Preventing proteostasis diseases by selective inhibition of a phosphatase regulatory subunit

Science

Volumn 348, Issue 6231, 2015, Pages 239-242

  Das, Indrajit ^a   Krzyzosiak, Agnieszka ^a   Schneider, Kim ^a   Wrabetz, Lawrence ^b,c   D'Antonio, Maurizio ^b   Barry, Nicholas ^a   Sigurdardottir, Anna ^a   Bertolotti, Anne ^a  

^a MRC LABORATORY OF MOLECULAR BIOLOGY   (United Kingdom)

^b SAN RAFFAELE HOSPITAL   (Italy)

^c UNIVERSITY AT BUFFALO   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ESTERASE INHIBITOR; GUANABENZ; INITIATION FACTOR 2ALPHA; PHOSPHOPROTEIN PHOSPHATASE 1; PPP1R15A PROTEIN; SELECTIVE INHIBITOR OF A HOLOPHOSPHATASE; UNCLASSIFIED DRUG; ENZYME INHIBITOR; PPP1R15A PROTEIN, HUMAN; PPP1R15A PROTEIN, MOUSE; SEPHIN1;

DEFECT; DISEASE CONTROL; ENZYME ACTIVITY; MOLECULAR ANALYSIS; SIGNALING;

ANIMAL CELL; ANIMAL EXPERIMENT; ANIMAL MODEL; ANIMAL TISSUE; ARTICLE; CONTROLLED STUDY; DEMYELINATING NEUROPATHY; DISORDERS OF AMINO ACID AND PROTEIN METABOLISM; DORSAL ROOT; ENZYME ACTIVE SITE; ENZYME INHIBITION; GENE EXPRESSION; MOUSE; NERVE FIBER; NONHUMAN; PRIORITY JOURNAL; PROTEIN HOMEOSTASIS; PROTEIN PHOSPHORYLATION; SCIATIC NERVE; SPATIAL LEARNING; WEIGHT GAIN; AMYOTROPHIC LATERAL SCLEROSIS; ANALOGS AND DERIVATIVES; ANIMAL; ANTAGONISTS AND INHIBITORS; CELL CULTURE; CHARCOT-MARIE-TOOTH DISEASE; DISEASE MODEL; DRUG EFFECTS; ENDOPLASMIC RETICULUM STRESS; HELA CELL LINE; HUMAN; METABOLISM; MOLECULARLY TARGETED THERAPY; PATHOLOGY; PHOSPHORYLATION; PROTEIN FOLDING; PROTEOSTASIS DEFICIENCIES; SIGNAL TRANSDUCTION; SYNTHESIS; TRANSGENIC MOUSE;

MUS;

AMYOTROPHIC LATERAL SCLEROSIS; ANIMALS; CELLS, CULTURED; CHARCOT-MARIE-TOOTH DISEASE; DISEASE MODELS, ANIMAL; ENDOPLASMIC RETICULUM STRESS; ENZYME INHIBITORS; GUANABENZ; HELA CELLS; HUMANS; MICE; MICE, TRANSGENIC; MOLECULAR TARGETED THERAPY; PHOSPHORYLATION; PROTEIN FOLDING; PROTEIN PHOSPHATASE 1; PROTEOSTASIS DEFICIENCIES; SIGNAL TRANSDUCTION;

EID: 84927619395     PISSN: 00368075     EISSN: 10959203     Source Type: Journal    
DOI: 10.1126/science.aaa4484     Document Type: Article

References (25)

1. H. P. Harding, Y. Zhang, A. Bertolotti, H. Zeng, D. Ron, Mol. Cell 5, 897-904 (2000).
2. D. Scheuner et al., Mol. Cell 7, 1165-1176 (2001).
3. H. P. Harding et al., Mol. Cell 11, 619-633 (2003).
4. P. Tsaytler, H. P. Harding, D. Ron, A. Bertolotti, Science 332, 91-94 (2011).
5. D. Scheuner et al., J. Biol. Chem. 281, 21458-21468 (2006).
6. W. E. Balch, R. I. Morimoto, A. Dillin, J. W. Kelly, Science 319, 916-919 (2008).
7. B. Holmes, R. N. Brogden, R. C. Heel, T. M. Speight, G. S. Avery, Drugs 26, 212-229 (1983).
8. M. A. Brostrom, X. J. Lin, C. Cade, D. Gmitter, C. O. Brostrom, J. Biol. Chem. 264, 1638-1643 (1989).
9. I. Novoa et al., EMBO J. 22, 1180-1187 (2003).
10. H. P. Harding et al., Mol. Cell 6, 1099-1108 (2000).
11. R. H. Meacham et al., J. Pharmacol. Exp. Ther. 214, 594-598 (1980).
12. A. H. Hall, S. C. Smolinske, K. W. Kulig, B. H. Rumack, Ann. Intern. Med. 102, 787-788 (1985).
13. D. Genoux et al., Nature 418, 970-975 (2002).
14. M. Costa-Mattioli et al., Cell 129, 195-206 (2007).
15. R. G. M. Morris, P. Garrud, J. N. P. Rawlins, J. O'Keefe, Nature 297, 681-683 (1982).
16. M. Pennuto et al., Neuron 57, 393-405 (2008).
17. M. D'Antonio et al., J. Exp. Med. 210, 821-838 (2013).
18. L. Wrabetz et al., J. Neurosci. 26, 2358-2368 (2006).
19. A. Nordlund, M. Oliveberg, HFSP J. 2, 354-364 (2008).
20. H. Nishitoh et al., Genes Dev. 22, 1451-1464 (2008).
21. L. Wang, B. Popko, R. P. Roos, Hum. Mol. Genet. 23, 2629-2638 (2014).
22. M. E. Gurney et al., Science 264, 1772-1775 (1994).
23. S. J. Marciniak et al., Genes Dev. 18, 3066-3077 (2004).
24. J. Wang et al., Proc. Natl. Acad. Sci. U.S.A. 106, 1392-1397 (2009).
25. H. P. Harding et al., Proc. Natl. Acad. Sci. U.S.A. 106, 1832-1837 (2009).