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1 Department of Cellular and Molecular Physiology, The Pennsylvania State University College of Medicine, Hershey, Pennsylvania 17033; and 2 The Skirball Institute, New York University School of Medicine, New York, New York 10016
In eukaryotic cells subjected to
environmental stress, untranslated mRNA accumulates in discrete
cytoplasmic foci that have been termed stress granules. Recent studies
have shown that in addition to mRNA, stress granules also contain 40S
ribosomal subunits and various translation initiation factors,
including the mRNA binding proteins eIF4E and eIF4G. However, eIF2, the
protein that transfers initiator methionyl-tRNAi
(Met-tRNAi) to the 40S ribosomal subunit, has not been
detected in stress granules. This result is surprising because the
eIF2 · GTP · Met-tRNAi complex is thought to
bind to the 40S ribosomal subunit before the
eIF4G · eIF4E · mRNA complex. In the present study, we
show in both NIH-3T3 cells and mouse embryo fibroblasts that stress
granules contain not only eIF2 but also the guanine nucleotide exchange
factor for eIF2, eIF2B. Moreover, we show that phosphorylation of the 
-subunit of eIF2 is necessary and sufficient for stress granule formation during the unfolded protein response. Finally, we also show
that stress granules contain many, if not all, of the components of the
48S preinitiation complex, but not 60S ribosomal subunits, suggesting
that they represent stalled translation initiation complexes.
eIF4E; eIF4G; eIF3; unfolded protein response; PERK
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