Stress granules and processing bodies are dynamically linked sites of mRNP remodeling
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Open Access
- 20 June 2005
- journal article
- Published by Rockefeller University Press in The Journal of cell biology
- Vol. 169 (6), 871-884
- https://doi.org/10.1083/jcb.200502088
Abstract
Stress granules (SGs) are cytoplasmic aggregates of stalled translational preinitiation complexes that accumulate during stress. GW bodies/processing bodies (PBs) are distinct cytoplasmic sites of mRNA degradation. In this study, we show that SGs and PBs are spatially, compositionally, and functionally linked. SGs and PBs are induced by stress, but SG assembly requires eIF2α phosphorylation, whereas PB assembly does not. They are also dispersed by inhibitors of translational elongation and share several protein components, including Fas-activated serine/threonine phosphoprotein, XRN1, eIF4E, and tristetraprolin (TTP). In contrast, eIF3, G3BP, eIF4G, and PABP-1 are restricted to SGs, whereas DCP1a and 2 are confined to PBs. SGs and PBs also can harbor the same species of mRNA and physically associate with one another in vivo, an interaction that is promoted by the related mRNA decay factors TTP and BRF1. We propose that mRNA released from disassembled polysomes is sorted and remodeled at SGs, from which selected transcripts are delivered to PBs for degradation.Keywords
This publication has 46 references indexed in Scilit:
- Staufen Recruitment into Stress Granules Does Not Affect Early mRNA Transport in OligodendrocytesMolecular Biology of the Cell, 2005
- Survival motor neuron protein facilitates assembly of stress granulesFEBS Letters, 2004
- Cytoplasmic foci are sites of mRNA decay in human cellsThe Journal of cell biology, 2004
- In vivo kinetics of Cajal body componentsThe Journal of cell biology, 2004
- RETRACTED: The RasGAP-associated endoribonuclease G3BP assembles stress granulesThe Journal of cell biology, 2003
- Trapping of messenger RNA by Fragile X Mental Retardation protein into cytoplasmic granules induces translation repressionHuman Molecular Genetics, 2002
- Modulation of Eukaryotic mRNA Stability via the Cap-binding Translation Complex eIF4FJournal of Molecular Biology, 2002
- Nonsense-mediated mRNA decayCurrent Biology, 2002
- Tight Binding of the Phosphorylated α Subunit of Initiation Factor 2 (eIF2α) to the Regulatory Subunits of Guanine Nucleotide Exchange Factor eIF2B Is Required for Inhibition of Translation InitiationMolecular and Cellular Biology, 2001
- The 3' to 5' degradation of yeast mRNAs is a general mechanism for mRNA turnover that requires the SKI2 DEVH box protein and 3' to 5' exonucleases of the exosome complexThe EMBO Journal, 1998