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J. Biol. Chem., Vol. 280, Issue 17, 16925-16933, April 29, 2005
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Heme-regulated Inhibitor Kinase-mediated Phosphorylation of Eukaryotic Translation Initiation Factor 2 Inhibits Translation, Induces Stress Granule Formation, and Mediates Survival upon Arsenite Exposure*
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From the
Howard Hughes Medical Institute and the ||Department of Biological Chemistry, University of Michigan Medical Center, Ann Arbor, Michigan 48109, the Division of Rheumatology, Immunology, and Allergy, Brigham and Women's Hospital, Boston, Massachusetts 02115, and the ¶Harvard-MIT Division of Health Sciences and Technology, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139
Exposure to arsenite inhibits protein synthesis and activates multiple stress signaling pathways. Although arsenite has diverse effects on cell metabolism, we demonstrated that phosphorylation of eukaryotic translation initiation factor 2 at Ser-51 on the 
subunit was necessary to inhibit protein synthesis initiation in arsenite-treated cells and was essential for stress granule formation. Of the four protein kinases known to phosphorylate eukaryotic translation initiation factor 2, only the heme-regulated inhibitor kinase (HRI) was required for the translational inhibition in response to arsenite treatment in mouse embryonic fibroblasts. In addition, HRI expression was required for stress granule formation and cellular survival after arsenite treatment. In vivo studies elucidated a fundamental requirement for HRI in murine survival upon acute arsenite exposure. The results demonstrated an essential role for HRI in mediating arsenite stress-induced phosphorylation of eukaryotic translation initiation factor 2, inhibition of protein synthesis, stress granule formation, and survival.
Received for publication, November 15, 2004 , and in revised form, January 28, 2005.
* Portions of this work were supported by National Institutes of Health RO1 Grants DK42394 (to R. J. K.) and DK 16272 (to J.-J. C.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.
** To whom correspondence should be addressed: Howard Hughes Medical Inst. and the Dept. of Biological Chemistry, University of Michigan Medical Center, Ann Arbor, MI 48109-0650. Tel.: 734-763-9037; Fax: 734-763-9323; E-mail: kaufmanr{at}umich.edu.
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