ArticleMolecular biology of the cell2015
P-body assembly requires DDX6 repression complexes rather than decay or Ataxin2/2L complexes.
Article in Molecular biology of the cell, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 113 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
113 citing papers in PubMed, 202 citations in OpenAlex.
- Proximity labeling puts ZFP36L1 as central hub for posttranscriptional regulation networks in T cells.Life science alliance · 2026Article
- Selective RNA sequestration in biomolecular condensates directs cell fate transitions.Nature biotechnology · 2026Article
- Modulating RNA condensates to control cell fate.Nature biotechnology · 2026Article
- Global cellular responses to lysosomal damage.Current biology : CB · 2026Review
- Novel post-transcriptional dimension of glucocorticoid action through mRNA translation and P-body remodeling.Signal transduction and targeted therapy · 2026Article
- RNA helicase DDX6 governs ASC speck formation in P-bodies and the transition to stress granules via phase separation during inflammasome activation.Cell discovery · 2026Article
- Article
- The Effect of Protein Tagging on Aggregation and Phase Separation.Journal of cellular biochemistry · 2026Review
- The enteroviral protease target LSM14A operates outside of P-bodies to augment antiviral innate immunity.bioRxiv : the preprint server for biology · 2026Article
- A framework for the exploration of subcellular compartmentalization of RNA-binding proteins.Nature communications · 2026Article
- Polyphosphate modulates the stress-responsive formation of functional RNA-protein condensates in bacteria and mammalian cells.PLoS biology · 2026Article
- Plant P-bodies in post-transcriptional control: Composition, dynamics, and context-dependent roles.Plant communications · 2026Review
- Fluorescence-activated particle sorting for condensate purification.Nature protocols · 2026Review
- The role of low-complexity repeats in RNA-RNA interactions and a deep learning framework for duplex prediction.Nature communications · 2026Article
- Reshaping cancer cell plasticity by P-body dynamics and protein translation.Communications biology · 2026Review
- DDX6 undergoes phase separation to modulate metabolic plasticity and chemoresistance.Nature communications · 2025Article
- The yeast Mkt1/Pbp1 complex promotes adaptive responses to respiratory growth.The Journal of cell biology · 2025Article
- Processing bodies promote lysosomal quality control and cell survival during recovery from lysosomal damage.Research square · 2025Article
- DDX6 interacts with DDX3X to repress translation in microRNA-mediated silencing.Nucleic acids research · 2025Article
- Translational repression by 4E-T is crucial to maintain the prophase-I arrest in vertebrate oocytes.Nature communications · 2025Article
53 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
Abstract
P-bodies are cytoplasmic ribonucleoprotein granules involved in posttranscriptional regulation. DDX6 is a key component of their assembly in human cells. This DEAD-box RNA helicase is known to be associated with various complexes, including the decapping complex, the CPEB repression complex, RISC, and the CCR4/NOT complex. To understand which DDX6 complexes are required for P-body assembly, we analyzed the DDX6 interactome using the tandem-affinity purification methodology coupled to mass spectrometry. Three complexes were prominent: the decapping complex, a CPEB-like complex, and an Ataxin2/Ataxin2L complex. The exon junction complex was also found, suggesting DDX6 binding to newly exported mRNAs. Finally, some DDX6 was associated with polysomes, as previously reported in yeast. Despite its high enrichment in P-bodies, most DDX6 is localized out of P-bodies. Of the three complexes, only the decapping and CPEB-like complexes were recruited into P-bodies. Investigation of P-body assembly in various conditions allowed us to distinguish required proteins from those that are dispensable or participate only in specific conditions. Three proteins were required in all tested conditions: DDX6, 4E-T, and LSM14A. These results reveal the variety of pathways of P-body assembly, which all nevertheless share three key factors connecting P-body assembly to repression.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.