P-body formation is a consequence, not the cause, of RNA-mediated gene silencing
Open accessAbstract
P bodies are cytoplasmic domains that contain proteins involved in diverse posttranscriptional processes, such as mRNA degradation, nonsense-mediated mRNA decay (NMD), translational repression, and RNA-mediated gene silencing. The localization of these proteins and their targets in P bodies raises the question of whether their spatial concentration in discrete cytoplasmic domains is required for posttranscriptional gene regulation. We show that processes such as mRNA decay, NMD, and RNA-mediated gene silencing are functional in cells lacking detectable microscopic P bodies. Although P bodies are not required for silencing, blocking small interfering RNA or microRNA silencing pathways at any step prevents P-body formation, indicating that P bodies arise as a consequence of silencing. Consistently, we show that releasing mRNAs from polysomes is insufficient to trigger P-body assembly: polysome-free mRNAs must enter silencing and/or decapping pathways to nucleate P bodies. Thus, even though P-body components play crucial roles in mRNA silencing and decay, aggregation into P bodies is not required for function but is instead a consequence of their activity.
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
P-bodies form in an RNA-dependent manner as a consequence of RNAi and RNA degradation.
“Furthermore, P-bodies form in an RNA-dependent manner as a consequence of RNAi and RNA degradation (80).”
From Overview of MicroRNA Biogenesis, Mechanisms of Actions, and Circulation (2018) · cites this paper as [80]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
Mechanisms of gene silencing by double-stranded RNA
Meister, G., & Tuschl, T. (2004) · Nature · doi:10.1038/nature02873 · Cited by 2,539 · see citing works
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 · see citing works
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 1,431 · see citing works
Decapping and Decay of Messenger RNA Occur in Cytoplasmic Processing Bodies
Sheth, U., & Parker, R. (2003) · Science · doi:10.1126/science.1082320 · Cited by 1,372 · see citing works
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 1,332 · see citing works
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 · see citing works
Behm‐Ansmant, I., Rehwinkel, J., Doerks, T., Stark, A., Bork, P., & Izaurralde, E. (2006) · Genes & Development · doi:10.1101/gad.1424106 · Cited by 1,030 · see citing works
Anderson, P., & Kedersha, N. (2006) · The Journal of Cell Biology · doi:10.1083/jcb.200512082 · Cited by 984 · see citing works
P bodies: at the crossroads of post-transcriptional pathways
Eulálio, A., Behm‐Ansmant, I., & Izaurralde, E. (2006) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2080 · Cited by 939 · see citing works
Distinct roles for Argonaute proteins in small RNA-directed RNA cleavage pathwaysPreprint
岡村, 勝., Ishizuka, A., Siomi, H., & Siomi, M. C. (2004) · Genes & Development · doi:10.1101/gad.1210204 · Cited by 833 · see citing works
The enzymes and control of eukaryotic mRNA turnover
Parker, R., & Song, H. (2004) · Nature Structural & Molecular Biology · doi:10.1038/nsmb724 · Cited by 813 · see citing works
Movement of Eukaryotic mRNAs Between Polysomes and Cytoplasmic Processing Bodies
Brengues, M., Teixeira, D., & Parker, R. (2005) · Science · doi:10.1126/science.1115791 · Cited by 796 · see citing works
Processing bodies require RNA for assembly and contain nontranslating mRNAs
Teixeira, D., Sheth, U., Valencia-Sanchez, M. A., Brengues, M., & Parker, R. (2005) · RNA · doi:10.1261/rna.7258505 · Cited by 728 · see citing works
A role for the P-body component GW182 in microRNA function
Liu, J., Rivas, F. V., Wohlschlegel, J. A., Yates, J. R., Parker, R., & Hannon, G. J. (2005) · Nature Cell Biology · doi:10.1038/ncb1333 · Cited by 680 · see citing works
Cytoplasmic foci are sites of mRNA decay in human cells
Cougot, N., Babajko, S., & Séraphin, B. (2004) · The Journal of Cell Biology · doi:10.1083/jcb.200309008 · Cited by 647 · see citing works
RNA-quality control by the exosome
Houseley, J. M., LaCava, J., & Tollervey, D. W. (2006) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1964 · Cited by 645 · see citing works
Argonaute 2/RISC resides in sites of mammalian mRNA decay known as cytoplasmic bodies
