The DOI matches its Crossref record; 62 of the 62 references it cites were found in a registry or an index.
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.
Overview
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
Verification
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?
In the citing paper
“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.
Citations
Cites
Mechanisms of gene silencing by double-stranded RNA
Meister, G., & Tuschl, T. (2004) · Nature · doi:10.1038/nature02873 · Cited by 2,598
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
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
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
Behm‐Ansmant, I., Rehwinkel, J., Doerks, T., Stark, A., Bork, P., & Izaurralde, E. (2006) · Genes & Development · doi:10.1101/gad.1424106 · Cited by 1,113
Anderson, P., & Kedersha, N. (2006) · The Journal of Cell Biology · doi:10.1083/jcb.200512082 · Cited by 984
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 970
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 866
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
The enzymes and control of eukaryotic mRNA turnover
Parker, R., & Song, H. (2004) · Nature Structural & Molecular Biology · doi:10.1038/nsmb724 · Cited by 730
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
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 715
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 679
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 670
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
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
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 581
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 551
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
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
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
Lykke‐Andersen, J., & Wagner, E. (2005) · Genes & Development · doi:10.1101/gad.1282305 · Cited by 486
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
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
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
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
Leung, A. K. L., Calabrese, J. M., & Sharp, P. A. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0608845103 · Cited by 414
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
Ingelfinger, D., Arndt‐Jovin, D. J., Lührmann, R., & Achsel, T. (2002) · RNA · doi:10.1017/s1355838202021726 · Cited by 404
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
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 387
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 369
Barbee, S. A., Estes, P. S., Cziko, A.-M., Hillebrand, J., Luedeman, R. A., Coller, J., Johnson, N., Howlett, I. C., Geng, C., Ueda, R., et al. (2006) · Neuron · doi:10.1016/j.neuron.2006.10.028 · Cited by 365
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 323
Targeting of Aberrant mRNAs to Cytoplasmic Processing Bodies
Sheth, U., & Parker, R. (2006) · Cell · doi:10.1016/j.cell.2006.04.037 · Cited by 304
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
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 269
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 267
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
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
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 253
Targeting an mRNA for Decapping
Tharun, S., & Parker, R. (2001) · Molecular Cell · doi:10.1016/s1097-2765(01)00395-1 · Cited by 238
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
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 215
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
Zaessinger, S., Busseau, I., & Simonelig, M. (2006) · Development · doi:10.1242/dev.02649 · Cited by 202
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
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
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
Wilhelm, J. E., Buszczak, M., & Sayles, S. (2005) · Developmental Cell · doi:10.1016/j.devcel.2005.09.015 · Cited by 166
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
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 145
Bonnerot, C., Boeck, R., & Lapeyre, B. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.16.5939-5946.2000 · Cited by 138
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 126
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 117
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
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
Anantharaman, V., & Aravind, L. (2004) · BMC Genomics · doi:10.1186/1471-2164-5-45 · Cited by 79
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 60
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
Flagged first, then by citations
Research works printed but not linked: 1
- Chu C. Y., 2006, PLoS Biol., 4, 1122
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
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 5,161
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
(2008) · doi:10.1038/nrg2290 · Cited by 5,199
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
Metadata
- 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