A selective inhibitor of elF2α dephosphorylation protects cells from ER stress

Science

Volumn 307, Issue 5711, 2005, Pages 935-939

  Boyce, Michael ^a   Bryant, Kevin F ^a   Jousse, Céline ^b   Long, Kai ^c   Harding, Heather P ^b   Scheuner, Donalyn ^d   Kaufman, Randal J ^d   Ma, Dawei ^c   Coen, Donald M ^a   Ron, David ^b   Yuan, Junying ^a  

^a HARVARD MEDICAL SCHOOL   (United States)

^b NEW YORK UNIVERSITY SCHOOL OF MEDICINE   (United States)

^c SHANGHAI INSTITUTE OF ORGANIC CHEMISTRY   (China)

^d UNIVERSITY OF MICHIGAN HEALTH SYSTEM   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

COMPLEXATION; ENZYME INHIBITION; ENZYMES; PHOSPHORUS COMPOUNDS; VIRUSES;

DEPHOSPHORYLATION; ENDOPLASMIC RETICULUM (ER) STRESS; PHOSPHATASE; VIRUS PROTEINS;

CELLS;

INITIATION FACTOR 2ALPHA; PROTEIN INHIBITOR; SALUBRINAL; UNCLASSIFIED DRUG; VIRUS PROTEIN; CALYCULIN A; CELL CYCLE PROTEIN; CINNAMIC ACID DERIVATIVE; CREP PROTEIN, MOUSE; DIFFERENTIATION ANTIGEN; DRUG DERIVATIVE; ENZYME INHIBITOR; GAMMA 34.5 PROTEIN, HUMAN HERPESVIRUS 1; INITIATION FACTOR 2; OXAZOLE DERIVATIVE; PHOSPHOPROTEIN PHOSPHATASE; PPP1R15A PROTEIN, MOUSE; PROTEIN; PROTEIN KINASE; THIOUREA; TUNICAMYCIN;

INHIBITOR;

ANIMAL CELL; ARTICLE; CELL PROTECTION; CONTROLLED STUDY; DEPHOSPHORYLATION; DRUG INHIBITION; DRUG SCREENING; DRUG TARGETING; ENDOPLASMIC RETICULUM; HERPES SIMPLEX VIRUS; NONHUMAN; OXIDATIVE STRESS; PRIORITY JOURNAL; RAT; VIRUS REPLICATION; ANIMAL; APOPTOSIS; CELL LINE; CELL STRAIN; DOSE RESPONSE; DRUG EFFECT; HERPES SIMPLEX KERATITIS; HERPES SIMPLEX VIRUS 1; MALE; METABOLISM; MOUSE; PHOSPHORYLATION; PHYSIOLOGY; PROTEIN FOLDING; REPORTER GENE; VIROLOGY;

ANIMALIA; EUKARYOTA; HERPES; SIMPLEXVIRUS;

ANIMALS; ANTIGENS, DIFFERENTIATION; APOPTOSIS; CELL CYCLE PROTEINS; CELL LINE; CINNAMATES; CYTOPROTECTION; DOSE-RESPONSE RELATIONSHIP, DRUG; ENDOPLASMIC RETICULUM; ENZYME INHIBITORS; EUKARYOTIC INITIATION FACTOR-2; GENES, REPORTER; HERPESVIRUS 1, HUMAN; KERATITIS, HERPETIC; MALE; MICE; OXAZOLES; PC12 CELLS; PHOSPHOPROTEIN PHOSPHATASE; PHOSPHORYLATION; PROTEIN FOLDING; PROTEIN KINASES; PROTEINS; RATS; THIOUREA; TUNICAMYCIN; VIRAL PROTEINS; VIRUS REPLICATION;

EID: 13644256191     PISSN: 00368075     EISSN: None     Source Type: Journal    
DOI: 10.1126/science.1101902     Document Type: Article

References (32)

