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AU-Rich-Element-Mediated Upregulation of Translation by FXR1 and Argonaute 2
Open accessAbstract
AU-rich elements (AREs), present in mRNA 3'-UTRs, are potent posttranscriptional regulatory signals that can rapidly effect changes in mRNA stability and translation, thereby dramatically altering gene expression with clinical and developmental consequences. In human cell lines, the TNFalpha ARE enhances translation relative to mRNA levels upon serum starvation, which induces cell-cycle arrest. An in vivo crosslinking-coupled affinity purification method was developed to isolate ARE-associated complexes from activated versus basal translation conditions. We surprisingly found two microRNP-related proteins, fragile-X-mental-retardation-related protein 1 (FXR1) and Argonaute 2 (AGO2), that associate with the ARE exclusively during translation activation. Through tethering and shRNA-knockdown experiments, we provide direct evidence for the translation activation function of both FXR1 and AGO2 and demonstrate their interdependence for upregulation. This novel cell-growth-dependent translation activation role for FXR1 and AGO2 allows new insights into ARE-mediated signaling and connects two important posttranscriptional regulatory systems in an unexpected way.
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“In serum starved cells, AGO2 and another protein related to the miRNA-protein complex (microRNPs), Fragile-x-mental retardation related protein 1 (FXR1), were associated with AU-rich elements (AREs) at 3′ UTR to activate translation (55).”
From Overview of MicroRNA Biogenesis, Mechanisms of Actions, and Circulation (2018) · cites this paper as [55]
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Cites
Argonaute2 is the catalytic engine of mammalian RNAi
Liu, J., Carmell, M. A., Rivas, F. V., Marsden, C. G., Thomson, J. M., Song, J.-J., Hammond, S. M., Joshua-Tor, L., & Hannon, G. J. (2004) · Science · doi:10.1126/science.1102513 · Cited by 2,796
Control of translation and mRNA degradation by miRNAs and siRNAs: Table 1.
Valencia-Sanchez, M. A., Liu, J., Hannon, G. J., & Parker, R. (2006) · Genes & Development · doi:10.1101/gad.1399806 · Cited by 2,060
Human Argonaute2 mediates RNA cleavage targeted by miRNAs and siRNAs
Meister, G., Landthaler, M., Patkaniowska, A., Dorsett, Y., Teng, G., & Tuschl, T. (2004) · Molecular Cell · doi:10.1016/j.molcel.2004.07.007 · Cited by 2,052
Stress granules and processing bodies are dynamically linked sites of mRNP remodeling
Kedersha, N., Stoecklin, G., Ayodele, M. O., Yacono, P. W., Lykke‐Andersen, J., Fritzler, M. J., Scheuner, D. L., Kaufman, R. J., Golan, D. E., & Anderson, P. (2005) · The Journal of Cell Biology · doi:10.1083/jcb.200502088 · Cited by 1,494
Inhibition of Translational Initiation by Let-7 MicroRNA in Human Cells
Pillai, R. S., Bhattacharyya, S. N., Artus-Revel, C. G., Zoller, T., Cougot, N., Basyuk, E. I., Bertrand, É., & Filipowicz, W. (2005) · Science · doi:10.1126/science.1115079 · Cited by 1,489
Relief of microRNA-Mediated Translational Repression in Human Cells Subjected to Stress
Bhattacharyya, S. N., Habermacher, R., Martiné, U., Closs, E. I., & Filipowicz, W. (2006) · Cell · doi:10.1016/j.cell.2006.04.031 · Cited by 1,384
Impaired On/Off Regulation of TNF Biosynthesis in Mice Lacking TNF AU-Rich Elements
Kontoyiannis, D. L., Pasparakis, M., Pizarro, T. T., Cominelli, F., & Kollias, G. A. (1999) · Immunity · doi:10.1016/s1074-7613(00)80038-2 · Cited by 1,329
