translational repression by FMRP (reviewed in Klann and Richter, 2007), it was recently reported that FMRP binds to eIF4E via CYFIP1 (cytoplasmic FMRP interacting protein 1), thus displacing eIF4G and consequently inhibiting translation…”
Self-citationBarco, A., Alarcon, J. M., & Kandel, E. (2002) · Cell · doi:10.1016/s0092-8674(02)00657-8 · Cited by 595 · cited 1× · see citing works
“ATF4 suppresses memory because it inhibits the transcription factor CREB (cyclic AMP response element binding protein)-mediated gene expression, which is critical for long-term synaptic plasticity and memory (Barco et al., 2002).”
Pestova, T., & Kolupaeva, V. (2002) · Genes & Development · doi:10.1101/gad.1020902 · Cited by 590 · see citing works
Moerke, N., Aktas, H., Chen, H., Cantel, S., Reibarkh, M., Fahmy, A., Gross, J., Degterev, A., Yuan, J., Chorev, M., et al. (2007) · Cell · doi:10.1016/j.cell.2006.11.046 · Cited by 568 · cited 1× · see citing works
“Another study generated compounds that inhibit the eIF4E-eIF4G interaction and retard the growth of tumor cells (Moerke et al., 2007).”
Cap-Dependent Translation Initiation in Eukaryotes Is Regulated by a Molecular Mimic of eIF4G
Marcotrigiano, J., Gingras, A., Sonenberg, N., & Burley, S. K. (1999) · Molecular Cell · doi:10.1016/s1097-2765(01)80003-4 · Cited by 512 · cited 1× · see citing works
“The 4E-BPs compete with eIF4G for a shared binding site on eIF4E (Marcotrigiano et al., 1999).”
Self-citationDissecting eIF4E action in tumorigenesis.Preprint
Wendel, H., Silva, R. L. A., Malina, A., Mills, J., Zhu, H., Ueda, T., Watanabe‐Fukunaga, R., Fukunaga, R., Teruya-Feldstein, J., Pelletier, J., et al. (2007) · Genes & Development · doi:10.1101/gad.1604407 · Cited by 512 · see citing works
Costa‐Mattioli, M., Gobert, D., Stern, E., Gamache, K., Colina, R., Cuello, A. C., Sossin, W. S., Kaufman, R. J., Pelletier, J., Rosenblum, K., et al. (2007) · Cell · doi:10.1016/j.cell.2007.01.050 · Cited by 510 · see citing works
Self-citationYang, H.-S., Jansen, A. P., Komar, A. A., Zheng, X., Merrick, W. C., Costes, S., Lockett, S. J., Sonenberg, N., & Colburn, N. H. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.1.26-37.2003 · Cited by 494 · cited 1× · see citing works
“S6Ks also phosphorylate Pdcd4, which is a tumor suppressor that binds and suppresses eIF4A activity (Yang et al., 2003).”
Self-citationInhibition of mRNA translation extends lifespan in Caenorhabditis elegans
Pan, K. Z., Palter, J. E., Rogers, A. N., Olsen, A., Chen, D., Lithgow, G. J., & Kapahi, P. (2006) · Aging Cell · doi:10.1111/j.1474-9726.2006.00266.x · Cited by 491 · cited 1× · see citing works
“Studies in the nematode Caenorhabditis elegans demonstrated that inhibition of several components of the eIF4F complex including eIF4E and eIF4G or lowering their levels extends life span (Pan et al., 2007; Syntichaki et al., 2007; Curran and Ruvkun, 2007; Hansen et al., 2007; Henderson et al., 2006).”
Kahvejian, A., Svitkin, Y. V., Sukarieh, R., M'Boutchou, M.-N., & Sonenberg, N. (2005) · Genes & Development · doi:10.1101/gad.1262905 · Cited by 491 · cited 2× · see citing works
“PABP also stimulates 60S subunit joining (Kahvejian et al., 2005), and findings from yeast suggest that the poly(A) tail is required to block the inhibitory effects of two RNA helicases on subunit joining factor eIF5B (Searfoss et al.”
Self-citationLifespan Regulation by Evolutionarily Conserved Genes Essential for Viability
Curran, S. P., & Ruvkun, G. (2007) · PLoS Genetics · doi:10.1371/journal.pgen.0030056 · Cited by 479 · cited 1× · see citing works
“Studies in the nematode Caenorhabditis elegans demonstrated that inhibition of several components of the eIF4F complex including eIF4E and eIF4G or lowering their levels extends life span (Pan et al., 2007; Syntichaki et al., 2007; Curran and Ruvkun, 2007; Hansen et al., 2007; Henderson et al., 2006).”
An mRNA m7G Cap Binding-like Motif within Human Ago2 Represses Translation
Kiriakidou, M., Tan, G. S., Lamprinaki, S., Planell-Saguer, M. D., Nelson, P. T., & Mourelatos, Z. (2007) · Cell · doi:10.1016/j.cell.2007.05.016 · Cited by 462 · see citing works
Suppression of Myc oncogenic activity by ribosomal protein haploinsufficiency
Barna, M., Pusic, A., Zollo, O., Costa, M. J., Kondrashov, N., Rego, E., Rao, P., & Ruggero, D. (2008) · Nature · doi:10.1038/nature07449 · Cited by 434 · cited 1× · see citing works
“In the same vein, Barna et al. (2008) showed that activation of the Myc oncogene causes an increase in cap-dependent translation at the expense of IRES-dependent translation, and thus a reduction in Cdk11 levels, resulting in tumorigenesis.”
Leung, A., Calabrese, J. M., & Sharp, P. (2006) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.0608845103 · Cited by 428 · see citing works
Translational control of hippocampal synaptic plasticity and memory by the eIF2α kinase GCN2
Costa-Mattioli, M., Gobert, D., Harding, H., Herdy, B., Azzi, M., Bruno, M., Bidinosti, M., Mamou, C. B., Marcinkiewicz, E., Yoshida, M., et al. (2005) · Nature · doi:10.1038/nature03897 · Cited by 421 · cited 1× · see citing works
“This could be explained by augmented synaptic plasticity, as evidenced by a lower threshold of stimulation to achieve lasting LTP (Costa-Mattioli et al., 2005).”
Self-citationEulálio, A., Huntzinger, E., & Izaurralde, E. (2008) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1405 · Cited by 414 · see citing works
Maskin Is a CPEB-Associated Factor that Transiently Interacts with eIF-4E
Stebbins-Boaz, B., Cao, Q., de Moor, C. D., Méndez, R., & Richter, J. (1999) · Molecular Cell · doi:10.1016/s1097-2765(00)80230-0 · Cited by 404 · cited 1× · see citing works
“The foregoing mechanism is similar to that suggested originally from studies in Xenopus oocytes for the inhibition of translation by CPEB through Maskin, which binds to eIF4E (Stebbins-Boaz et al., 1999) (Figure 4A).”
Nakamura, A., Sato, K., & Hanyu-Nakamura, K. (2004) · Developmental Cell · doi:10.1016/s1534-5807(03)00400-3 · Cited by 399 · cited 2× · see citing works
“, 2004) and to oskar mRNA by Bruno (Chekulaeva et al., 2006; Nakamura et al., 2004).”
Graff, J., Konicek, B., Vincent, T. M., Lynch, R. L., Monteith, D., Weir, S., Schwier, P., Capen, A., Goode, R., Dowless, M., et al. (2007) · Journal of Clinical Investigation · doi:10.1172/jci32044 · Cited by 393 · cited 1× · see citing works
“Likewise, antisense oligonucleotides to eIF4E inhibit tumor growth in mice while not causing any deleterious effects (Graff et al., 2007).”
Spahn, C. M. T., Gómez-Lorenzo, M. G., Grassucci, R. A., Jørgensen, R., Andersen, G. R., Beckmann, R., Penczek, P. A., Ballesta, J. P. G., & Frank, J. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600102 · Cited by 385 · cited 1× · see citing works
“This model reveals strong similarities to 70S ribosomes, including the inter-subunit space containing the mRNA binding cleft and decoding sites (Spahn et al., 2004).”
Ribosome loading onto the mRNA cap is driven by conformational coupling between eIF4G and eIF4E.
Gross, J., Moerke, N., von der Haar, T., Lugovskoy, A., Sachs, A., McCarthy, J., & Wagner, G. (2003) · Cell · doi:10.1016/s0092-8674(03)00975-9 · Cited by 368 · cited 1× · see citing works
“, 2007) and for eIF4E bound to a segment of eIF4G, which increases eIF4E’s affinity for the cap (Gross et al., 2003).”
Bacquer, O. L., Petroulakis, E., Paglialunga, S., Poulin, F., Richard, D., Cianflone, K., & Sonenberg, N. (2007) · Journal of Clinical Investigation · doi:10.1172/jci29528 · Cited by 365 · see citing works
Self-citationeIF4E function in somatic cells modulates ageing in Caenorhabditis elegans
Syntichaki, P., Troulinaki, K., & Tavernarakis, N. (2007) · Nature · doi:10.1038/nature05603 · Cited by 361 · cited 1× · see citing works
“Studies in the nematode Caenorhabditis elegans demonstrated that inhibition of several components of the eIF4F complex including eIF4E and eIF4G or lowering their levels extends life span (Pan et al., 2007; Syntichaki et al., 2007; Curran and Ruvkun, 2007; Hansen et al., 2007; Henderson et al., 2006).”
In Vivo Imaging of oskar mRNA Transport Reveals the Mechanism of Posterior Localization
Zimyanin, V., Belaya, K., Pécréaux, J., Gilchrist, M. J., Clark, A., Davis, I., & Johnston, D. S. (2008) · Cell · doi:10.1016/j.cell.2008.06.053 · Cited by 360 · cited 1× · see citing works
“Translational repression of oskar and nanos mRNA outside the posterior pole of the embryo is essential to buttress the targeting of the morphogens they encode, as the localization mechanisms for these mRNAs are inefficient (Bergsten and Gavis, 1999; Zimyanin et al., 2008).”