1. R. J. Kaufman, Genes Dev. 13, 1211 (1999).
2. H. P. Harding, M. Calfon, F. Urano, I. Novoa, D. Ron, Annu. Rev. Cell Dev. Biol. 18, 575 (2002).
3. M. Aridor, W. E. Balch, Nat. Med. 5, 745 (1999).
4. R. V. Rao, H. M. Ellerby, D. E. Bredesen, Cell Death Differ. 11, 372 (2004).
5. R. V. Rao et al. J. Biol. Chem. 276, 33869 (2001).
6. J. A. Morris, A. J. Domer, C. A. Edwards, L. M. Hendershot, R. J. Kaufman J. Biol. Chem. 272, 4327 (1997).
7. H. Yoshida, T. Matsui, A. Yamamoto, T. Okada, K. Mori, Cell 107, 881 (2001).
8. M. Calfon et al., Nature 415, 92 (2002).
9. H. P. Harding, Y. Zhang, D. Ron, Nature 397, 271 (1999).
10. R. Sood, A. C. Porter, D. A. Olsen, D. R. Cavener, R. C. Wek, Genetics 154, 787 (2000).
11. H. P. Harding et al., Mol. Cell 6, 1099 (2000).
12. J. W. Brewer, J. A. Diehl, Proc. Natl. Acad. Sci. U.S.A. 97, 12625 (2000).
13. I. Novoa, H. Zeng, H. P. Harding, D. Ron, J. Cell Biol. 153, 1011 (2001).
14. H. P. Harding, Y. Zhang, A. Bertolotti, H. Zeng, D. Ron, Mol. Cell 5, 897 (2000).
15. D. Scheuner et al., Mol. Cell 7, 1165 (2001).
16. C. Jousse et al., J. Cell Biol. 163, 767 (2003).
17. P. D. Lu et al., EMBO J. 23, 169 (2004).
18. A. Hinnebusch, in Translational Control of Gene Expression, N. Sonenberg, J. W. B. Hershey, M. B. Mathews, Eds. (Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY, 2000), pp. 185-244.
19. R. J. Kaufman, in Translational Control of Gene Expression, N. Sonenberg, J. W. B. Hershey, M. B. Mathews, Eds. (Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY, 2000), pp. 503-528.
20. J. J. Chen, in Translational Control of Gene expression, N. Sonenberg, J. W. B. Hershey, M. B. Mathews, Eds. (Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY, 2000), pp. 529-546.
21. M. Boyce et al., unpublished data.
22. X. Z. Wang et al., EMBO J. 17, 5708 (1998).
23. A. McCluskey, A. T. Sim, J. A. Sakoff, J. Med. Chem. 45, 1151 (2002).
24. N. G. Anderson, J. L. Maller, N. K. Tonks, T. W. Sturgill, Nature 343, 651 (1990).
25. M. Unlu, M. E. Morgan, J. S. Minden, Electrophoresis 18, 2071 (1997).
26. M. Boyce, J. S. Minden, J. Yuan, unpublished observations.
27. J. Chou, J. J. Chen, M. Gross, B. Roizman, Proc. Natl. Acad. Sci. U.S.A. 92, 10516 (1995).
28. J. Chou, B. Roizman, Proc. Natl. Acad. Sci. U.S.A. 91, 5247 (1994).
29. B. He, M. Gross, B. Roizman, Proc. Natl. Acad. Sci. U.S.A. 94, 843 (1997).
30. J. Chou, E. R. Kern, R. J. Whitley, B. Roizman, Science 250, 1262 (1990).
31. D. A. Leib et al., J. Virol. 63, 759 (1989).
32. We thank J. Alvarez, J.-J. Chen, J. Glaven, O. Gozani, R. King, T. Mitchison, F. Roth, S. Ryeom, M. Shair, C. T. Walsh, and members of the Yuan lab for reagents and advice and J. Follen and D. Hayes of the Harvard Institute of Chemistry and Cell Biology for tireless help with small molecule screening. Supported by NIH grants R37-AG012859 and GM64703 (J.Y.); DDK42394 (R.J.K.); AI26077, AI19838, and NS35138 (D.M.C.); and ES08681 and DK47119 (D.R.); NSF (M.B.); grant KGCX2-SW-209 from the Chinese Academy of Sciences; and grant 20228205 from the National Natural Science Foundation of China (D.M.).