MicroRNA-dependent localization of targeted mRNAs to mammalian P-bodies
Liu, J., Valencia-Sanchez, M. A., Hannon, G. J., & Parker, R. (2005) · Nature Cell Biology · doi:10.1038/ncb1274 · Cited by 1,234
Feedback Inhibition of Macrophage Tumor Necrosis Factor-α Production by Tristetraprolin
Carballo, E., Lai, W. S., & Blackshear, P. J. (1998) · Science · doi:10.1126/science.281.5379.1001 · Cited by 1,162
Brennan, C. M., & Steitz*, J. A. (2001) · Cellular and Molecular Life Sciences · doi:10.1007/pl00000854 · Cited by 1,095
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Hale, B. J., Keating, A. F., Yang, C., & Ross, J. W. (2015) · Advances in experimental medicine and biology · doi:10.1007/978-3-319-18881-2_3 · Cited by 13
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Ling, H., Cao, C., Han, K., Lv, Y., Ma, X., Cao, J., Chen, J., Li, S., Lin, J., Fang, Y., et al. (2022) · Oncogene · doi:10.1038/s41388-022-02439-y · Cited by 13
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Song, X., Cheng, L., Zhou, T., Guo, X., Zhang, X., Chen, Y. P., Han, P., & Sha, J. (2011) · Computers in Biology and Medicine · doi:10.1016/j.compbiomed.2011.10.001 · Cited by 12
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Puerta, C. J., Sincero, T. C. M., Stoco, P. H., Cuervo, C., & Grisard, E. C. (2009) · Vector-Borne and Zoonotic Diseases · doi:10.1089/vbz.2008.0017 · Cited by 10
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Portal, M. M. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1014018108 · Cited by 9
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Tay, D. J. W., Lew, Z. Z. R., Chu, J. J. H., & Tan, K. S. (2022) · Frontiers in Microbiology · doi:10.3389/fmicb.2022.844447 · Cited by 9
Qian, J., Zou, Y., Wang, J., Zhang, B., & Massion, P. P. (2015) · Genomics Data · doi:10.1016/j.gdata.2015.06.014 · Cited by 9
Granata, S., Santoro, G., Masola, V., Tomei, P., Sallustio, F., Pontrelli, P., Accetturo, M., Antonucci, N., Carratù, P., Lupo, A., et al. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19041250 · Cited by 9
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Ghosh, C., Uppala, J. K., Sathe, L., Hammond, C. I., Anshu, A., Pokkuluri, P. R., Turk, B. E., & Dey, M. (2021) · Science Signaling · doi:10.1126/scisignal.aaz4401 · Cited by 9
Roy, N., Sundar, S., Pillai, M. S., Patell-Socha, F., Ganesh, S., Aloysius, A., Rumman, M., Gala, H., Hughes, S. M., Zammit, P. S., et al. (2021) · Skeletal Muscle · doi:10.1186/s13395-021-00270-9 · Cited by 9
Yang, Y., Zhao, J., Li, Y., Li, X., Chen, X., & Feng, Z. (2021) · Journal of Neurochemistry · doi:10.1111/jnc.15485 · Cited by 9
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ARiBo pull-down for riboproteomic studies based on label-free quantitative mass spectrometry
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Girella, A., Vismara, M. E. M., O’Riordan, K. J., Gunnigle, E., Mercante, F., Girone, N., Pucci, M., Gatta, V., Konstantinidou, F., Stuppia, L., et al. (2025) · Pharmacological Research · doi:10.1016/j.phrs.2025.107891 · Cited by 8
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Kwofie, K. D., Hernandez, E. P., Anisuzzaman, A., Kawada, H., Koike, Y., Sasaki, S., Inoue, T., Jimbo, K., Mikami, F., Ladzekpo, D., et al. (2023) · Scientific Reports · doi:10.1038/s41598-023-36523-4 · Cited by 7
Systematic integration of molecular and clinical approaches in HCV-induced hepatocellular carcinoma
