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A more recent version of this article appeared on January 1, 2002
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Submitted on May 1, 2001
Revised on October 17, 2001
Accepted on October 22, 2001
1 Division of Rheumatology and Immunology, Brigham and Women's Hospital, Boston, Massachusetts
2 Cancer Genetics, Columbia University, New York, New York
3 Max Delbruck Center for Molecular Medicine, Berlin, Germany
* Corresponding author. E-mail address: panderson{at}rics.bwh.harvard.edu.
Environmental stress-induced phosphorylation of eIF2alpha inhibits protein translation by reducing the availability of eIF2-GTP-tRNAiMet the ternary complex that joins initiator tRNAMet to the 43S pre-initiation complex. The resulting untranslated mRNA is dynamically routed to discrete cytoplasmic foci known as stress granules (SGs), a process requiring the related RNA-binding proteins TIA-1 and TIAR (Kedersha et al., 2000). SGs appear to be in equilibrium with polysomes, but the nature of this relationship is obscure. We now show that most components of the 48S preinitiation complex (i.e. small, but not large ribosomal subunits, eIF3, eIF4E, eIF4G) are coordinately recruited to SGs in arsenite-stressed cells. In contrast, eIF2 is not a component of newly assembled SGs. Cells expressing a phosphomimetic mutant (S51D) of eIF2alpha assemble SGs of similar composition, confirming that the recruitment of these factors is a direct consequence of blocked translational initiation and not due to other effects of arsenite. Surprisingly, phospho-eIF2alpha is recruited to SGs that are disassembling in cells recovering from arsenite-induced stress. We discuss these results in the context of a translational checkpoint model wherein TIA and eIF2 are functional antagonists of translational initiation, and in which lack of ternary complex drives SG assembly.
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