Stress granules and processing bodies are dynamically linked sites of mRNP remodeling

doi:10.1083/jcb.200502088

A correction to this article has been published: J. Cell Biol. 170 (5) 847
Published 20 June 2005. doi:10.1083/jcb.200502088
The Rockefeller University Press, 0021-9525 $8.00
JCB, Volume 169, Number 6, 871-884

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Stress granules and processing bodies are dynamically linked sites of mRNP remodeling

Nancy Kedersha¹, Georg Stoecklin¹, Maranatha Ayodele¹, Patrick Yacono², Jens Lykke-Andersen³, Marvin J. Fritzler⁴, Donalyn Scheuner⁵, Randal J. Kaufman⁵, David E. Golan², and Paul Anderson¹

¹ Division of Rheumatology and Immunology, Harvard Medical School, Hematology Division, Brigham and Women's Hospital, Boston, MA 02115
² Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Hematology Division, Brigham and Women's Hospital, Boston, MA 02115
³ Molecular, Cellular, and Developmental Biology, University of Colorado, Boulder, CO 80309
⁴ Department of Biochemistry and Molecular Biology, University of Calgary, Calgary, Alberta T2N 4N1, Canada
⁵ University of Michigan Medical Center and Howard Hughes Medical Institute, Ann Arbor, MI 48109

Correspondence to Nancy Kedersha: nkedersha{at}rics.bwh.harvard.edu

Stress granules (SGs) are cytoplasmic aggregates of stalledtranslational preinitiation complexes that accumulate duringstress. GW bodies/processing bodies (PBs) are distinct cytoplasmicsites of mRNA degradation. In this study, we show that SGs andPBs are spatially, compositionally, and functionally linked.SGs and PBs are induced by stress, but SG assembly requireseIF2 ${alpha}$ phosphorylation, whereas PB assembly does not. They arealso dispersed by inhibitors of translational elongation andshare several protein components, including Fas-activated serine/threoninephosphoprotein, XRN1, eIF4E, and tristetraprolin (TTP). In contrast,eIF3, G3BP, eIF4G, and PABP-1 are restricted to SGs, whereasDCP1a and 2 are confined to PBs. SGs and PBs also can harborthe same species of mRNA and physically associate with one anotherin vivo, an interaction that is promoted by the related mRNAdecay factors TTP and BRF1. We propose that mRNA released fromdisassembled polysomes is sorted and remodeled at SGs, fromwhich selected transcripts are delivered to PBs for degradation.

Abbreviations used in this paper: ARE, adenine/uridine-richdestabilizing elements; FAST, Fas-activated serine/threoninephosphoprotein; PB, processing body; SG, stress granule; siRNA,small interference RNA; TIA, T cell intracellular antigen; TIAR,TIA related; TTP, tristetraprolin.

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