期刊
MOLECULAR CELL
卷 68, 期 1, 页码 144-+出版社
CELL PRESS
DOI: 10.1016/j.molcel.2017.09.003
关键词
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资金
- Agence Nationale de la Recherche [ANR-14-CE09-0013-01]
- Fondation pour la Recherche Medicale [FRM SPF20130526681, DBI20131228556]
- Association pour la Recherche sur le Cancer [SFI2010201632]
- Idex Sorbonne Universite EMERGENCE [SU-15-R-EMR-08]
- France Genomique national infrastructure, as part of the Investissements d'Avenir [ANR-10-INBS-09]
- Ligue Nationale contre le Cancer (labelisation)
- Agence Nationale de la Recherche (ANR) [ANR-14-CE09-0013] Funding Source: Agence Nationale de la Recherche (ANR)
Within cells, soluble RNPs can switch states to coassemble and condense into liquid or solid bodies. Although these phase transitions have been reconstituted in vitro, for endogenous bodies the diversity of the components, the specificity of the interaction networks, and the function of the coassemblies remain to be characterized. Here, by developing a fluorescence-activated particle sorting (FAPS) method to purify cytosolic processing bodies (P-bodies) from human epithelial cells, we identified hundreds of proteins and thousands of mRNAs that structure a dense network of interactions, separating P-body from non-P-body RNPs. mRNAs segregating into P-bodies are translationally repressed, but not decayed, and this repression explains part of the poor genome-wide correlation between RNA and protein abundance. P-bodies condense thousands of mRNAs that strikingly encode regulatory processes. Thus, we uncovered how P-bodies, by condensing and segregating repressed mRNAs, provide a physical substrate for the coordinated regulation of posttranscriptional mRNA regulons.
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