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Vol. 13, Issue 1, 195-210, January 2002
Environmental stress-induced phosphorylation of eIF2Division of Rheumatology and Immunology, Brigham and
Women's Hospital, Boston, Massachusetts 02115; Cancer
Genetics, Columbia University, New York, New York 10032; and
§Max Delbrueck Center for Molecular Medicine, D-13092
Berlin, Germany
inhibits
protein translation by reducing the availability of
eIF2-GTP-tRNAiMet, the ternary complex that joins initiator
tRNAMet to the 43S preinitiation 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. 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 eIF2 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-eIF2 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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