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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.
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“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]
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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
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Filho, C. M. C. C. (2014) · Digital Library of Theses and Dissertations (Universidade de São Paulo) · doi:10.11606/d.5.2014.tde-29102014-165054
Mendes, D. C. C. (2015) · Digital Library of Theses and Dissertations (Universidade de São Paulo) · doi:10.11606/d.5.2015.tde-01042015-143533
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Manveen, K., Duan, Z.-H., Karnik, S. S., & Pras, S. V. N. (2012) · InTech eBooks · doi:10.5772/27248
Doidge, R. (2013) · UPT. Syiah Kuala University Library (Syiah Kuala University)
Exploring the regulatory roles of microRNAs in mammalian development
Zheng, G. X. Y. (2010) · DSpace@MIT (Massachusetts Institute of Technology)
Structure and Gene-Silencing Mechanisms of Small Noncoding RNAs
Chu, C., & Rana, T. M. (2008) · Springer series in biophysics · doi:10.1007/978-3-540-70840-7_17
Reich, J. (2009) · Texas ScholarWorks (Texas Digital Library)
Ngoc, L. V., Gueydan, C., & Kruys, V. (2014)
Pour, N. K. (2012) · TSpace (University of Toronto)
Natalin, P. (2009) · heiDOK (Heidelberg University) · doi:10.11588/heidok.00008939
Gruppen, F. A. (2011) · Utrecht University Repository (Utrecht University)
Connecting the dots of RNA-directed DNA methylation in Arabidopsis thaliana
Costa‐Nunes, P., Vitins, A. P., & Pontes, O. (2014) · Chromosome Research · doi:10.1007/s10577-014-9425-9
Role of Mirna in HIV-1 Latency
Zhang, H. (2008) · Future HIV Therapy · doi:10.2217/17469600.2.3.281
Characterization of three novel RNAi machinery components in C. elegans
Yang, H. (2013) · KU ScholarWorks (The University of Kansas)
Huang, H., Wei, N., Xiong, Y., Yang, F., Fang, H., Xie, W., Zhou, Z., Cheng, H., Liang, Z., & Du, Q. (2010) · Frontiers in Biology · doi:10.1007/s11515-010-0047-0
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Kohl, A., Khromykh, A. A., Geertsema, C., Goldbach, R. W., Sterken, M. G., & Leung, J. Y. (2012)
Regulation of mRNA Decay in S. cerevisiae by the Sequence-specific RNA-binding Protein Vts1
Rendl, L. M. (2010) · TSpace (University of Toronto)
The Interplay of Eukaryotic mRNA Translation and Degradation
Hu, W. (2010) · OhioLink ETD Center (Ohio Library and Information Network)
Polysome profiling in Drosophila S2 cells
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Transgenerational Genetic Effects In Mouse Models Of Complex Traits
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Kaul, N. (2018) · Digital Commons - DU (University of Denver)
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Yoon, J. (2011) · UA Campus Repository (The University of Arizona)
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Chatterjee, S., Chakrabarty, Y., Banerjee, S., Ghosh, S., & Bhattacharyya, S. (2020) · bioRxiv · doi:10.1101/2020.05.20.105601
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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
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