Sen, G. L., & Blau, H. M. (2005) · Nature Cell Biology · doi:10.1038/ncb1265 · Cited by 645 · see citing works
General Translational Repression by Activators of mRNA Decapping
Coller, J. M., & Parker, R. (2005) · Cell · doi:10.1016/j.cell.2005.07.012 · Cited by 629 · see citing works
Identification of Novel Argonaute-Associated Proteins
Meister, G., Landthaler, M., Peters, L., Chen, P., Urlaub, H., Lührmann, R., & Tuschl, T. (2005) · Current Biology · doi:10.1016/j.cub.2005.10.048 · Cited by 554 · see citing works
Translation Repression in Human Cells by MicroRNA-Induced Gene Silencing Requires RCK/p54
Chu, C., & Rana, T. M. (2006) · PLoS Biology · doi:10.1371/journal.pbio.0040210 · Cited by 521 · see citing works
Disruption of GW bodies impairs mammalian RNA interference
Jakymiw, A., Lian, S., Eystathioy, T., Li, S., Satoh, M., Hamel, J. C., Fritzler, M. J., & Chan, E. K. L. (2005) · Nature Cell Biology · doi:10.1038/ncb1334 · Cited by 496 · see citing works
Human Dcp2: a catalytically active mRNA decapping enzyme located in specific cytoplasmic structures
van Dijk, E., Cougot, N., Meyer, S., Babajko, S., Wahle, E., & Séraphin, B. (2002) · The EMBO Journal · doi:10.1093/emboj/cdf678 · Cited by 495 · see citing works
A crucial role for GW182 and the DCP1:DCP2 decapping complex in miRNA-mediated gene silencing
Rehwinkel, J., Behm‐Ansmant, I., Gatfield, D., & Izaurralde, E. (2005) · RNA · doi:10.1261/rna.2191905 · Cited by 493 · see citing works
Lykke‐Andersen, J., & Wagner, E. (2005) · Genes & Development · doi:10.1101/gad.1282305 · Cited by 482 · see citing works
Nonsense-mediated mRNA decay: molecular insights and mechanistic variations across species
Conti, E., & Izaurralde, E. (2005) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2005.04.005 · Cited by 479 · see citing works
Multiple Processing Body Factors and the ARE Binding Protein TTP Activate mRNA Decapping
Fenger-Grøn, M., Fillman, C. L., Norrild, B., & Lykke‐Andersen, J. (2005) · Molecular Cell · doi:10.1016/j.molcel.2005.10.031 · Cited by 459 · see citing works
Dissociation of Mammalian Polyribosomes into Subunits by Puromycin
Blobel, G., & Sabatini, D. M. (1971) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.68.2.390 · Cited by 440 · see citing works
Yeast Sm-like proteins function in mRNA decapping and decay
Tharun, S., He, W., Mayes, A. E., Lennertz, P., Beggs, J. D., & Parker, R. (2000) · Nature · doi:10.1038/35006676 · Cited by 433 · see citing works
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
A role for eIF4E and eIF4E-transporter in targeting mRNPs to mammalian processing bodies
Andrei, M. A., Ingelfinger, D., Heintzmann, R., Achsel, T., Rivera-Pomar, R. V., & Lührmann, R. (2005) · RNA · doi:10.1261/rna.2340405 · Cited by 406 · see citing works
Ingelfinger, D., Arndt‐Jovin, D. J., Lührmann, R., & Achsel, T. (2002) · RNA · doi:10.1017/s1355838202021726 · Cited by 404 · see citing works
A Sm‐like protein complex that participates in mRNA degradation
Bouveret, E., Rigaut, G., Shevchenko, A., Wilm, M., & Séraphin, B. (2000) · The EMBO Journal · doi:10.1093/emboj/19.7.1661 · Cited by 395 · see citing works
Eystathioy, T., Chan, E. K. L., Tenenbaum, S. A., Keene, J. D., Griffith, K. J., & Fritzler, M. J. (2002) · Molecular Biology of the Cell · doi:10.1091/mbc.01-11-0544 · Cited by 363 · see citing works
Barbee, S. A., Estes, P. S., Cziko, A.-M., Hillebrand, J., Luedeman, R. A., Coller, J. M., Johnson, N., Howlett, I. C., Geng, C., Ueda, R., et al. (2006) · Neuron · doi:10.1016/j.neuron.2006.10.028 · Cited by 359 · see citing works
Decay of mRNAs targeted by RISC requires XRN1, the Ski complex, and the exosome
Orbán, T. I., & Izaurralde, E. (2005) · RNA · doi:10.1261/rna.7231505 · Cited by 356 · see citing works
SMG7 Acts as a Molecular Link between mRNA Surveillance and mRNA Decay
Unterholzner, L., & Izaurralde, E. (2004) · Molecular Cell · doi:10.1016/j.molcel.2004.10.013 · Cited by 309 · see citing works
The translational regulator CPEB1 provides a link between dcp1 bodies and stress granules
Wilczynska, A., Aigueperse, C., Kress, M., Dautry, F., & Barbieri-Weill, D. (2005) · Journal of Cell Science · doi:10.1242/jcs.01692 · Cited by 302 · see citing works
Targeting of Aberrant mRNAs to Cytoplasmic Processing Bodies
Sheth, U., & Parker, R. (2006) · Cell · doi:10.1016/j.cell.2006.04.037 · Cited by 292 · see citing works