Drosophila miR2 induces pseudo-polysomes and inhibits translation initiation
Thermann, R., & Hentze, M. (2007) · Nature · doi:10.1038/nature05878 · Cited by 345 · see citing works
Passmore, L. A., Schmeing, T. M., Maag, D., Applefield, D. J., Acker, M. G., Algire, M. A., Lorsch, J. R., & Ramakrishnan, V. (2007) · Molecular Cell · doi:10.1016/j.molcel.2007.03.018 · Cited by 327 · cited 1× · see citing works
“It appears that eIF1 promotes scanning when nonAUG codons occupy the P-site by stabilizing an open conformation of the mRNA binding cleft of the 40S subunit, possibly by modulating the conformation of the “latch” to the mRNA entry channel (Passmore et al., 2007) (Figures 2A and 2B).”
A hypoxia-controlled cap-dependent to cap-independent translation switch in breast cancer.
Braunstein, S., Karpisheva, K., Pola, C., Goldberg, J., Hochman, T., Yee, H., Cangiarella, J., Arju, R., Formenti, S., & Schneider, R. (2007) · Molecules and Cells · doi:10.1016/j.molcel.2007.10.019 · Cited by 320 · cited 1× · see citing works
“A switch from cap-dependent to cap-independent mRNA translation is mediated by hypoxia in large advanced breast cancers and is required for promoting angiogenesis and tumor survival and progression (Braunstein et al., 2007).”
Banko, J., Poulin, F., Hou, L., Demaria, C., Sonenberg, N., & Klann, E. (2005) · Journal of Neuroscience · doi:10.1523/jneurosci.2423-05.2005 · Cited by 317 · cited 1× · see citing works
“These results were interpreted to mean that the excessive translation could be deleterious to the synaptic plasticity required for learning and memory (Banko et al., 2005).”
Self-citationOpposing polymerase-deadenylase activities regulate cytoplasmic polyadenylation.
Kim, J. H., & Richter, J. (2006) · Molecules and Cells · doi:10.1016/j.molcel.2006.08.016 · Cited by 305 · see citing works
Wakiyama, M., Takimoto, K., Ohara, O., & Yokoyama, S. (2007) · Genes & Development · doi:10.1101/gad.1566707 · Cited by 304 · cited 1× · see citing works
“In contrast to the disparate results obtained from studies in cells, in vitro experiments in cell-free translation extracts prepared from mammalian or Drosophila embryos all indicated that miRNAs suppress cap-dependent but not IRES-mediated translation (Mathonnet et al., 2007; Thermann and Hentze, 2007; Wakiyama et al…”
Following translation by single ribosomes one codon at a time
Wen, J.-D., Lancaster, L., Hodges, C., Zeri, A., Yoshimura, S., Noller, H., Bustamante, C., & Tinoco, I. (2008) · Nature · doi:10.1038/nature06716 · Cited by 292 · cited 1× · see citing works
“Recently, singlemolecule experiments were used to study the kinetics of ribosome movement on the mRNA during translation (Wen et al., 2008).”
Structural Roles for Human Translation Factor eIF3 in Initiation of Protein Synthesis
Siridechadilok, B., Fraser, C., Hall, R., Doudna, J., & Nogales, E. (2005) · Science · doi:10.1126/science.1118977 · Cited by 291 · cited 3× · see citing works
“A cryo-EM model of the eIF3eIF4G-40S complex places eIF4G near the mRNA exit channel on the solvent side of the 40S subunit (Siridechadilok et al., 2005).”
Katsafanas, G., & Moss, B. (2007) · Cell Host and Microbe · doi:10.1016/j.chom.2007.08.005 · Cited by 280 · see citing works
Ostareck, D., Ostareck-Lederer, A., Shatsky, I., & Hentze, M. (2001) · Cell · doi:10.1016/s0092-8674(01)00212-4 · Cited by 280 · see citing works
Cho, P. F., Poulin, F., Yoon, A. C.-P., Cho-Park, I. B., Chicoine, J., Lasko, P., & Sonenberg, N. (2005) · Cell · doi:10.1016/j.cell.2005.02.024 · Cited by 279 · cited 1× · see citing works
“Bicoid represses the translation of caudal mRNA at the anterior of the embryo, where it is present, by binding simultaneously to the 3′UTR of caudal mRNA and to an eIF4E-related protein (d4E-HP) at the 5′ end of the mRNA (Figure 4A) (Cho et al., 2005).”
Self-citationSampath, P., Pritchard, D. K., Pabon, L., Reinecke, H., Schwartz, S. M., Morris, D. R., & Murry, C. E. (2008) · Cell Stem Cell · doi:10.1016/j.stem.2008.03.013 · Cited by 277 · cited 1× · see citing works
“Sampath et al. (2008) demonstrated a striking increase in ribosome recruitment to mRNA during the differentiation of ESCs into embryoid bodies.”
Semotok, J., Cooperstock, R. L., Pinder, B., Vari, H. K., Lipshitz, H., & Smibert, C. (2005) · Current Biology · doi:10.1016/j.cub.2005.01.048 · Cited by 275 · cited 1× · see citing works
“, 2004), or recruiting the CCR4 deadenylase complex to specific target mRNAs (Chicoine et al., 2007; Kadyrova et al., 2007; Semotok et al., 2005; Zaessinger et al., 2006), also contribute importantly to embryonic patterning and development.”
Drosophila Cup is an eIF4E‐binding protein that functions in Smaug‐mediated translational repression
Nelson, M. R., Leidal, A. M., & Smibert, C. (2004) · EMBO Journal · doi:10.1038/sj.emboj.7600026 · Cited by 275 · cited 1× · see citing works
“Cup, an eIF4E-binding protein, is recruited to nanos mRNA by Smaug (Nelson et al., 2004) and to oskar mRNA by Bruno (Chekulaeva et al.”
4E-Binding Protein 1: A Key Molecular “Funnel Factor” in Human Cancer with Clinical Implications
Armengol, G., Rojo, F., Castellví, J., Iglesias, C., Cuatrecasas, M., Pons, B., Baselga, J. M., & y Cajal, S. R. (2007) · Cancer Research · doi:10.1158/0008-5472.can-07-0881 · Cited by 272 · see citing works
Viral IRES RNA structures and ribosome interactions.
Kieft, J. (2008) · TIBS -Trends in Biochemical Sciences. Regular ed · doi:10.1016/j.tibs.2008.04.007 · Cited by 272 · see citing works
Topisirovic, I., Ruiz-Gutierrez, M., & Borden, K. (2004) · Cancer Research · doi:10.1158/0008-5472.can-04-2677 · Cited by 267 · cited 2× · see citing works
“A Ser209Ala mutant of eIF4E is unable to transform NIH 3T3 cultured cells (Topisirovic et al., 2004). Furthermore, Wendel et al. (2007) demonstrated that Ser209 is required for eIF4E’s oncogenic activity in a mouse model of B cell lymphoma.”
Structural basis for messenger RNA movement on the ribosome
Yusupova, G. Z., Jenner, L. B., Rees, B., Moras, D., & Yusupov, M. (2006) · Nature · doi:10.1038/nature05281 · Cited by 264 · cited 1× · see citing works
“The stunning progress on crystal structures of bacterial 70S ribosomes bound to mRNAs and tRNAs (Selmer et al., 2006; Yusupova et al., 2006) has provided atomic details of the path of mRNA and contacts made with tRNAs in the decoding sites.”
MicroRNAs and viral infection.
Sullivan, C. S., & Ganem, D. (2005) · Molecules and Cells · doi:10.1016/j.molcel.2005.09.012 · Cited by 262 · see citing works
Algire, M. A., Maag, D., & Lorsch, J. (2005) · Molecules and Cells · doi:10.1016/j.molcel.2005.09.008 · Cited by 262 · cited 1× · see citing works
“These “gate-keeper” functions are neutralized at the AUG codon when eIF1 dissociates from its location near the P-site (Algire et al., 2005; Maag et al., 2005).”
Buchkovich, N. J., Yu, Y., Zampieri, C. A., & Alwine, J. (2008) · Nature Reviews Microbiology · doi:10.1038/nrmicro1855 · Cited by 255 · cited 1× · see citing works
“Stimulation of eIF4F assembly is caused in part by the activation of the PI3K/Akt/mTOR pathway, which results in phosphorylation of 4E-BPs through different mechanisms (Buchkovich et al., 2008).”
Topology and regulation of the human eIF4A/4G/4H helicase complex in translation initiation
Marintchev, A., Edmonds, K., Marintcheva, B., Hendrickson, E., Oberer, M., Suzuki, C., Herdy, B., Sonenberg, N., & Wagner, G. (2009) · Cell · doi:10.1016/j.cell.2009.01.014 · Cited by 248 · cited 1× · see citing works
“An intriguing new structural model envisions that eIF4G could interact with mRNA sequences both upstream and downstream of the nucleotides located in the decoding sites and could position eIF4A at the mRNA entry channel for its presumed role in unwinding secondary structure in advance of the scanning PIC (Marintchev e…”
Self-citationChekulaeva, M., Hentze, M., & Ephrussi, A. (2006) · Cell · doi:10.1016/j.cell.2006.01.031 · Cited by 247 · see citing works
Translation initiation on mammalian mRNAs with structured 5′-UTRs requires DExH-box protein DHX29
Pisareva, V., Pisarev, A., Komar, A., Hellen, C., & Pestova, T. (2008) · Cell · doi:10.1016/j.cell.2008.10.037 · Cited by 241 · see citing works
Recycling of eukaryotic posttermination ribosomal complexes.
Pisarev, A., Hellen, C., & Pestova, T. (2007) · Cell · doi:10.1016/j.cell.2007.08.041 · Cited by 241 · cited 1× · see citing works
“Interestingly, eIF3 was implicated in dissociation of 60S subunits from posttermination ribosomes following polypeptide termination, when ribosome recycling was reconstituted in vitro (Pisarev et al., 2007).”
New modes of translational control in development, behavior, and disease.
Sonenberg, N., & Hinnebusch, A. (2007) · Molecules and Cells · doi:10.1016/j.molcel.2007.11.018 · Cited by 240 · see citing works
Self-citationTranslational control of maternal Cyclin B mRNA by Nanos in the Drosophila germline
Kadyrova, L. Y., Habara, Y., Lee, T. H., & Wharton, R. P. (2007) · Development · doi:10.1242/dev.002212 · Cited by 240 · cited 1× · see citing works
“, 2004), or recruiting the CCR4 deadenylase complex to specific target mRNAs (Chicoine et al., 2007; Kadyrova et al., 2007; Semotok et al., 2005; Zaessinger et al., 2006), also contribute importantly to embryonic patterning and development.”
