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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 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 eIF2 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.

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

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