Bringing the role of mRNA decay in the control of gene expression into focus
Wilusz, C. J., & Wilusz, J. (2004) · Trends in Genetics · doi:10.1016/j.tig.2004.07.011 · Cited by 268 · see citing works
Eystathioy, T., Jakymiw, A., Chan, E. K. L., Séraphin, B., Cougot, N., & Fritzler, M. J. (2003) · RNA · doi:10.1261/rna.5810203 · Cited by 267 · see citing works
Nonsense-mediated messenger RNA decay is initiated by endonucleolytic cleavage in Drosophila
Gatfield, D., & Izaurralde, E. (2004) · Nature · doi:10.1038/nature02559 · Cited by 255 · see citing works
A role for the eIF4E-binding protein 4E-T in P-body formation and mRNA decay
Ferraiuolo, M. A., Basak, S., Dostie, J., Murray, E. L., Schoenberg, D. R., & Sonenberg, N. (2005) · The Journal of Cell Biology · doi:10.1083/jcb.200504039 · Cited by 255 · see citing works
SMG7 Is a 14-3-3-like Adaptor in the Nonsense-Mediated mRNA Decay Pathway
Fukuhara, N., Ebert, J., Unterholzner, L., Lindner, D., Izaurralde, E., & Conti, E. (2005) · Molecular Cell · doi:10.1016/j.molcel.2005.01.010 · Cited by 242 · see citing works
Targeting an mRNA for Decapping
Tharun, S., & Parker, R. (2001) · Molecular Cell · doi:10.1016/s1097-2765(01)00395-1 · Cited by 238 · see citing works
ARE‐mRNA degradation requires the 5′–3′ decay pathway
Stoecklin, G., Mayo, T., & Anderson, P. (2005) · EMBO Reports · doi:10.1038/sj.embor.7400572 · Cited by 237 · see citing works
Zaessinger, S., Busseau, I., & Simonelig, M. (2006) · Development · doi:10.1242/dev.02649 · Cited by 212 · see citing works
A complex containing the CCR4 and CAF1 proteins is involved in mRNA deadenylation in Drosophila
Temme, C., Zaessinger, S., Meyer, S., Simonelig, M., & Wahle, E. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600273 · Cited by 212 · see citing works
Yang, Z., Jakymiw, A., Wood, M. R., Eystathioy, T., Rubin, R. L., Fritzler, M. J., & Chan, E. K. L. (2004) · Journal of Cell Science · doi:10.1242/jcs.01477 · Cited by 208 · see citing works
Human Retroviral Host Restriction Factors APOBEC3G and APOBEC3F Localize to mRNA Processing Bodies
Wichroski, M. J., Robb, G. B., & Rana, T. M. (2006) · PLoS Pathogens · doi:10.1371/journal.ppat.0020041 · Cited by 199 · see citing works
Ge-1 is a central component of the mammalian cytoplasmic mRNA processing body
YU, J. H., Yang, W.-H., Gulick, T., Bloch, K. D., & Bloch, D. B. (2005) · RNA · doi:10.1261/rna.2142405 · Cited by 199 · see citing works
RNA-associated protein 55 (RAP55) localizes to mRNA processing bodies and stress granules
Yang, W.-H., YU, J. H., Gulick, T., Bloch, K. D., & Bloch, D. B. (2006) · RNA · doi:10.1261/rna.2302706 · Cited by 172 · see citing works
Wilhelm, J. E., Buszczak, M., & Sayles, S. (2005) · Developmental Cell · doi:10.1016/j.devcel.2005.09.015 · Cited by 166 · see citing works
Identification of Edc3p as an Enhancer of mRNA Decapping inSaccharomyces cerevisiae
Kshirsagar, M., & Parker, R. (2004) · Genetics · doi:10.1534/genetics.166.2.729 · Cited by 150 · see citing works
Bonnerot, C., Boeck, R., & Lapeyre, B. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.16.5939-5946.2000 · Cited by 138 · see citing works
Genome-Wide Analysis of mRNAs Regulated by Drosha and Argonaute Proteins in Drosophila melanogaster
Rehwinkel, J., Natalin, P., Stark, A., Brennecke, J., Cohen, S. M., & Izaurralde, E. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.26.8.2965-2975.2006 · Cited by 138 · see citing works
Formation of GW bodies is a consequence of microRNA genesis
Pauley, K. M., Eystathioy, T., Jakymiw, A., Hamel, J. C., Fritzler, M. J., & Chan, E. K. L. (2006) · EMBO Reports · doi:10.1038/sj.embor.7400783 · Cited by 124 · see citing works
RAP55, a Cytoplasmic mRNP Component, Represses Translation in Xenopus Oocytes
Tanaka, K. J., Ogawa, K., Takagi, M., Imamoto, N., Matsumoto, K., & Tsujimoto, M. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m609059200 · Cited by 113 · see citing works
Virus-like particles of the Ty3 retrotransposon assemble in association with P-body components
Beliakova‐Bethell, N., Beckham, C. J., Giddings, T. H., Winey, M., Parker, R., & Sandmeyer, S. B. (2005) · RNA · doi:10.1261/rna.2264806 · Cited by 99 · see citing works
Novel Sm‐like proteins with long C‐terminal tails and associated methyltransferases
Albrecht, M., & Lengauer, T. (2004) · FEBS Letters · doi:10.1016/j.febslet.2004.03.126 · Cited by 92 · see citing works