Schütz, P., Bumann, M., Oberholzer, A., Bieniossek, C., Trachsel, H., Altmann, M., & Baumann, U. (2008) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.0800418105 · Cited by 239 · cited 1× · see citing works
“Binding to eIF4G helps to hold the two lobes of eIF4A together and align the DEAD-box motifs in the orientation required for ATP-dependent helicase activity (Schutz et al., 2008).”
Epigenetic Activation of a Subset of mRNAs by eIF4E Explains Its Effects on Cell Proliferation
Mamane, Y., Petroulakis, E., Martineau, Y., Sato, T.-A., Larsson, O., Rajasekhar, V., & Sonenberg, N. (2007) · PLoS ONE · doi:10.1371/journal.pone.0000242 · Cited by 237 · cited 1× · see citing works
“The transforming activity of eIF4E can be explained by its ability to promote translation of a subset of mRNAs encoding proteins involved in regulating growth, proliferation, and apoptosis, most likely in a combinatorial fashion (Larsson et al., 2007; Mamane et al., 2007).”
Self-citationEukaryotic Initiation Factor 6 is rate-limiting in translation, growth and transformation
Gandin, V., Miluzio, A., Barbieri, A., Beugnet, A., Kiyokawa, H., Marchisio, P., & Biffo, S. (2008) · Nature · doi:10.1038/nature07267 · Cited by 235 · cited 1× · see citing works
“The factor eIF6 binds to 60S subunits and could thereby regulate ribosomal subunit joining, but evidence for a role in general translation initiation in vivo was obtained only recently (Gandin et al., 2008).”
Structure of the 30S translation initiation complex
Simonetti, A., Marzi, S., Myasnikov, A. G., Fabbretti, A., Yusupov, M., Gualerzi, C. O., & Klaholz, B. P. (2008) · Nature · doi:10.1038/nature07192 · Cited by 235 · cited 1× · see citing works
“Interestingly, it is seen that domain IV of IF2 interacts with the accepter end of Met-tRNAi, explaining how IF2 stabilizes fMet-tRNAi binding until the 50S subunit joins (Simonetti et al., 2008).”
Cap-Independent Translation Is Required for Starvation-Induced Differentiation in Yeast
Gilbert, W., Zhou, K., Butler, T. K., & Doudna, J. (2007) · Science · doi:10.1126/science.1144467 · Cited by 232 · see citing works
Ribosomal position and contacts of mRNA in eukaryotic translation initiation complexes
Pisarev, A. V., KOLUPAEVA, V. G., Yusupov, M., Hellen, C. U. T., & Pestova, T. V. (2008) · The EMBO Journal · doi:10.1038/emboj.2008.90 · Cited by 227 · cited 3× · see citing works
“Indeed, UV crosslinking of substituted mRNAs in reconstituted mammalian 48S PICs revealed many similarities with the mRNA path in bacterial 70S complexes (Pisarev et al., 2008).”
Zaessinger, S., Busseau, I., & Simonelig, M. (2006) · Development · doi:10.1242/dev.02649 · Cited by 212 · cited 2× · see citing works
“, 2004), or recruiting the CCR4 deadenylase complex to specific target mRNAs (Chicoine et al., 2007; Kadyrova et al., 2007; Semotok et al., 2005; Zaessinger et al., 2006), also contribute importantly to embryonic patterning and development.”
Structure of the ribosome-bound cricket paralysis virus IRES RNA
Schüler, M., Connell, S., Lescoute, A., Giesebrecht, J., Dabrowski, M., Schroeer, B., Mielke, T., Penczek, P., Westhof, E., & Spahn, C. (2006) · Nature Structural &Molecular Biology · doi:10.1038/nsmb1177 · Cited by 212 · cited 1× · see citing works
“This IRES uses different pseudoknot domains to contact 40S and 60S components and occupy the decoding center, placing the GCU triplet in the A-site (Schuler et al., 2006) where translation begins after a “pseudotranslocation” event moves the alanyltRNA decoding the GCU triplet into the P-site (Doudna and Sarnow, 2007;…”
Maag, D., Fekete, C. A., Gryczynski, Z., & Lorsch, J. (2005) · Molecules and Cells · doi:10.1016/j.molcel.2004.11.051 · Cited by 211 · cited 1× · see citing works
“These “gate-keeper” functions are neutralized at the AUG codon when eIF1 dissociates from its location near the P-site (Algire et al., 2005; Maag et al., 2005).”
14-3-3σ controls mitotic translation to facilitate cytokinesis
Wilker, E., van Vugt, M. V., Artim, S. C., Huang, P. H., Petersen, C. P., Reinhardt, H., Feng, Y., Sharp, P. A., Sonenberg, N., White, F. M., et al. (2007) · Nature · doi:10.1038/nature05584 · Cited by 209 · cited 2× · see citing works
“The tumor suppressor 14-3-3σ inhibits cap-dependent translation during mitosis through its binding to several initiation factors, which is expected to result in elevated IRES-dependent translation (Wilker et al., 2007).”
Self-citationTranslation factors promote the formation of two states of the closed-loop mRNP
Amrani, N., Ghosh, S., Mangus, D. A., & Jacobson, A. (2008) · Nature · doi:10.1038/nature06974 · Cited by 200 · cited 1× · see citing works
“Surprisingly, this last interaction also stimulates initiation complex (IC) formation in vitro independently of a prior termination event (Amrani et al., 2008).”
Eukaryotic translation initiation machinery can operate in a bacterial-like mode without eIF2
Terenin, I., Dmitriev, S., Andreev, D., & Shatsky, I. (2008) · Nature Structural &Molecular Biology · doi:10.1038/nsmb.1445 · Cited by 193 · cited 1× · see citing works
“The IRESs of hepatitis C virus (HCV) dispense with eIF4F entirely, binding directly to the 40S, and require only eIF3 and either eIF2/eIF5 or eIF5B to pair tRNAi with the IRES start codon and produce a 48S PIC competent for subunit joining (Pestova et al., 2008; Terenin et al., 2008).”
CPEB Interacts with an Ovary-specific eIF4E and 4E-T in Early Xenopus Oocytes*
Minshall, N., Reiter, M., Weil, D., & Standart, N. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m704629200 · Cited by 181 · cited 1× · see citing works
“In early oogenesis when Maskin is absent, a different mechanism operates to silence the translation of maternal mRNAs in which CPEB binds to eIF4E1b (a homolog of eIF4E) through 4E-T (4E-transporter) (Figure 4A) (Minshall et al., 2007).”
Role for mRNA localization in translational activation but not spatial restriction of nanos RNA
Bergsten, S. E., & Gavis, E. R. (1999) · Development · doi:10.1242/dev.126.4.659 · Cited by 180 · see citing works
Dissociation of eIF1 from the 40S ribosomal subunit is a key step in start codon selection in vivo.Preprint
Cheung, Y., Maag, D., Mitchell, S. F., Fekete, C. A., Algire, M. A., Takacs, J. E., Shirokikh, N. E., Pestova, T., Lorsch, J., & Hinnebusch, A. (2007) · Genes & Development · doi:10.1101/gad.1528307 · Cited by 175 · cited 1× · see citing works
“, UUG) start codons by allowing premature eIF1 dissociation (Cheung et al., 2007), whereas overexpressing eIF1 suppresses UUG initiation in relaxed-fidelity (Sui−) yeast mutants.”
Self-citationtRNA–mRNA mimicry drives translation initiation from a viral IRES
Costantino, D., Pfingsten, J. S., Rambo, R., & Kieft, J. (2008) · Nature Structural &Molecular Biology · doi:10.1038/nsmb1351 · Cited by 173 · cited 1× · see citing works
“Remarkably, the IRES domain that occupies the P-site mimics precisely the anticodon stem loop of tRNAi and an AUG start codon (Costantino et al., 2008) (Figure 3B).”
VASA mediates translation through interaction with a Drosophila yIF2 homolog.
Carrera, P., Johnstone, O., Nakamura, A., Casanova, J., Jäckle, H., & Lasko, P. (2000) · Molecules and Cells · doi:10.1016/s1097-2765(00)80414-1 · Cited by 170 · cited 1× · see citing works
“Vasa (Vas) is a DEAD-box helicase that localizes during oogenesis to the posterior and that binds to eIF5B (Carrera et al., 2000).”
A plant viral "reinitiation" factor interacts with the host translational machinery.
Park, H., Himmelbach, A., Browning, K., Hohn, T., & Ryabova, L. (2001) · Cell · doi:10.1016/s0092-8674(01)00487-1 · Cited by 167 · cited 1× · see citing works
“, 2004) and is targeted by the protein TAV (transactivator/viroplasmin) that enables efficient reinitiation on polycistronic mRNAs of cauliflower mosaic virus (Park et al., 2001).”
Gaba, A., Jacobson, A., & Sachs, M. (2005) · Molecules and Cells · doi:10.1016/j.molcel.2005.09.019 · Cited by 166 · cited 1× · see citing works
“Stalling at the stop codon of the uORF controlling translation of yeast CPA1 (encoding an arginine biosynthetic enzyme) is dependent on arginine and, interestingly, the stalled ribosome activates nonsense-mediated decay to also reduce CPA1 mRNA levels (Gaba et al., 2005).”
Cho, P. F., Gamberi, C., Yoon, A. C.-P., Cho-Park, I. B., Lasko, P., & Sonenberg, N. (2006) · Current Biology · doi:10.1016/j.cub.2006.08.093 · Cited by 165 · cited 1× · see citing works
“Similarly, d4E-HP binds to a protein complex containing Nanos at the 3′UTR of hunchback mRNA to inhibit its translation at the posterior (Cho et al., 2006).”
Self-citationValášek, L., Mathew, A., Shin, B., Nielsen, K. H., Szamecz, B., & Hinnebusch, A. (2003) · Genes & Development · doi:10.1101/gad.1065403 · Cited by 164 · see citing works
Self-citationLarsson, O., Li, S.-N., Issaenko, O. A., Avdulov, S. V., Peterson, M., Smith, K. A., Bitterman, P., & Polunovsky, V. (2007) · Cancer Research · doi:10.1158/0008-5472.can-07-0752 · Cited by 162 · cited 1× · see citing works
“The transforming activity of eIF4E can be explained by its ability to promote translation of a subset of mRNAs encoding proteins involved in regulating growth, proliferation, and apoptosis, most likely in a combinatorial fashion (Larsson et al., 2007; Mamane et al., 2007).”