Shabangu, C. S., Su, W.-H., Li, C., Yu, M., Dai, C., Huang, J., Chuang, W., & Wang, S. (2024) · Journal of Translational Medicine · doi:10.1186/s12967-024-04925-1 · Cited by 7
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Nichols, R. C., Botson, J. K., Wang, X. W., Hamilton, B. J., Collins, J. E., Uribe, V., Brooks, S. A., Zan, M., & Rigby, W. F. C. (2010) · Molecular Biotechnology · doi:10.1007/s12033-010-9360-8 · Cited by 7
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Ghosh, U., & Adhya, S. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.696377 · Cited by 6
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Bhaskar, V., Jia, M. Z., & Chao, J. A. (2020) · Methods in molecular biology · doi:10.1007/978-1-0716-0712-1_16 · Cited by 6
Pull-down of biotinylated RNA and protein
Uppala, J. K., Ghosh, C., Sabat, G., & Dey, M. (2022) · BIO-PROTOCOL · doi:10.21769/bioprotoc.4331 · Cited by 6
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Velizhanina, M. E., & Galkin, A. P. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23147997 · Cited by 6
Lin, Y., Su, C.-H., Chen, H.-M., Wu, M.-S., Pan, H., Chang, C.-N., Cheng, Y., Chang, W., Chiu, C., & Teng, Y. (2024) · Aging · doi:10.18632/aging.205571 · Cited by 6
Mols, J., BERG, A., Otsuka, M., ZHENG, M., CHEN, J., & Han, J. (2008) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2008.03.007 · Cited by 6
Flather, D. P., Cathcart, A. L., Cruz, C., Baggs, E., Ngo, T., Gershon, P. D., & Semler, B. L. (2016) · Viruses · doi:10.3390/v8020039 · Cited by 6
Edwards, M. M., & Joseph, S. (2021) · Journal of Molecular Biology · doi:10.1016/j.jmb.2021.167396 · Cited by 7
Bukhari, S. I. A., Truesdell, S. S., & Vasudevan, S. (2017) · Methods in molecular biology · doi:10.1007/978-1-4939-7371-2_18 · Cited by 7
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Shikha, S., Kumar, U., Sarkhel, S., & Kumari, M. (2025) · Plant Pathology · doi:10.1111/ppa.70053 · Cited by 5
Metadata
- Authors
- Vasudevan, S., & Steitz, J. A.
- Affiliations
- Howard Hughes Medical Institute (US)
- Corresponding author
- Steitz, Joan A.
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2007-03
- Volume
- 128
- Issue
- 6
- Pages
- 1105-1118
- ISSN
- 0092-8674 (ISSN-L)
- PMC
- PMC3430382
- OpenAlex
- W2010763857
- Cited by
- 656
- References
- 66
- Citations by year
- 2026: 10 · 2025: 24 · 2024: 25 · 2023: 25 · 2022: 31 · 2021: 38 · 2020: 31 · 2019: 26 · 2018: 21 · 2017: 13 · 2016: 39 · 2015: 32 · 2014: 34 · 2013: 48 · 2012: 43
- FWCI
- 21.61
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Cell (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institutes of Health
- National Institute of General Medical Sciences (GM26154, R01GM026154)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA Research and Splicing
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA Interference and Gene Delivery
- Keywords
- AU-rich elements, FXR1, Argonaute 2, translation activation, post-transcriptional regulation, mRNA 3' UTR, microRNA-induced silencing complex, TNF-α, serum deprivation, cell cycle arrest, protein-protein interaction, cell growth
- MeSH terms
- Cell Cycle, Cell Line, Chromatography, Affinity, Humans, Monocytes, Peptide Initiation Factors, Polyribosomes, Ribonucleoproteins, Protein Biosynthesis, Tumor Necrosis Factor-alpha, Eukaryotic Initiation Factor-2, Up-Regulation, RNA-Binding Proteins, Culture Media, Serum-Free, Genes, Reporter, 3' Untranslated Regions, Regulatory Sequences, Ribonucleic Acid, Serum, Luciferases, Firefly, Argonaute Proteins
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