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J. Biol. Chem., Vol. 281, Issue 43, 32870-32878, October 27, 2006

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Eukaryotic Initiation Factor 2-independent Pathway of Stress Granule Induction by the Natural Product Pateamine A^*

Yongjun Dang, Nancy Kedersha, Woon-Kai Low, Daniel Romo^¶, Myriam Gorospe^||, Randal Kaufman^**, Paul Anderson, and Jun O. Liu¹

From the Department of Pharmacology and Molecular Sciences, Solomon H. Snyder Department of Neuroscience, and Department of Oncology, Johns Hopkins School of Medicine, Baltimore, Maryland 21205, Division of Rheumatology and Immunology, Harvard Medical School, Brigham and Women's Hospital, Boston, Massachusetts 02115, ^¶Department of Chemistry, Texas A&M University, College Station, Texas 77842, ^||RNA Regulation Section, NIA, National Institutes of Health, Baltimore, Maryland 21224, and ^**Howard Hughes Medical Institute, Departments of Biological Chemistry and Internal Medicine, University of Michigan Medical Center, Ann Arbor, Michigan 48109-0650

Stress granules are aggregates of small ribosomal subunits, mRNA, and numerous associated RNA-binding proteins that include several translation initiation factors. Stress granule assembly occurs in the cytoplasm of higher eukaryotic cells under a wide variety of stress conditions, including heat shock, UV irradiation, hypoxia, and exposure to arsenite. Thus far, a unifying principle of eukaryotic initiation factor 2 phosphorylation prior to stress granule formation has been observed from the majority of experimental evidence. Pateamine A, a natural product isolated from marine sponge, was recently reported to inhibit eukaryotic translation initiation and induce the formation of stress granules. In this report, the protein composition and fundamental progression of stress granule formation and disassembly induced by pateamine A was found to be similar to that for arsenite. However, pateamine A-induced stress granules were more stable and less prone to disassembly than those formed in the presence of arsenite. Most significantly, pateamine A induced stress granules independent of eukaryotic initiation factor 2 phosphorylation, suggesting an alternative mechanism of formation from that previously described for other cellular stresses. Taking into account the known inhibitory effect of pateamine A on eukaryotic translation initiation, a model is proposed to account for the induction of stress granules by pateamine A as well as other stress conditions through perturbation of any steps prior to the rejoining of the 60S ribosomal subunit during the entire translation initiation process.

Received for publication, June 27, 2006 , and in revised form, August 31, 2006.

^* This work was supported by NCI, National Institutes of Health (NIH) and the Keck Foundation (to J. O. L.), NIH Grants A1033600 (to P. J. A. and N. L. K.) and DK42394 (to R. J. K.), and a Canadian Institutes of Health Research fellowship (to W. K. L.). 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.

The on-line version of this article (available at http://www.jbc.org) contains supplemental Figs. S1-S3.

¹ To whom correspondence should be addressed: Dept. of Pharmacology and Molecular Sciences, Johns Hopkins School of Medicine, Hunterian 516, 725 N. Wolfe St., Baltimore, MD 21205. Tel.: 410-955-4619; Fax: 410-955-4620; E-mail: joliu{at}jhu.edu.

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