Anantharaman, V., & Aravind, L. (2004) · BMC Genomics · doi:10.1186/1471-2164-5-45 · Cited by 79 · see citing works
Overlapping Functions of Argonaute Proteins in Patterning and Morphogenesis of Drosophila Embryos
Meyer, W., Schreiber, S., Guo, Y., Volkmann, T. E., Welte, M. A., & Müller, H. ‐. J. (2006) · PLoS Genetics · doi:10.1371/journal.pgen.0020134 · Cited by 62 · see citing works
Identification of Edc3p as an Enhancer of mRNA Decapping in Saccharomyces cerevisiae
Kshirsagar, M., & Parker, R. (2004) · Genetics · doi:10.1093/genetics/166.2.729 · Cited by 22 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
Overview of MicroRNA Biogenesis, Mechanisms of Actions, and Circulation
O'Brien, J., Hayder, H., Zayed, Y., & Peng, C. (2018) · Frontiers in Endocrinology · doi:10.3389/fendo.2018.00402 · Cited by 5,287 · see citing works
Origins and Mechanisms of miRNAs and siRNAs
Carthew, R. W., & Sontheimer, E. J. (2009) · Cell · doi:10.1016/j.cell.2009.01.035 · Cited by 5,023 · see citing works
The widespread regulation of microRNA biogenesis, function and decay
Krol, J., Loedige, I., & Filipowicz, W. (2010) · Nature Reviews Genetics · doi:10.1038/nrg2843 · Cited by 4,672 · see citing works
(2008) · doi:10.1038/nrg2290 · Cited by 5,199 · see citing works
Regulation of mRNA Translation and Stability by microRNAs
Fabian, M. R., Sonenberg, N., & Filipowicz, W. (2010) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060308-103103 · Cited by 3,214 · see citing works
MicroRNA biogenesis pathways in cancer
Lin, S., & Gregory, R. I. (2015) · Nature reviews. Cancer · doi:10.1038/nrc3932 · Cited by 2,117 · see citing works
Towards a molecular understanding of microRNA-mediated gene silencing
Jonas, S., & Izaurralde, E. (2015) · Nature Reviews Genetics · doi:10.1038/nrg3965 · Cited by 1,872 · see citing works
Lee, Y. S., & Dutta, A. (2008) · Annual Review of Pathology Mechanisms of Disease · doi:10.1146/annurev.pathol.4.110807.092222 · Cited by 1,511 · see citing works
Getting to the Root of miRNA-Mediated Gene Silencing
Eulálio, A., Huntzinger, E., & Izaurralde, E. (2008) · Cell · doi:10.1016/j.cell.2007.12.024 · Cited by 1,071 · see citing works
A framework for understanding the functions of biomolecular condensates across scales
Lyon, A. S., Peeples, W. B., & Rosen, M. K. (2021) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-020-00303-z · Cited by 895 · see citing works
Biogenesis, Turnover, and Mode of Action of Plant MicroRNAs
Rogers, K. M., & Chen, X. (2013) · The Plant Cell · doi:10.1105/tpc.113.113159 · Cited by 938 · see citing works
RNA granules: post-transcriptional and epigenetic modulators of gene expression
Anderson, P., & Kedersha, N. (2009) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2694 · Cited by 866 · see citing works
Quality and quantity control of gene expression by nonsense-mediated mRNA decay
Kurosaki, T., Popp, M. W., & Maquat, L. E. (2019) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-019-0126-2 · Cited by 834 · see citing works
P-Bodies and Stress Granules: Possible Roles in the Control of Translation and mRNA DegradationPreprint
Decker, C. J., & Parker, R. (2012) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a012286 · Cited by 806 · see citing works
P-Body Purification Reveals the Condensation of Repressed mRNA Regulons
Hubstenberger, A., Courel, M., Bénard, M., Souquère, S., Ernoult‐Lange, M., Chouaib, R., Zhou, Y., Morlot, J.-B., Munier, A., Fradet, M., et al. (2017) · Molecular Cell · doi:10.1016/j.molcel.2017.09.003 · Cited by 793 · see citing works
RNA contributions to the form and function of biomolecular condensates
Roden, C., & Gladfelter, A. S. (2020) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-020-0264-6 · Cited by 638 · see citing works
Mechanisms of miRNA-mediated post-transcriptional regulation in animal cells
Chekulaeva, M., & Filipowicz, W. (2009) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2009.04.009 · Cited by 595 · see citing works
P-bodies: Composition, properties and functions
Luo, Y., Na, Z., & Slavoff, S. (2018) · Biochemistry · doi:10.1021/acs.biochem.7b01162 · Cited by 538 · see citing works
MicroRNA regulation by RNA-binding proteins and its implications for cancer
van Kouwenhove, M., Kedde, M., & Agami, R. (2011) · Nature Reviews Cancer · doi:10.1038/nrc3107 · Cited by 617 · see citing works