Chicoine, J., Benoit, P., Gamberi, C., Paliouras, M., Simonelig, M., & Lasko, P. (2007) · Developmental Cell · doi:10.1016/j.devcel.2007.10.002 · Cited by 161 · see citing works
HCV and CSFV IRES domain II mediate eIF2 release during 80S ribosome assembly
Locker, N., Easton, L. E., & Lukavsky, P. (2007) · EMBO Journal · doi:10.1038/sj.emboj.7601549 · Cited by 161 · cited 1× · see citing works
“Domain II is also crucial for eIF5-dependent GTP hydrolysis by TC (in the eIF2-dependent mode of initiation) and subunit joining (Doudna and Sarnow, 2007; Locker et al., 2007; Pestova et al., 2008), suggesting that it also facilitates the conformational change(s) elicited by perfect codon-anticodon pairing in the cano…”
Interaction with eIF5B is essential for Vasa function during development
Johnstone, O., & Lasko, P. (2004) · Development · doi:10.1242/dev.01286 · Cited by 156 · cited 1× · see citing works
“In vas null oocytes, grk translation is greatly reduced, an effect also observed in oocytes that express only a form of Vas (VasΔ617) that is specifically compromised for eIF5B binding (Johnstone and Lasko, 2004).”
eIF2‐dependent and eIF2‐independent modes of initiation on the CSFV IRES: a common role of domain II
Pestova, T., de Breyne, S., Pisarev, A., Abaeva, I., & Hellen, C. (2008) · EMBO Journal · doi:10.1038/emboj.2008.49 · Cited by 155 · cited 2× · see citing works
“Domain II is also crucial for eIF5-dependent GTP hydrolysis by TC (in the eIF2-dependent mode of initiation) and subunit joining (Doudna and Sarnow, 2007; Locker et al., 2007; Pestova et al., 2008), suggesting that it also facilitates the conformational change(s) elicited by perfect codon-anticodon pairing in the cano…”
RNA-mediated sequestration of the RNA helicase eIF4A by Pateamine A inhibits translation initiation.
Bordeleau, M.-È., Cencic, R., Lindqvist, L., Oberer, M., Northcote, P., Wagner, G., & Pelletier, J. (2006) · Chemistry and Biology · doi:10.1016/j.chembiol.2006.10.005 · Cited by 154 · cited 1× · see citing works
“Screening natural compound libraries yielded potent inhibitors of eIF4A (Bordeleau et al., 2006; Pelletier and Peltz, 2007).”
daf-16 Protects the Nematode Caenorhabditis elegans During Food Deprivation
Henderson, S. T., Bonafè, M., & Johnson, T. E. (2006) · The Journals of Gerontology Series A · doi:10.1093/gerona/61.5.444 · Cited by 154 · cited 1× · see citing works
“Studies in the nematode Caenorhabditis elegans demonstrated that inhibition of several components of the eIF4F complex including eIF4E and eIF4G or lowering their levels extends life span (Pan et al., 2007; Syntichaki et al., 2007; Curran and Ruvkun, 2007; Hansen et al., 2007; Henderson et al., 2006).”
DAPK-ZIPK-L13a Axis Constitutes a Negative-Feedback Module Regulating Inflammatory Gene Expression
Mukhopadhyay, R., Ray, P. S., Arif, A., Brady, A. K., Kinter, M., & Fox, P. (2008) · Molecules and Cells · doi:10.1016/j.molcel.2008.09.019 · Cited by 151 · cited 1× · see citing works
“Recently, Fox and colleagues (Mukhopadhyay et al., 2008) showed that the zipper-interacting protein kinase (ZIPK) phosphorylates L13a on a single site and, in turn, is activated by phosphorylation of a second IFNγ-induced kinase, death-associated protein kinase-1.”
Szamecz, B., Rutkai, E., Cuchalová, L., Munzarová, V., Herrmannová, A., Nielsen, K. H., Burela, L., Hinnebusch, A., & Valášek, L. (2008) · Genes & Development · doi:10.1101/gad.480508 · Cited by 145 · cited 1× · see citing works
“There is now evidence that the 5′ enhancer sequences interact with the eIF3a-NTD (N-terminal domain), presumably as they emerge from the mRNA exit pore, to promote retention of post-termination 40S subunits on the mRNA (Szamecz et al., 2008).”
Self-citationMitchell, S. A., Spriggs, K. A., Bushell, M., Evans, J. R., Stoneley, M., Quesne, J. L., Spriggs, R. V., & Willis, A. (2005) · Genes & Development · doi:10.1101/gad.339105 · Cited by 142 · see citing works
Kinetic checkpoint at a late step in translation initiation.
Milón, P., Konevega, A., Gualerzi, C., & Rodnina, M. (2008) · Molecules and Cells · doi:10.1016/j.molcel.2008.04.014 · Cited by 141 · cited 1× · see citing works
“Moreover, IF1 inhibits subunit joining to the 30S IC when these mRNA signals are absent (Milon et al., 2008), reminiscent of the role played by the eIF1A in blocking non-AUG selection during scanning.”
eIF3j is located in the decoding center of the human 40S ribosomal subunit.
Fraser, C., Berry, K. E., Hershey, J., & Doudna, J. (2007) · Molecules and Cells · doi:10.1016/j.molcel.2007.05.019 · Cited by 140 · cited 1× · see citing works
“Interestingly, the j-subunit of eIF3 can bind near the A-site and mRNA entry channel of the 40S subunit and impede mRNA binding in the absence of TC, presumably to ensure that TC loading precedes 40S binding to mRNA (Fraser et al., 2007).”
N‐ and C‐terminal residues of eIF1A have opposing effects on the fidelity of start codon selection
Fekete, C. A., Mitchell, S. F., Cherkasova, V., Applefield, D., Algire, M. A., Maag, D., Saini, A., Lorsch, J., & Hinnebusch, A. (2007) · EMBO Journal · doi:10.1038/sj.emboj.7601613 · Cited by 132 · cited 2× · see citing works
“Its C-terminal region promotes continued scanning at non-AUG codons, whereas its N-terminal extension acts in the opposite way to arrest scanning and promote eIF1 release at AUG codons (Fekete et al., 2007) (Figure 2A).”
Self-citationDivergent tRNA-like element supports initiation, elongation, and termination of protein biosynthesis
Jan, E., Kinzy, T., & Sarnow, P. (2003) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.2535183100 · Cited by 131 · cited 1× · see citing works
“, 2006) where translation begins after a “pseudotranslocation” event moves the alanyltRNA decoding the GCU triplet into the P-site (Doudna and Sarnow, 2007; Jan et al., 2003).”
Antoun, A., Pavlov, M., Lovmar, M., & Ehrenberg, M. (2006) · Molecules and Cells · doi:10.1016/j.molcel.2006.05.030 · Cited by 130 · cited 1× · see citing works
“cognate elongator tRNAs at the expense of Met-tRNAi (Antoun et al., 2006).”
Svitkin, Y., Herdy, B., Costa-Mattioli, M., Gingras, A., Raught, B., & Sonenberg, N. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.23.10556-10565.2005 · Cited by 126 · cited 1× · see citing works
“Inhibition of cap-dependent translation in vitro causes an increase in IRES-dependent translation (Svitkin et al., 2005).”
Self-citationThe fidelity of translation initiation: reciprocal activities of eIF1, IF3 and YciH
Lomakin, I., Shirokikh, N. E., Yusupov, M., Hellen, C., & Pestova, T. (2006) · EMBO Journal · doi:10.1038/sj.emboj.7600904 · Cited by 126 · cited 1× · see citing works
“IF3 and eIF1 can even substitute for one another in vitro, suggesting that they elicit similar conformational changes in the PIC according to codon-anticodon pairing in the P-site (Lomakin et al., 2006).”
Shin, B., Maag, D., Roll-Mecak, A., Arefin, M. S., Burley, S., Lorsch, J., & Dever, T. (2002) · Cell · doi:10.1016/s0092-8674(02)01171-6 · Cited by 123 · see citing works
Gomez, E., Mohammad, S. S., & Pavitt, G. (2002) · EMBO Journal · doi:10.1093/emboj/cdf515 · Cited by 120 · cited 1× · see citing works
“Remarkably, only a small portion of one subunit (ε) of eIF2B is sufficient for GEF function (Gomez et al., 2002), and three of the remaining subunits provide a binding site for phosphorylated eIF2α that inhibits GEF function (Hinnebusch et al.”
Walsh, D., Arias, C., Pérez, C., Halladin, D. K., Escandon, M., Ueda, T., Watanabe‐Fukunaga, R., Fukunaga, R., & Mohr, I. (2008) · Molecular and Cellular Biology · doi:10.1128/mcb.01631-07 · Cited by 116 · cited 1× · see citing works
“Finally, Vaccinia virus promotes eIF4F assembly and also recruits initiation factors to cytoplasmic replication compartments, effectively increasing their local concentration (Katsafanas and Moss, 2007; Walsh et al., 2008).”
A dual inhibitory mechanism restricts msl-2 mRNA translation for dosage compensation in Drosophila.
Beckmann, K., Grs̆ković, M., Gebauer, F., & Hentze, M. (2005) · Cell · doi:10.1016/j.cell.2005.06.011 · Cited by 115 · cited 1× · see citing works
“Dosage compensation is eliminated in females by translational repression of MSL-2 mRNA by Sex-lethal (SXL) protein, expressed only in females, by a combination of two mechanisms: SXL binds to the 3′UTR of the msl-2 mRNA together with the RNA-binding protein, UNR, and inhibits recruitment of the 43S PIC to the mRNA, wh…”
Higher-Order Substrate Recognition of eIF2α by the RNA-Dependent Protein Kinase PKR
Dar, A., Dever, T., & Sicheri, F. (2005) · Cell · doi:10.1016/j.cell.2005.06.044 · Cited by 107 · see citing works
Searfoss, A. M., Dever, T., & Wickner, R. (2001) · Molecular and Cellular Biology · doi:10.1128/mcb.21.15.4900-4908.2001 · Cited by 105 · see citing works
Kim, T.-H., Kim, B.-H., Yahalom, A., Chamovitz, D., & von Arnim, A. G. (2004) · The Plant Cell Online · doi:10.1105/tpc.104.026880 · Cited by 103 · see citing works
Acker, M., Shin, B., Dever, T., & Lorsch, J. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m600210200 · Cited by 100 · cited 1× · see citing works
“Interaction of eIF5B with the extreme C terminus of eIF1A stimulates both subunit joining and the GTP hydrolysis that triggers eIF5B release from the initiation complex (Acker et al., 2006; Shin et al., 2002).”
