Hsp90 is involved in the formation of P-bodies and stress granules |
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Authors: | Matsumoto Ken Minami Michiko Shinozaki Fumika Suzuki Yukari Abe Keiko Zenno Shuhei Matsumoto Shogo Minami Yasufumi |
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Institution: | aMolecular Entomology Laboratory, RIKEN, 2-1 Hirosawa, Wako, Saitama 351-0198, Japan;bPRESTO, Japan Science and Technology Agency, 4-1-8 Honcho, Kawaguchi, Saitama 332-0012, Japan;cDepartment of Natural and Environmental Science, Faculty of Education, Tokyo Gakugei University, 1-1-4 Nukuikitamachi, Koganei, Tokyo 184-8501, Japan;dGraduate School of Agricultural and Life Sciences, University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo 113-8657, Japan;eDepartment of Biotechnology, Maebashi Institute of Technology, 460-1 Kamisadori-cho, Maebashi, Gunma 371-0816, Japan |
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Abstract: | Previously, we found that treatment of cells with the Hsp90 inhibitor geldanamycin (GA) leads to a substantial reduction in the number of processing bodies (P-bodies), and also alters the size and subcellular localization of stress granules. These findings imply that the chaperone activity of Hsp90 is involved in the formation of P-bodies and stress granules. To verify these observations, we examined whether another Hsp90 inhibitor radicicol (RA) affected P-bodies and stress granules. Treatment with RA reduced the level of the Hsp90 client protein Argonaute 2 and the number of P-bodies. Although stress granules still assembled in RA-treated cells upon heat shock, they were smaller and more dispersed in the cytoplasm than those in untreated cells. Furthermore eIF4E and eIF4E-transporter were dissociated selectively from stress granules in RA-treated cells. These observations were comparable to those obtained upon treatment with GA in our previous work. Thus, we conclude that abrogation of the chaperone activity of Hsp90 affects P-body formation and the integrity of stress granules. |
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Keywords: | Abbreviations: GA geldanamycin P-body Processing body 4E-T eIF4E-transporter Ago Argonaute RA radicicol |
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