Höck, J., & Meister, G. (2008) · Genome biology · doi:10.1186/gb-2008-9-2-210 · Cited by 557 · see citing works
Posttranscriptional Upregulation by MicroRNAs
Vasudevan, S. (2011) · Wiley Interdisciplinary Reviews - RNA · doi:10.1002/wrna.121 · Cited by 512 · see citing works
A guide to membraneless organelles and their various roles in gene regulation
Hirose, T., Ninomiya, K., Nakagawa, S., & Yamazaki, T. (2022) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-022-00558-8 · Cited by 496 · see citing works
Stress Granules and Processing Bodies in Translational ControlPreprint
Ivanov, P. V., Kedersha, N., & Anderson, P. (2018) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a032813 · Cited by 501 · see citing works
Decker, C. J., Teixeira, D., & Parker, R. (2007) · The Journal of Cell Biology · doi:10.1083/jcb.200704147 · Cited by 468 · see citing works
Buchan, J. R. (2014) · RNA Biology · doi:10.4161/15476286.2014.972208 · Cited by 459 · see citing works
Messenger RNA regulation: to translate or to degrade
Shyu, A., Wilkinson, M., & van Hoof, A. (2008) · The EMBO Journal · doi:10.1038/sj.emboj.7601977 · Cited by 447 · see citing works
Ohn, T., Kedersha, N., Hickman, T. T., Tisdale, S., & Anderson, P. (2008) · Nature Cell Biology · doi:10.1038/ncb1783 · Cited by 414 · see citing works
Let Me Count the Ways: Mechanisms of Gene Regulation by miRNAs and siRNAs
Wu, L., & Belasco, J. G. (2008) · Molecular Cell · doi:10.1016/j.molcel.2007.12.010 · Cited by 409 · see citing works
Stress granules, P-bodies and cancer
Anderson, P., Kedersha, N., & Ivanov, P. V. (2014) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2014.11.009 · Cited by 396 · see citing works
The roles of microRNA in cancer and apoptosis
Lynam‐Lennon, N., Maher, S. G., & Reynolds, J. V. (2008) · Biological reviews/Biological reviews of the Cambridge Philosophical Society · doi:10.1111/j.1469-185x.2008.00061.x · Cited by 408 · see citing works
How do microRNAs regulate gene expression?
Cannell, I. G., Kong, Y. W., & Bushell, M. (2008) · Biochemical Society Transactions · doi:10.1042/bst0361224 · Cited by 407 · see citing works
The Control of mRNA Decapping and P-Body Formation
Franks, T. M., & Lykke‐Andersen, J. (2008) · Molecular Cell · doi:10.1016/j.molcel.2008.11.001 · Cited by 399 · see citing works
Brooks, S. A., & Blackshear, P. J. (2013) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2013.02.003 · Cited by 392 · see citing works
Polysomes, P bodies and stress granules: states and fates of eukaryotic mRNAs
Balagopal, V., & Parker, R. (2009) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2009.03.005 · Cited by 391 · see citing works
Organizing Principles of Mammalian Nonsense-Mediated mRNA Decay
Popp, M. W., & Maquat, L. E. (2013) · Annual Review of Genetics · doi:10.1146/annurev-genet-111212-133424 · Cited by 371 · see citing works
XRN 5′→3′ exoribonucleases: Structure, mechanisms and functions
Nagarajan, V. K., Jones, C. I., Newbury, S. F., & Green, P. J. (2013) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2013.03.005 · Cited by 366 · 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
Ketting, R. F. (2011) · Developmental Cell · doi:10.1016/j.devcel.2011.01.012 · Cited by 341 · see citing works
Nicholson, P., Yepiskoposyan, H., Metze, S., Orozco, R. Z., Kleinschmidt, N., & Mühlemann, O. (2009) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-009-0177-1 · Cited by 336 · see citing works
Proteomic and functional analysis of Argonaute-containing mRNA-protein complexes in human cells
Höck, J., Weinmann, L., Ender, C., Rüdel, S., Kremmer, E., Raabe, M., Urlaub, H., & Meister, G. (2007) · The EMBO Reports · doi:10.1038/sj.embor.7401088 · Cited by 310 · see citing works
Co-translational mRNA decay in Saccharomyces cerevisiae
Hu, W., Sweet, T. J., Chamnongpol, S., Baker, K. E., & Coller, J. M. (2009) · Nature · doi:10.1038/nature08265 · Cited by 334 · see citing works
Biogenesis and regulation of the let-7 miRNAs and their functional implications
Lee, H., Han, S., Kwon, C. S., & Lee, D. (2015) · Protein & Cell · doi:10.1007/s13238-015-0212-y · Cited by 329 · see citing works
RISC assembly: Coordination between small RNAs and Argonaute proteins
Kobayashi, H., & Tomari, Y. (2015) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2015.08.007 · Cited by 306 · see citing works