Pöyry, T., Kaminski, A., Connell, E., Fraser, C., & Jackson, R. (2007) · Genes & Development · doi:10.1101/gad.439507 · Cited by 97 · cited 1× · see citing works
“eIF3 also stimulates reinitiation after translation of a long uORF in a polycistronic mRNA of feline calicivirus (FCV) by binding to a sequence at the 3′ end of the uORF (Poyry et al., 2007).”
L13a Blocks 48S Assembly: Role of a General Initiation Factor in mRNA-Specific Translational Control
Kapasi, P., Chaudhuri, S., Vyas, K., Baus, D., Komar, A. A., Fox, P. L., Merrick, W. C., & Mazumder, B. (2007) · Molecular Cell · doi:10.1016/j.molcel.2006.11.028 · Cited by 94 · see citing works
Assembly of an active translation initiation factor complex by a viral protein.Preprint
Walsh, D., & Mohr, I. (2006) · Genes & Development · doi:10.1101/gad.1375006 · Cited by 93 · cited 1× · see citing works
“In addition, viral gene products, such as the ICP6 of Herpes simplex virus, which binds to eIF4G, enhance eIF4F assembly (Walsh and Mohr, 2006).”
5 Translation Initiation by Viral Internal Ribosome Entry SitesPreprint
Doudna, J., & Sarnow, P. (2007) · Cold Spring Harbor Monograph Archive · doi:10.1101/087969767.48.129 · Cited by 93 · see citing works
13 eIF2α Phosphorylation in Cellular Stress Responses and DiseasePreprint
Ron, D., & Harding, H. (2007) · Cold Spring Harbor Monograph Archive · doi:10.1101/087969767.48.345 · Cited by 92 · see citing works
Activation of Host Translational Control Pathways by a Viral Developmental Switch
Arias, C., Walsh, D., Harbell, J., Wilson, A., & Mohr, I. (2009) · PLoS Pathogens · doi:10.1371/journal.ppat.1000334 · Cited by 80 · cited 1× · see citing works
“This is important for acute virus replication in quiescent cells and is also observed upon reactivation of latent infections (Arias et al., 2009).”
An mRNA-rRNA base-pairing mechanism for translation initiation in eukaryotes
Dresios, J., Chappell, S., Zhou, W., & Mauro, V. (2006) · Nature Structural &Molecular Biology · doi:10.1038/nsmb1031 · Cited by 79 · cited 1× · see citing works
“, 2007), and sequences capable of Shine-Delgarno-like pairing with rRNA (Dresios et al., 2006).”
Squid, Cup, and PABP55B function together to regulate gurken translation in Drosophila.
Clouse, K. N., Ferguson, S. B., & Schüpbach, T. (2008) · Developmental Biology · doi:10.1016/j.ydbio.2007.11.008 · Cited by 77 · cited 1× · see citing works
“Activation of grk mRNA translation at the anterodorsal cortex of the developing oocyte is mediated by poly(A) binding protein 55D (PABP55D) in association with the large cytoplasmic protein Encore (Clouse et al., 2008).”
Janzen, D. M., Frolova, L., & Geballe, A. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.24.8562-8570.2002 · Cited by 76 · cited 1× · see citing works
“For the uORF that inhibits translation of the cytomegalovirus UL4 gene, the uORF-encoded peptidyl-tRNA interacts with release factor eRF1 to block polypeptide hydrolysis and stall the ribosome at the stop codon (Janzen et al., 2002).”
Fringer, J., Acker, M., Fekete, C. A., Lorsch, J., & Dever, T. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.02254-06 · Cited by 72 · cited 1× · see citing works
“Its interaction with eIF1A helps to recruit eIF5B to the 48S PIC for subunit joining while eIF5B, in turn, promotes release of eIF1A from the 80S initiation complex to open up the A-site for the first aminoacyl-tRNA (Fringer et al., 2007).”
Norsgaard, H., Clark, B., & Rattan, S. I. S. (1996) · Experimental Gerontology · doi:10.1016/0531-5565(96)00011-3 · Cited by 60 · cited 1× · see citing works
“Aging is associated with decreased protein synthesis (Norsgaard et al., 1996).”
9 Mechanism of Translation Initiation in the Yeast Saccharomyces cerevisiaePreprint
Hinnebusch, A., Dever, T., & Asano, K. (2007) · Cold Spring Harbor Monograph Archive · doi:10.1101/087969767.48.225 · Cited by 58 · see citing works
Self-citation15 Translational Control in Cancer Development and Progression
Schneider, R., & Sonenberg, N. (2007) · doi:10.1101/087969767.48.401 · Cited by 43
Self-citationDong, J.-S., Nanda, J., Rahman, H., Pruitt, M. R., Shin, B., Wong, C.-M., Lorsch, J., & Hinnebusch, A. (2008) · Genes & Development · doi:10.1101/gad.1696608 · Cited by 41 · cited 1× · see citing works
“Moreover, there is genetic evidence that certain rRNA contacts with the P-site tRNA in 70S complexes are functionally conserved in eukaryotic PICs (Dong et al., 2008).”
Self-citationCis-regulatory sequences and trans-acting factors in translation control
Hentze, M., Gebauer, F., & Preiss, T. (2007) · ANU Open Research (Australian National University) · doi:10.1101/087969767.48.269 · Cited by 36 · see citing works
20 Protein Synthesis and Translational Control during Viral Infection
Mohr, I., Pe'ery, T., & Mathews, M. (2007) · doi:10.1101/087969767.48.545 · Cited by 35
30 Therapeutic Opportunities in TranslationPreprint
Pelletier, J., & Peltz, S. (2007) · Cold Spring Harbor Monograph Archive · doi:10.1101/087969767.48.855 · Cited by 17 · see citing works
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- Elroy-Stein O Merrick WC Mathews M Sonenberg N Hershey JWB 2007 Translation initiation via celluar internal ribosome entry sites Translational Control in Biology and Medicine Cold Spring Harbor, NY Cold Spring Harbor Laboratory Press 155 172
- Fox PL Ray PS Arif A Jia J Mathews M Sonenberg N Hershey JWB 2007 Noncanonical functions of aminoacyl-tRNA synthetases in translational control Translational Control in Biology and Medicine Cold Spring Harbor, NY Cold Spring Harbor Laboratory Press 804 829
- Klann E Richter JD Mathews M Sonenberg N Hershey JWB 2007 Translational control of synaotic plasticity and learning and memory Translational Control in Bioloy and Medicine Cold Spring Harbor, NY Cold Spring Harbor Laboratory Press 485 506
- Pestova TV Lorsch JR Hellen CUT Mathews M Sonenberg N Hershey JWB 2007 The mechanism of translation initiation in eukaryotes Translational Control in Biology and Medicine Cold Spring Harbor, NY Cold Spring Harbor Laboratory Press 87 128
- Raught B Gingras AC Mathews M Sonenberg N Hershey JWB 2007 Signaling to translation initiation Translational Control in Biology and Medicine Cold Spring Harbor, NY Cold Spring Harbor Laboratory Press 369 400
- Ron D Harding HP Mathews M Sonenberg N Hershey JWB 2007 eIF2α phosphorylation in celluar stress responses and disease Translational Control in Biology and Medicine Cold Spring Harbor, NY Cold Spring Harbor Laboratory Press 345 368
- Thompson B Wickens M Kimble J Mathews M Sonenberg N Hershey JWB 2007 Translational control in development Translational Control in Biology and Medicine Cold Spring Harbor, NY Cold Spring Harbor Laboratory Press 486 507
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Sorted by citations
Global quantification of mammalian gene expression control
Schwanhäusser, B., Busse, D., Li, N., Dittmar, G., Schuchhardt, J., Wolf, J., Chen, W., & Selbach, M. (2011) · Nature · doi:10.1038/nature10098 · Cited by 6,566 · see citing works
Ingolia, N. T., Lareau, L. F., & Weissman, J. S. (2011) · Cell · doi:10.1016/j.cell.2011.10.002 · Cited by 2,187 · see citing works
Extensive translation of circular RNAs driven by N6-methyladenosine
Yang, Y., Fan, X., Mao, M., Song, X., Wu, P., Zhang, Y., Jin, Y., Yang, Y., Chen, L.-L., Wang, Y., et al. (2017) · Cell Research · doi:10.1038/cr.2017.31 · Cited by 1,855 · see citing works
Pamudurti, N. R., Bartok, O., Jens, M., Ashwal-Fluss, R., Stottmeister, C., Ruhe, L., Hanan, M., Wyler, E., Perez-Hernandez, D., Ramberger, E., et al. (2017) · Molecular Cell · doi:10.1016/j.molcel.2017.02.021 · Cited by 1,810 · see citing works
Global signatures of protein and mRNA expression levels
de Sousa Abreu, R., Penalva, L. O., Marcotte, E. M., & Vogel, C. (2009) · Molecular BioSystems · doi:10.1039/b908315d · Cited by 1,248 · see citing works
Cellular Adaptation to Hypoxia through Hypoxia Inducible Factors and beyond
Lee, P., Chandel, N. S., & Simon, M. C. (2020) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-020-0227-y · Cited by 1,272 · see citing works
Mechanisms of Life Span Extension by Rapamycin in the Fruit Fly Drosophila Melanogaster
Bjedov, I., Toivonen, J. M., Kerr, F., Slack, C., Jacobson, J., Foley, A., & Partridge, L. (2010) · Cell Metabolism · doi:10.1016/j.cmet.2009.11.010 · Cited by 1,057 · see citing works
Functional 5′ UTR mRNA structures in eukaryotic translation regulation and how to find them
Leppek, K., Das, R., & Barna, M. (2018) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2017.103 · Cited by 949 · see citing works
Analysis of aptamer discovery and technology
Dunn, M. R., Jimenez, R. M., & Chaput, J. C. (2017) · Nature Reviews Chemistry · doi:10.1038/s41570-017-0076 · Cited by 938 · see citing works
Targeting the translation machinery in cancer
Bhat, M., Robichaud, N., Hulea, L., Sonenberg, N., Pelletier, J., & Topisirovic, I. (2015) · Nature Reviews Drug Discovery · doi:10.1038/nrd4505 · Cited by 799 · see citing works
Self-citationHigh-Resolution View of the Yeast Meiotic Program Revealed by Ribosome Profiling
Brar, G. A., Yassour, M., Friedman, N., Regev, A., Ingolia, N. T., & Weissman, J. S. (2012) · Science · doi:10.1126/science.1215110 · Cited by 533 · see citing works
Human ADAR1 Prevents Endogenous RNA from Triggering Translational Shutdown
Chung, H., Calis, J. J. A., Wu, X., Sun, T., Yu, Y., Sarbanes, S. L., Dao Thi, V. L., Shilvock, A. R., Hoffmann, H.-H., Rosenberg, B. R., et al. (2018) · Cell · doi:10.1016/j.cell.2017.12.038 · Cited by 538 · see citing works
Gene Expression Regulation by Upstream Open Reading Frames and Human Disease
Barbosa, C., Peixeiro, I., & Romão, L. (2013) · PLoS Genetics · doi:10.1371/journal.pgen.1003529 · Cited by 525 · see citing works
Ribosome collisions trigger general stress responses to regulate cell fate
Wu, C. C.-C., Peterson, A. F., Zinshteyn, B., Regot, S., & Green, R. (2020) · Cell · doi:10.1016/j.cell.2020.06.006 · Cited by 503 · see citing works
“Two commonly used mechanisms for reducing initiation include the phosphorylation of eIF2a by stress-specific kinases and the phosphorylation of 4E-BPs by mTORC1 (Sonenberg and Hinnebusch, 2009).”