A human microprotein that interacts with the mRNA decapping complex
D’Lima, N. G., Ma, J., Winkler, L., Chu, Q., Loh, K. H., Corpuz, E. O., Budnik, B., Lykke‐Andersen, J., Saghatelian, A., & Slavoff, S. A. (2016) · Nature Chemical Biology · doi:10.1038/nchembio.2249 · Cited by 302 · see citing works
Noncoding Flavivirus RNA Displays RNA Interference Suppressor Activity in Insect and Mammalian Cells
Schnettler, E., Sterken, M. G., Leung, J. Y., Metz, S., Geertsema, C., Goldbach, R. W., Vlak, J. M., Kohl, A., Khromykh, A. A., & Pijlman, G. P. (2012) · Journal of Virology · doi:10.1128/jvi.01104-12 · Cited by 299 · see citing works
Target-specific requirements for enhancers of decapping in miRNA-mediated gene silencingPreprint
Eulálio, A., Rehwinkel, J., Stricker, M., Huntzinger, E., Yang, S.-F., Doerks, T., Dorner, S., Peer Bork, B., Boutros, M., & Izaurralde, E. (2007) · Genes & Development · doi:10.1101/gad.443107 · Cited by 297 · see citing works
Emerging Role of MicroRNAs in Cardiovascular Biology
Latronico, M. V. G., Catalucci, D., & Condorelli, G. (2007) · Circulation Research · doi:10.1161/circresaha.107.163147 · Cited by 283 · see citing works
Functional aspects of animal microRNAs
Williams, A. E. (2007) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-007-7355-9 · Cited by 281 · see citing works
Olivieri, D., Sykora, M. M., Sachidanandam, R., Mechtler, K., & Brennecke, J. (2010) · The EMBO Journal · doi:10.1038/emboj.2010.212 · Cited by 268 · see citing works
Control of protein synthesis and mRNA degradation by microRNAs
Liu, J. (2008) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2008.01.006 · Cited by 264 · see citing works
RNA granules: The good, the bad and the ugly
Thomas, M. G., Loschi, M., Desbats, M. A., & Boccaccio, G. L. (2010) · Cellular Signalling · doi:10.1016/j.cellsig.2010.08.011 · Cited by 262 · see citing works
Intracellular and extracellular microRNA: An update on localization and biological role
Makarova, J. A., Shkurnikov, M. Y., Wicklein, D., Lange, T., Samatov, T. R., Turchinovich, A. A., & Tonevitsky, A. (2016) · Progress in Histochemistry and Cytochemistry · doi:10.1016/j.proghi.2016.06.001 · Cited by 260 · see citing works
Phase Transitions in the Assembly and Function of Human miRISC
Sheu‐Gruttadauria, J., & MacRae, I. J. (2018) · Cell · doi:10.1016/j.cell.2018.02.051 · Cited by 258 · see citing works
P-Bodies: Cytosolic Droplets for Coordinated mRNA Storage.
Standart, N., & Weil, D. (2018) · Trends in Genetics · doi:10.1016/j.tig.2018.05.005 · Cited by 231 · see citing works
Emerging Roles of Disordered Sequences in RNA-Binding Proteins
Calabretta, S., & Richard, S. (2015) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2015.08.012 · Cited by 240 · see citing works
The Dynamics of mRNA Turnover Revealed by Single-Molecule Imaging in Single Cells
Horvathova, I., Voigt, F., Kotrys, A. V., Zhan, Y., Artus-Revel, C. G., Eglinger, J., Stadler, M. B., Giorgetti, L., & Chao, J. A. (2017) · Molecular Cell · doi:10.1016/j.molcel.2017.09.030 · Cited by 225 · see citing works
Complexities of post-transcriptional regulation and the modeling of ceRNA crosstalk
Smillie, C. L., Sirey, T., & Ponting, C. P. (2018) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.1080/10409238.2018.1447542 · Cited by 238 · see citing works
The rough endoplasmatic reticulum is a central nucleation site of siRNA‐mediated RNA silencing
Stalder, L., Heusermann, W., Sokol, L., Trojer, D., Wirz, J., Hean, J., Fritzsche, A., Aeschimann, F., Pfanzagl, V., Basselet, P., et al. (2013) · The EMBO Journal · doi:10.1038/emboj.2013.52 · Cited by 229 · see citing works
Deadenylation is prerequisite for P-body formation and mRNA decay in mammalian cells
Zheng, D., Ezzeddine, N., Chen, C. A., Zhu, W., He, X., & Shyu, A. (2008) · The Journal of Cell Biology · doi:10.1083/jcb.200801196 · Cited by 227 · see citing works
The Dynamics of Mammalian P Body Transport, Assembly, and Disassembly In Vivo
Aizer, A., Brody, Y., Ler, L. W., Sonenberg, N., Singer, R. H., & Shav‐Tal, Y. (2008) · Molecular Biology of the Cell · doi:10.1091/mbc.e08-05-0513 · Cited by 227 · see citing works
Multiple Modes of Protein–Protein Interactions Promote RNP Granule Assembly
Mittag, T., & Parker, R. (2018) · Journal of Molecular Biology · doi:10.1016/j.jmb.2018.08.005 · Cited by 226 · see citing works
Phosphorylation of Argonaute 2 at serine-387 facilitates its localization to processing bodies
Zeng, Y., Sankala, H. M., Zhang, X., & Graves, P. R. (2008) · Biochemical Journal · doi:10.1042/bj20080599 · Cited by 225 · see citing works
Enzymatic Noncovalent Synthesis
He, H., Tan, W., Guo, J., Yi, M., Shy, A. N., & Xu, B. (2020) · Chemical Reviews · doi:10.1021/acs.chemrev.0c00306 · Cited by 224 · see citing works
MicroRNAs identified in highly purified liver-derived mitochondria may play a role in apoptosis
Kren, B. T., Wong, P. Y.-P., Sarver, A. L., Zhang, X., Zeng, Y., & Steer, C. J. (2009) · RNA Biology · doi:10.4161/rna.6.1.7534 · Cited by 216 · see citing works
MicroRNAs: Biogenesis and Molecular Functions
Liu, X., Fortin, K., & Mourelatos, Z. (2008) · Brain Pathology · doi:10.1111/j.1750-3639.2007.00121.x · Cited by 214 · see citing works
Translational coregulation of 5′TOP mRNAs by TIA-1 and TIARPreprint
Damgaard, C. K., & Lykke‐Andersen, J. (2011) · Genes & Development · doi:10.1101/gad.17355911 · Cited by 214 · see citing works
Kulkarni, M. G., Ozgur, S., & Stoecklin, G. (2010) · Biochemical Society Transactions · doi:10.1042/bst0380242 · Cited by 208 · see citing works
Eulálio, A., Tritschler, F., & Izaurralde, E. (2009) · RNA · doi:10.1261/rna.1703809 · Cited by 207 · see citing works
The role of disordered protein regions in the assembly of decapping complexes and RNP granulesPreprint
Jonas, S., & Izaurralde, E. (2013) · Genes & Development · doi:10.1101/gad.227843.113 · Cited by 207 · see citing works
Breunig, M., Hozsa, C., Lungwitz, U., Watanabe, K. I., Umeda, I., Kato, H., & Göpferich, A. M. (2008) · Journal of Controlled Release · doi:10.1016/j.jconrel.2008.05.016 · Cited by 205 · see citing works
Diversion of stress granules and P-bodies during viral infection
Reineke, L. C., & Lloyd, R. E. (2013) · Virology · doi:10.1016/j.virol.2012.11.017 · Cited by 205 · see citing works
PIWI proteins and their interactors in piRNA biogenesis, germline development and gene expression
Ku, H.-Y., & Lin, H. (2014) · National Science Review · doi:10.1093/nsr/nwu014 · Cited by 198 · see citing works
Small RNAs: Regulators and guardians of the genome
Chu, C., & Rana, T. M. (2007) · Journal of Cellular Physiology · doi:10.1002/jcp.21230 · Cited by 195 · see citing works
HSP90 Protein Stabilizes Unloaded Argonaute Complexes and Microscopic P-bodies in Human Cells
Johnston, M. J. G., Geoffroy, M., Sobala, A., Hay, R. T., & Hutvágner, G. (2010) · Molecular Biology of the Cell · doi:10.1091/mbc.e09-10-0885 · Cited by 194 · see citing works
The Whereabouts of microRNA Actions: Cytoplasm and Beyond
Leung, A. K. L. (2015) · Trends in Cell Biology · doi:10.1016/j.tcb.2015.07.005 · Cited by 192 · see citing works
Nuclear Bodies: Random Aggregates of Sticky Proteins or Crucibles of Macromolecular Assembly?
Matera, A. G., Izaguire-Sierra, M., Praveen, K., & Rajendra, T. K. (2009) · Developmental Cell · doi:10.1016/j.devcel.2009.10.017 · Cited by 186 · see citing works
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 · see citing works
Ccr4-Not complex: the control freak of eukaryotic cells
Miller, J. E., & Reese, J. C. (2012) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.3109/10409238.2012.667214 · Cited by 176 · see citing works
Dynein and kinesin regulate stress-granule and P-body dynamics
Loschi, M., Leishman, C. C., Berardone, N., & Boccaccio, G. L. (2009) · Journal of Cell Science · doi:10.1242/jcs.051383 · Cited by 175 · see citing works
Formation, function, and pathology of RNP granules
Ripin, N., & Parker, R. (2023) · Cell · doi:10.1016/j.cell.2023.09.006 · Cited by 174 · see citing works
Stress-induced changes in miRNA biogenesis and functioning
Olejniczak, M., Kotowska‐Zimmer, A., & Krzyżosiak, W. J. (2017) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-017-2591-0 · Cited by 179 · see citing works
Hallacli, E., Kayatekin, C., Nazeen, S., Wang, X. H., Sheinkopf, Z. R., Sathyakumar, S., Sarkar, S., Jiang, X., Dong, X.-J., Maio, R. D., et al. (2022) · Cell · doi:10.1016/j.cell.2022.05.008 · Cited by 154 · see citing works
Subunits of the Drosophila CCR4-NOT complex and their roles in mRNA deadenylation
Temme, C., Zhang, L., Kremmer, E., Ihling, C. H., Chartier, A., Sinz, A., Simonelig, M., & Wahle, E. (2010) · RNA · doi:10.1261/rna.2145110 · Cited by 164 · see citing works
How do miRNAs mediate translational repression?