Life of RISC: Formation, action, and degradation of RNA-induced silencing complex
Iwakawa, H.-O., & Tomari, Y. (2022) · Molecular Cell · doi:10.1016/j.molcel.2021.11.026 · Cited by 488 · see citing works
Bramham, C. R., Alme, M. N., Bittins, M., Kuipers, S. D., Nair, R. R., Pai, B., Panja, D., Schubert, M., Soule, J., Tiron, A., et al. (2010) · Experimental Brain Research · doi:10.1007/s00221-009-1959-2 · Cited by 452 · see citing works
Dynamic profiling of the protein life cycle in response to pathogens
Jovanovic, M., Rooney, M. S., Mertins, P., Przybylski, D., Chevrier, N., Satija, R., Rodriguez, E. H., Fields, A. P., Schwartz, S., Raychowdhury, R., et al. (2015) · Science · doi:10.1126/science.1259038 · Cited by 460 · see citing works
Weinberg, D. E., Shah, P., Eichhorn, S. W., Hussmann, J. A., Plotkin, J. B., & Bartel, D. P. (2016) · Cell Reports · doi:10.1016/j.celrep.2016.01.043 · Cited by 392 · see citing works
Signaling pathways in Parkinson’s disease: molecular mechanisms and therapeutic interventions
Xu, D.-C., Yong, C., Xu, Y., Chen-Yu, S., & Peng, L. (2023) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-023-01353-3 · Cited by 498 · see citing works
Slobodin, B., Han, R., Calderone, V., Vrielink, J. A. F. O., Loayza-Puch, F., Elkon, R., & Agami, R. (2017) · Cell · doi:10.1016/j.cell.2017.03.031 · Cited by 434 · see citing works
The challenge and prospect of mRNA therapeutics landscape
Weng, Y., Li, C., Yang, T., Hu, B., Zhang, M., Guo, S., Xiao, H., Liang, X.-J., & Huang, Y. (2020) · Biotechnology Advances · doi:10.1016/j.biotechadv.2020.107534 · Cited by 417 · see citing works
mTOR complexes in neurodevelopmental and neuropsychiatric disorders
Costa-Mattioli, M., & Monteggia, L. M. (2013) · Nature Neuroscience · doi:10.1038/nn.3546 · Cited by 367 · see citing works
NRF2 Promotes Tumor Maintenance by Modulating mRNA Translation in Pancreatic Cancer
Chio, I. I. C., Jafarnejad, S. M., Ponz-Sarvise, M., Park, Y., Rivera, K., Palm, W., Wilson, J., Sangar, V., Hao, Y., Öhlund, D., et al. (2016) · Cell · doi:10.1016/j.cell.2016.06.056 · Cited by 378 · see citing works
“…cysteinemodifications, prompting us to further evaluate the functional role of Nrf2 inmRNA translation for pancreatic cancer cells. mRNA Translation Is Impeded in Nrf2-Deficient Cells mRNA translation is a vital cellular process that regulates growth and metabolism (Sonenberg and Hinnebusch, 2009).”
Self-citationNew frontiers in translational control of the cancer genome
Truitt, M. L., & Ruggero, D. (2016) · Nature Reviews Cancer · doi:10.1038/nrc.2016.27 · Cited by 378 · see citing works
Ribosomal proteins and human diseases: molecular mechanisms and targeted therapy
Kang, J., Brajanovski, N., Chan, K. T., Xuan, J., Pearson, R. B., & Sanij, E. (2021) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-021-00728-8 · Cited by 412 · see citing works
Translational control in synaptic plasticity and cognitive dysfunction
Buffington, S. A., Huang, W., & Costa-Mattioli, M. (2014) · Annual Review of Neuroscience · doi:10.1146/annurev-neuro-071013-014100 · Cited by 348 · see citing works
Impact of mRNA chemistry and manufacturing process on innate immune activation
Nelson, J., Sorensen, E. W., Mintri, S., Rabideau, A. E., Zheng, W., Besin, G., Khatwani, N., Su, S. V., Miracco, E. J., Issa, W. J., et al. (2020) · Science Advances · doi:10.1126/sciadv.aaz6893 · Cited by 354 · see citing works
“One possible outcome of immune activation is reduced mRNA translation due to feedback between the innate immune system and translation machinery, which will decrease the potency of therapeutic mRNA ( 18 , 19 ).”
InfluentialRNA targets of wild-type and mutant FET family proteins
Hoell, J. I., Larsson, E., Runge, S., Nusbaum, J. D., Duggimpudi, S., Farazi, T. A., Hafner, M., Borkhardt, A., Sander, C., & Tuschl, T. (2011) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2163 · Cited by 350 · see citing works
Translational control by changes in poly(A) tail length: recycling mRNAs
Weill, L., Belloc, E., Bava, F.-A., & Méndez, R. (2012) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2311 · Cited by 328 · see citing works
Dietary restriction and lifespan: lessons from invertebrate models
Kapahi, P., Kaeberlein, M., & Hansen, M. (2017) · Ageing Research Reviews · doi:10.1016/j.arr.2016.12.005 · Cited by 340 · see citing works
Mammalian stress granules and P bodies at a glance
Riggs, C. L., Kedersha, N., Ivanov, P., & Anderson, P. (2020) · Journal of Cell Science · doi:10.1242/jcs.242487 · Cited by 335 · see citing works
“…of translation inhibition eIF2α-P-independent Na2SeO3, aa starvation, rapamycin, H2O2 Inhibition of mTOR, leading to hypophosphorylation of 4E-BP (Sonenberg and Hinnebusch, 2009) Interference with canonical cap-dependent translation tiRNAs, pateamine A, silvestrol, hippuristanol, rocaglamide…”
BackgroundAn oxygen-regulated switch in the protein synthesis machinery
Uniacke, J., Holterman, C. E., Lachance, G., Franovic, A., Jacob, M. D., Fabian, M. R., Payette, J., Holcik, M., Pause, A., & Lee, S. (2012) · Nature · doi:10.1038/nature11055 · Cited by 319 · see citing works
METTL16 exerts an m6A-independent function to facilitate translation and tumorigenesis
Su, R., Dong, L., Li, Y.-C., Gao, M., He, P., Liu, W., Wei, J.-B., Zhao, Z., Gao, L., Han, L., et al. (2022) · Nature Cell Biology · doi:10.1038/s41556-021-00835-2 · Cited by 305 · see citing works
De Rubeis, S., Pasciuto, E., Li, K. W., Fernández, E., Di Marino, D., Buzzi, A., Ostroff, L. E., Klann, E., Zwartkruis, F. J. T., Komiyama, N. H., et al. (2013) · Neuron · doi:10.1016/j.neuron.2013.06.039 · Cited by 296 · see citing works
Svitkin, Y. V., Cheng, Y. M., Chakraborty, T., Presnyak, V., John, M., & Sonenberg, N. (2017) · Nucleic Acids Research · doi:10.1093/nar/gkx135 · Cited by 278 · see citing works
Self-citationZhang, D., Liu, Y., Zhu, Y., Zhang, Q. Y., Guan, H., Liu, S., Chen, S., Chen, M., Chen, C., Liao, Z., et al. (2022) · Nature Cell Biology · doi:10.1038/s41556-022-00894-z · Cited by 295 · see citing works
IRES-mediated cap-independent translation, a path leading to hidden proteome
Yang, Y., & Wang, Z. (2019) · Journal of Molecular Cell Biology · doi:10.1093/jmcb/mjz091 · Cited by 260 · see citing works
Ribosome profiling reveals post-transcriptional buffering of divergent gene expression in yeast
McManus, C. J., May, G. E., Spealman, P., & Shteyman, A. (2014) · Genome Research · doi:10.1101/gr.164996.113 · Cited by 219 · see citing works
Circular RNA vaccine in disease prevention and treatment
Niu, D., Wu, Y., & Lian, J. (2023) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-023-01561-x · Cited by 273 · see citing works
“326,327 Hence, the requisite modi fi cation can enhance RNA vaccine stability and prevent the innate immune response.”
BackgroundBDNF activates mTOR to regulate GluR1 expression required for memory formation
Slipczuk, L., Bekinschtein, P., Katche, C., Cammarota, M., Izquierdo, I., & Medina, J. H. (2009) · PLoS ONE · doi:10.1371/journal.pone.0006007 · Cited by 246 · see citing works
Synonymous but Not Silent: The Codon Usage Code for Gene Expression and Protein Folding
Liu, Y., Yang, Q., & Zhao, F. (2021) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-071320-112701 · Cited by 242 · see citing works
“For actively translated mRNAs, translation efficiency is mainly determined by the number of ribosomes loaded at the 5′ end of the mRNA, and translation initiation—rather than elongation—was previously thought to be the main ratelimiting step and primary determinant of translation efficiency (35, 40).”
BackgroundExosome biogenesis, secretion and function of exosomal miRNAs in skeletal muscle myogenesis
Yue, B., Yang, H., Wang, J., Ru, W.-X., Wu, J.-Y., Huang, Y.-Z., Lan, X., Lei, C., & Chen, H. (2020) · Cell Proliferation · doi:10.1111/cpr.12857 · Cited by 231 · see citing works
Kuhn, A. N., Diken, M., Kreiter, S., Selmi, A., Kowalska, J., Jemielity, J., Darzynkiewicz, E., Huber, C., Türeci, Ö., & Sahin, U. (2010) · Gene Therapy · doi:10.1038/gt.2010.52 · Cited by 226 · see citing works
The plasticity of mRNA translation during cancer progression and therapy resistance
Fabbri, L., Chakraborty, A., Robert, C., & Vagner, S. (2021) · Nature reviews. Cancer · doi:10.1038/s41568-021-00380-y · Cited by 273 · see citing works
Monga, A., Fulke, A. B., & Dasgupta, D. (2022) · Journal of Hazardous Materials Advances · doi:10.1016/j.hazadv.2022.100113 · Cited by 217 · see citing works
Shi, Z., & Barna, M. (2015) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev-cellbio-100814-125346 · Cited by 205 · see citing works
A stay of execution: ATF4 regulation and potential outcomes for the integrated stress response
Neill, G., & Masson, G. (2023) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2023.1112253 · Cited by 180 · see citing works
What turns CREB on? And off? And why does it matter?
Steven, A., Friedrich, M., Jank, P., Heimer, N., Budczies, J., Denkert, C., & Seliger, B. (2020) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-020-03525-8 · Cited by 214 · see citing works
RNA-binding Proteins in Regulating mRNA Stability and Translation: Roles and Mechanisms in Cancer
Li, W., Deng, X., & Chen, J.-J. (2022) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2022.03.025 · Cited by 168 · see citing works
Gregorio, D. D., Aguilar‐Valles, A., Preller, K. H., Heifets, B. D., Hibicke, M., Mitchell, J., & Gobbi, G. (2020) · Journal of Neuroscience · doi:10.1523/jneurosci.1659-20.2020 · Cited by 261 · see citing works
“…mTORC1 controls numerous neuronal functions, including nucleotide and lipid synthesis, glucose metabolism, autophagy, lysosome biogenesis, proteasome assembly, and 59 cap-dependent mRNA translation (also known as protein synthesis) (Sonenberg and Hinnebusch, 2009; Saxton and Sabatini, 2017).”
Mechanisms tailoring the expression of heat shock proteins to proteostasis challenges
Boopathy, L. R. A., Jacob‐Tomas, S., Alecki, C., & Vera, M. (2022) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2022.101796 · Cited by 178 · see citing works
“The eIF4F complex is made of the cap recognizing factor eIF4E, the scaffold protein eIF4G, and the ATP-driven RNA helicase eIF4A that unwinds secondary structures in the 50 untranslated region (UTR) of mRNAs (75, 93).”
BackgroundThe new function of circRNA: translation
Shi, Y., Jia, X., & Xu, J. (2020) · Clinical & Translational Oncology · doi:10.1007/s12094-020-02371-1 · Cited by 182 · see citing works
Yan, L. L., & Zaher, H. S. (2020) · Molecular Cell · doi:10.1016/j.molcel.2020.11.033 · Cited by 173 · see citing works
“Saccharomyces cerevisiae has only one eIF2α kinase, Gcn2, and the organism has proven to be an invaluable model for studying ISR (Masson, 2019), especially in response to aminoacid starvation (Sonenberg and Hinnebusch, 2009).”
BackgroundTranslational control via protein-regulated upstream open reading frames
Medenbach, J., Seiler, M., & Hentze, M. W. (2011) · Cell · doi:10.1016/j.cell.2011.05.005 · Cited by 140 · see citing works
Profiling SARS-CoV-2 HLA-I peptidome reveals T cell epitopes from out-of-frame ORFs
Weingarten-Gabbay, S., Klaeger, S., Sarkizova, S., Pearlman, L. R., Chen, D.-Y., Gallagher, K. M. E., Bauer, M. R., Taylor, H. B., Dunn, W. A., Tarr, C., et al. (2021) · Cell · doi:10.1016/j.cell.2021.05.046 · Cited by 147 · see citing works
“For example, viruses can attenuate translation of host proteins, downregulate proteasome machinery, and interfere with HLA-I expression (Hansen and Bouvier, 2009; Sonenberg and Hinnebusch, 2009).”
BackgroundAntidepressant actions of ketamine engage cell-specific translation via eIF4E
Aguilar-Valles, A., De Gregorio, D., Matta-Camacho, E., Eslamizade, M. J., Khlaifia, A., Skaleka, A., Lopez-Canul, M., Torres-Berrio, A., Bermudez, S., Rurak, G. M., et al. (2021) · Nature · doi:10.1038/s41586-020-03047-0 · Cited by 144 · see citing works
Self-citationChi, F., Sharpley, M. S., Nagaraj, R., Roy, S. S., & Banerjee, U. K. (2020) · Developmental Cell · doi:10.1016/j.devcel.2020.02.015 · Cited by 187 · see citing works
“A key phosphorylation target of mTOR is 4E-BP1, which enables CAP-dependent translation (Sonenberg and Hinnebusch, 2009).”
BackgroundChen, A. F., Parks, B., Kathiria, A. S., Ober-Reynolds, B., Goronzy, J. J., & Greenleaf, W. J. (2022) · Nature Methods · doi:10.1038/s41592-022-01461-y · Cited by 139 · see citing works
Small molecule cognitive enhancer reverses age-related memory decline in mice
Krukowski, K., Nolan, A., Frias, E. S., Boone, M., Ureta, G., Grue, K. A., Paladini, M. S., Elizarraras, E., Delgado, L. M., Bernales, S., et al. (2020) · eLife · doi:10.7554/elife.62048 · Cited by 161 · see citing works
Translational Control in the Brain in Health and Disease
Sossin, W. S., & Costa-Mattioli, M. (2019) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a032912 · Cited by 138 · see citing works
Regulation of PTEN translation by PI3K signaling maintains pathway homeostasis
Mukherjee, R., Vanaja, K. G., Boyer, J. A., Gadal, S., Solomon, H., Chandarlapaty, S., Levchenko, A., & Rosen, N. (2021) · Molecular Cell · doi:10.1016/j.molcel.2021.01.033 · Cited by 135 · see citing works
“Dephosphorylated 4E-BPs bind to eIF4E/5’capped-mRNA and, by doing so, interfere with the assembly of the pre-initiation complex (Gingras et al., 1999; Sonenberg and Hinnebusch, 2009).”
BackgroundG-Quadruplexes as pathogenic drivers in neurodegenerative disorders
Wang, E., Thombre, R., Shah, Y., Latanich, R., & Wang, J. (2021) · Nucleic Acids Research · doi:10.1093/nar/gkab164 · Cited by 148 · see citing works
“The roles that G4s play in the regulation of translation initiation are particularly important to elucidate because it is believed that most regulation of translation occurs at the initiation stage in eukaryotes (82).”
BackgroundClinical and immunological effects of mRNA vaccines in malignant diseases
Heine, A., Juranek, S., & Brossart, P. (2021) · Molecular Cancer · doi:10.1186/s12943-021-01339-1 · Cited by 185 · see citing works
Zu, T., Guo, S., Bardhi, O., Ryskamp, D. A., Li, J., Khoramian Tusi, S., Engelbrecht, A., Klippel, K., Chakrabarty, P., Nguyen, L., et al. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2005748117 · Cited by 133 · see citing works
Self-citationHypoxia Dictates Metabolic Rewiring of Tumors: Implications for Chemoresistance
Belisario, D. C., Kopecka, J., Pasino, M., Akman, M., De Smaele, E., Donadelli, M., & Riganti, C. (2020) · Cells · doi:10.3390/cells9122598 · Cited by 133 · see citing works
“Concurrently HIF-2α activates mTOR, a sensor of the cellular energy status and of the AA availability, and a stimulator of protein translation and cell proliferation [104].”
BackgroundInsight into antibacterial mechanism of polysaccharides: A review
Wang, Z., Sun, Q., Zhang, H., Wang, J.-Q., Fu, Q.-H., Qiao, H., & Wang, Q. (2021) · LWT · doi:10.1016/j.lwt.2021.111929 · Cited by 131 · see citing works
Nanoplatforms for mRNA Therapeutics
Meng, C., Chen, Z., Li, G., Welte, T., & Shen, H. (2021) · Advanced Therapeutics · doi:10.1002/adtp.202000099 · Cited by 130 · see citing works
Plant Immune Mechanisms: From Reductionistic to Holistic Points of View
Zhang, J., Coaker, G., Zhou, J., & Dong, X. (2020) · Molecular Plant · doi:10.1016/j.molp.2020.09.007 · Cited by 166 · see citing works
“As PABPs link the poly(A) tail of an mRNA to its 50 cap through interactions with eIF4G and eIF3 to facilitate translation initiation (Sonenberg and Hinnebusch, 2009; Jackson et al., 2010), it is plausible that the 50 R-motif serves as a capindependent translation enhancer (CITE) (Shatsky et al.”
BackgroundThe roles of arginases and arginine in immunity
Canè, S., Geiger, R., & Bronte, V. (2024) · Nature reviews. Immunology · doi:10.1038/s41577-024-01098-2 · Cited by 135 · see citing works
Kwon, N. H., Kang, T., Lee, J. Y., Kim, H. H., Kim, H. R., Hong, J., Oh, Y. S., Han, J. M., Ku, M. J., Lee, S. Y., et al. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1103922108 · Cited by 120 · see citing works
Amino Acid Sensing in Metabolic Homeostasis and Health.