Gu, S., & Kay, M. A. (2010) · Silence · doi:10.1186/1758-907x-1-11 · Cited by 162 · see citing works
Small RNAs in early mammalian development: from gametes to gastrulation
Suh, N., & Blelloch, R. H. (2011) · Development · doi:10.1242/dev.056234 · Cited by 166 · see citing works
Structural Foundations of RNA Silencing by Argonaute
Sheu‐Gruttadauria, J., & MacRae, I. J. (2017) · Journal of Molecular Biology · doi:10.1016/j.jmb.2017.07.018 · Cited by 157 · see citing works
MicroRNAs , transforming growth factor beta‐1, and tissue fibrosis
Bowen, T., Jenkins, R. L., & Fraser, D. J. (2012) · The Journal of Pathology · doi:10.1002/path.4119 · Cited by 162 · see citing works
The DEAD-Box Protein Dhh1 Promotes Decapping by Slowing Ribosome Movement
Sweet, T. J., Kovalak, C., & Coller, J. M. (2012) · PLoS Biology · doi:10.1371/journal.pbio.1001342 · Cited by 163 · see citing works
Horman, S. R., Janas, M. M., Litterst, C. M., Wang, B., MacRae, I. J., Sever, M. J., Morrissey, D. V., Graves, P. R., Luo, B., Umesalma, S., et al. (2013) · Molecular Cell · doi:10.1016/j.molcel.2013.03.015 · Cited by 162 · see citing works
Savas, J. N., Makusky, A. J., Ottosen, S., Baillat, D., Then, F., Krainc, D., Shiekhattar, R., Markey, S. P., & Tanese, N. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0800658105 · Cited by 160 · see citing works
Stress-Induced mRNP Granules: Form and Function of P-bodies and Stress Granules
Guzikowski, A. R., Chen, Y. S., & Zid, B. M. (2019) · Wiley Interdisciplinary Reviews - RNA · doi:10.1002/wrna.1524 · Cited by 133 · see citing works
Bian, Z., Li, L., Tang, R., Hou, D., Chen, X., Zhang, C., & Zen, K. (2010) · Cell Research · doi:10.1038/cr.2010.119 · Cited by 155 · see citing works
Nonsense-Mediated RNA Decay Regulation by Cellular Stress: Implications for Tumorigenesis
Gardner, L. B. (2010) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-09-0502 · Cited by 155 · see citing works
The code within the code: microRNAs target coding regions
Forman, J. J., & Coller, H. A. (2010) · Cell Cycle · doi:10.4161/cc.9.8.11202 · Cited by 154 · see citing works
Glauninger, H., Hickernell, C. J. W., Bard, J. A. M., & Drummond, D. A. (2022) · Molecular Cell · doi:10.1016/j.molcel.2022.05.014 · Cited by 152 · see citing works
P-Body Loss Is Concomitant with Formation of a Messenger RNA Storage Domain in Mouse Oocytes1
Flemr, M., Ma, J., Schultz, R. M., & Svoboda, P. (2010) · Biology of Reproduction · doi:10.1095/biolreprod.109.082057 · Cited by 150 · see citing works
Argonaute protein identity and pairing geometry determine cooperativity in mammalian RNA silencing
Broderick, J. A., Salomon, W. E., Ryder, S., D, N. A. M., & Zamore, P. D. (2011) · RNA · doi:10.1261/rna.2778911 · Cited by 145 · see citing works
What have we learned from gene expression profiles in Huntington's disease?
Seredenina, T. S., & Luthi‐Carter, R. (2011) · Neurobiology of Disease · doi:10.1016/j.nbd.2011.07.001 · Cited by 145 · see citing works
NANOS2 interacts with the CCR4-NOT deadenylation complex and leads to suppression of specific RNAs
Suzuki, A., Igarashi, K., Aisaki, K., Kanno, J., & Saga, Y. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0908664107 · Cited by 148 · see citing works
Ozgur, S., Chekulaeva, M., & Stoecklin, G. (2010) · Molecular and Cellular Biology · doi:10.1128/mcb.00429-10 · Cited by 143 · see citing works
- Authors
- Eulalio, A., Behm-Ansmant, I., Schweizer, D., & Izaurralde, E.
- Affiliations
- MPI for Developmental Biology, Spemannstrasse 35, D-72076 Tübingen, Germany
- Max Planck Institute for Developmental Biology (DE)
- Corresponding author
- Izaurralde, Elisa
- ORCID
- Izaurralde, Elisa
- Venue
- Molecular and Cellular Biology
- Publisher
- Informa UK Limited
- Published
- 2007-06-01
- Volume
- 27
- Issue
- 11
- Pages
- 3970-3981
- ISSN
- 0270-7306 (ISSN-L)
- 1098-5549
- PMC
- PMC1900022
- OpenAlex
- W2101555571
- Cited by
- 710
- References
- 62
- Citations by year
- 2026: 18 · 2025: 20 · 2024: 25 · 2023: 26 · 2022: 34 · 2021: 33 · 2020: 30 · 2019: 26 · 2018: 31 · 2017: 29 · 2016: 30 · 2015: 32 · 2014: 40 · 2013: 45 · 2012: 58
- FWCI
- 22.81
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Molecular and Cellular Biology (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- HAL (submittedVersion, other-oa)
- Max Planck Institute for Plasma Physics (submittedVersion)
- Funders
- European Molecular Biology Organization
- Max-Planck-Gesellschaft
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA Research and Splicing
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA Interference and Gene Delivery
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
- Keywords
- P-bodies, RNA-mediated gene silencing, siRNA, microRNA, nonsense-mediated mRNA decay, mRNA degradation, post-transcriptional regulation, polysome association, mRNA decapping
- MeSH terms
- Animals, Drosophila melanogaster, Humans, Polyribosomes, Ribonucleoproteins, RNA, Messenger, Gene Silencing, RNA Stability, Cytoplasmic Structures, Drosophila Proteins, RNA, Small Interfering, MicroRNAs
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