Hu, X.-M., & Guo, F. (2020) · Endocrine reviews · doi:10.1210/endrev/bnaa026 · Cited by 123 · see citing works
Bond, P. (2016) · Journal of the International Society of Sports Nutrition · doi:10.1186/s12970-016-0118-y · Cited by 121 · see citing works
Clinical delivery of circular RNA: Lessons learned from RNA drug development
Young, T. L., Wang, K. C., Varley, A., & Li, B. (2023) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2023.114826 · Cited by 126 · see citing works
eIF4A supports an oncogenic translation program in pancreatic ductal adenocarcinoma
Chan, K., Robert, F., Oertlin, C., Kapeller-Libermann, D., Avizonis, D., Gutierrez, J., Handly-Santana, A., Doubrovin, M., Park, J., Schoepfer, C., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-13086-5 · Cited by 106 · see citing works
Millar, S. R., Huang, J. Q., Schreiber, K. J., Tsai, Y.-C., Won, J., Zhang, J., Moses, A. M., & Youn, J. (2023) · Chemical Reviews · doi:10.1021/acs.chemrev.2c00608 · Cited by 120 · see citing works
eIF2α controls memory consolidation via excitatory and somatostatin neurons
Sharma, V. K., Sood, R., Khlaifia, A., Eslamizade, M. J., Hung, T.-Y., Lou, D., Asgarihafshejani, A., Lalzar, M., Kiniry, S. J., Stokes, M. P., et al. (2020) · Nature · doi:10.1038/s41586-020-2805-8 · Cited by 137 · see citing works
Self-citationTransfer RNAs: diversity in form and function
Berg, M. D., & Brandl, C. J. (2020) · RNA Biology · doi:10.1080/15476286.2020.1809197 · Cited by 131 · see citing works
Revolutionizing immunization: a comprehensive review of mRNA vaccine technology and applications
Leong, K. Y., Tham, S. K., & Poh, C. L. (2025) · Virology Journal · doi:10.1186/s12985-025-02645-6 · Cited by 128 · see citing works
“The pairing of Met-tRNAi with the AUG codon signals the binding of the 60S ribosomal subunit, thus completing the assembly of the 80S ribosome, which is ready for protein synthesis [17].”
Branched chemically modified poly(A) tails enhance the translation capacity of mRNA
Chen, H., Liu, D., Guo, J., Aditham, A. J., Zhou, Y., Tian, J., Luo, S., Ren, J., Hsu, A., Huang, J., et al. (2024) · Nature Biotechnology · doi:10.1038/s41587-024-02174-7 · Cited by 129 · see citing works
tRNA overexpression rescues peripheral neuropathy caused by mutations in tRNA synthetase
Zuko, A., Mallik, M., Thompson, R., Spaulding, E., Wienand, A., Been, M., Tadenev, A., van Bakel, N., Sijlmans, C., Santos, L. A., et al. (2021) · Science · doi:10.1126/science.abb3356 · Cited by 111 · see citing works
An overview of rational design of mRNA-based therapeutics and vaccines
To, K. K. W., & Cho, W. C. S. (2021) · Expert Opinion on Drug Discovery · doi:10.1080/17460441.2021.1935859 · Cited by 110 · see citing works
eIF5B drives integrated stress response-dependent translation of PD-L1 in lung cancer
Suresh, S., Chen, B., Zhu, J., Golden, R. J., Lu, C., Evers, B. M., Novaresi, N., Smith, B., Zhan, X., Schmid, V., et al. (2020) · Nature Cancer · doi:10.1038/s43018-020-0056-0 · Cited by 126 · see citing works
Translation Regulation as a Therapeutic Target in Cancer
Grzmil, M., & Hemmings, B. A. (2012) · Cancer Research · doi:10.1158/0008-5472.can-12-0026 · Cited by 103 · see citing works
The ribotoxic stress response drives UV-mediated cell death
Sinha, N. K., McKenney, C. D., Yeow, Z. Y., Li, J. J., Nam, K. H., Yaron, T. M., Johnson, J. L., Huntsman, E. M., Cantley, L. C., Ordureau, A., et al. (2024) · Cell · doi:10.1016/j.cell.2024.05.018 · Cited by 142 · see citing works
The integrated stress response in metabolic adaptation
Ryoo, H. D. (2024) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2024.107151 · Cited by 120 · see citing works
“This initiates a sequence of mRNA regulatory mechanisms to induce the ISR, which has been reviewed extensively elsewhere (10, 33).”
BackgroundThe Target of Rapamycin Signalling Pathway in Ageing and Lifespan Regulation
Bjedov, I., & Rallis, C. (2020) · Genes · doi:10.3390/genes11091043 · Cited by 106 · see citing works
“An important feature of eIF4F complex, formed of eIF4E (cap binding), eIF4A (RNA helicase) and eIF4G (scaffolding protein), is its very low cellular concentration, which places it in a critical position to regulate translation [112].”
BackgroundProtein synthesis control in cancer: selectivity and therapeutic targeting
Kovalski, J. R., Kuzuoğlu‐Öztürk, D., & Ruggero, D. (2022) · The EMBO Journal · doi:10.15252/embj.2021109823 · Cited by 120 · see citing works
Yang, G., Smibert, C. A., Kaplan, D. R., & Miller, F. D. (2014) · Neuron · doi:10.1016/j.neuron.2014.10.022 · Cited by 98 · see citing works
Expanding uncapped translation and emerging function of circular RNA in carcinomas and noncarcinomas
Wang, Y., Wu, C., Du, Y., Li, Z., Li, M., Hou, P., Shen, Z., Chu, S., Zheng, J., & Bai, J. (2022) · Molecular Cancer · doi:10.1186/s12943-021-01484-7 · Cited by 112 · see citing works
“Canonical translation of eukaryotic mRNA depends on the m7G cap for recognition of the cap-binding protein initiation factor eIF4E complex, including eIF4E and eIF4G (a scaffold protein) and eIF4A (a helicase protein), and assembly of the 43S initiation complex to direct protein synthesis [42, 43].”
BackgroundmTORC1 promotes TOP mRNA translation through site-specific phosphorylation of LARP1
Jia, J.-J., Lahr, R. M., Solgaard, M. T., Moraes, B. J., Pointet, R., Yang, A.-D., Celucci, G., Graber, T. E., Hoang, H., Niklaus, M., et al. (2020) · Nucleic Acids Research · doi:10.1093/nar/gkaa1239 · Cited by 97 · see citing works
“4E-BPs (of which there are three homologs in mammals: 4E-BP1, 4EBP2 and 4E-BP3) and S6Ks (S6K1 and S6K2) are the most intensively studied direct mTORC1 substrates; accordingly, these targets are frequently referred to as the most important effectors of mTORC1 in mRNA translation (50).”
BackgroundEukaryotic translation initiation factors as promising targets in cancer therapy
Hao, P., Yu, J.-J., Ward, R., Liu, Y., Hao, Q., An, S., & Xu, T.-R. (2020) · Cell Communication and Signaling · doi:10.1186/s12964-020-00607-9 · Cited by 95 · see citing works
Determinants of genome-wide distribution and evolution of uORFs in eukaryotes
Zhang, H., Wang, Y., Wu, X., Tang, X., Wu, C., & Lü, J. (2021) · Nature Communications · doi:10.1038/s41467-021-21394-y · Cited by 100 · see citing works
Jeon, S., Jeon, Y., Lim, J.-Y., Kim, Y., Cha, B., & Kim, W. (2025) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-024-02070-1 · Cited by 97 · see citing works
Davies, N. M., Hovdal, D., Edmunds, N. J., Nordberg, P., Dahlén, A., Dabkowska, A. P., Arteta, M. Y., Rădulescu, A., Kjellman, T., Höijer, A., et al. (2021) · Molecular Therapy — Nucleic Acids · doi:10.1016/j.omtn.2021.03.008 · Cited by 88 · see citing works
mTOR-dependent translation amplifies microglia priming in aging mice
Keane, L., Antignano, I., Riechers, S., Zollinger, R., Dumas, A. A., Offermann, N., Bernis, M. E., Russ, J., Graelmann, F. J., McCormick, P. N., et al. (2020) · Journal of Clinical Investigation · doi:10.1172/jci132727 · Cited by 86 · see citing works
“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).”
Evaluating Efficiencies of Dual AAV Approaches for Retinal Targeting
Carvalho, L. S., Turunen, H. T., Wassmer, S. J., Luna-Velez, M. V., Xiao, R., Bennett, J., & Vandenberghe, L. H. (2017) · Frontiers in Neuroscience · doi:10.3389/fnins.2017.00503 · Cited by 86 · see citing works
The endoplasmic reticulum: Homeostasis and crosstalk in retinal health and disease
Zhang, S. X., Wang, J. J., Starr, C. R., Lee, E.-J., Park, K. S., Zhylkibayev, A. A., Medina, A., Lin, J. H., & Gorbatyuk, M. S. (2023) · Progress in Retinal and Eye Research · doi:10.1016/j.preteyeres.2023.101231 · Cited by 85 · see citing works
FMRP phosphorylation modulates neuronal translation through YTHDF1
Zou, Z.-Y., Jiangbo, W., Chen, Y.-T., Kang, Y., Shi, H., Yang, F., Shi, Z.-Y., Chen, S.-J., Zhou, Y., Sepich-Poore, C., et al. (2022) · bioRxiv · doi:10.1101/2022.11.29.518448 · Cited by 84
Insulin signaling regulates longevity through protein phosphorylation in Caenorhabditis elegans
Li, W.-J., Wang, C., Li, T., Yan, Y.-H., Zhang, M.-J., Liu, Z., Li, Y.-X., Zhao, H., Li, X.-M., He, X.-D., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-24816-z · Cited by 86 · see citing works
Activation of the integrated stress response by inhibitors of its kinases
Szaruga, M., Janssen, D. A., de Miguel, C., Hodgson, G., Fatalska, A., Pitera, A. P., Andreeva, A. E., & Bertolotti, A. (2023) · Nature Communications · doi:10.1038/s41467-023-40823-8 · Cited by 96 · see citing works
“The ISR is a central controller of cell and organismal fi tness elicited by phosphorylation of eIF2 α on serine 51, which results in attenuating bulk protein synthesis as well as reprograming gene expression to adapt to and survive challenges 1,2 .”
- 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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