Reaper eliminates IAP proteins through stimulated IAP degradation and generalized translational inhibition

Nature Cell Biology

Volumn 4, Issue 6, 2002, Pages 439-444

  Holley, Christopher L ^a   Olson, Michael R ^a   Colón Ramos, Daniel A ^a   Kornbluth, Sally ^a  

^a DUKE UNIVERSITY MEDICAL CENTER   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

APOPTOSIS INDUCING FACTOR; INHIBITOR OF APOPTOSIS PROTEIN; PROTEIN RPR; UBIQUITIN; UBIQUITIN PROTEIN LIGASE; UNCLASSIFIED DRUG;

AMINO TERMINAL SEQUENCE; ANIMAL CELL; APOPTOSIS; ARTICLE; CONTROLLED STUDY; ENZYME ACTIVITY; HUMAN; HUMAN CELL; NONHUMAN; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN FUNCTION; PROTEIN SYNTHESIS INHIBITION; TRANSLATION REGULATION;

ANIMALS; APOPTOSIS; CELL LINE; DROSOPHILA PROTEINS; HUMANS; INHIBITOR OF APOPTOSIS PROTEINS; KIDNEY; MOLECULAR SEQUENCE DATA; OOCYTES; PEPTIDES; PROTEIN BINDING; PROTEIN BIOSYNTHESIS; PROTEINS; TRANSFECTION; X-LINKED INHIBITOR OF APOPTOSIS PROTEIN; XENOPUS LAEVIS;

ANIMALIA; DROSOPHILA MELANOGASTER; INTRACISTERNAL A-PARTICLES; MAMMALIA; MELANOGASTER;

EID: 0036303143     PISSN: 14657392     EISSN: 14764679     Source Type: Journal    
DOI: 10.1038/ncb798     Document Type: Article

References (26)

1. Riedl, S. J. et al. Cell 104, 791–800 (2001).
2. Huang, Y. et al. Cell 104, 781–790 (2001).
3. Chai, J. et al. Cell 104, 769–780 (2001).
4. Yang, Y., Fang, S., Jensen, J. P., Weissman, A. M. & Ashwell, J. D. Science 288, 874–877 (2000).
5. Huang, H. et al. J. Biol. Chem. 275, 26661–26664 (2000).
6. White, K., et al. Science 264, 677–683 (1994).
7. Goyal, L., McCall, K., Agapite, J., Hartwieg, E. & Steller, H. EMBO J. 19, 589–597 (2000).
8. Wu, G. et al. Nature 408, 1008–1012 (2000).
9. Wu, J. W., Cocina, A. E., Chai, J., Hay, B. A. & Shi, Y. Mol. Cell 8, 95–104 (2001).
10. Verhagen, A. M. et al. Cell 102, 43–53 (2000).
11. Suzuki, Y. et al. Mol. Cell 8, 613–621 (2001).
12. Martins, L. M. et al. J. Biol. Chem. 277, 439–444 (2002).
13. Chen, P., Nordstrom, W., Gish, B. & Abrams, J. M. Genes Dev. 10, 1773–1782 (1996).
14. Grether, M. E., Abrams, J. M., Agapite, J., White, K. & Steller, H. Genes Dev. 9, 1694–1708 (1995).
15. Newmeyer, D. D., Farschon, D. M. and Reed J. C. Cell 79, 353–364 (1994).
16. Glotzer, M., Murray, A. & Kirschner, M. Nature 349, 132–138 (1991).
17. Avdonin, V. et al. Proc. Natl Acad. Sci. USA 95, 11703–11708 (1998).
18. Richter, B. W. & Duckett, C. S. Science STKE [online] (cited 8 August 2000) http://stke.sciencemag.org/cgi/content/full/OC_sigtrans;2000/44/pe1 (2000).
19. Clem, R. J. et al. J. Biol. Chem. 276, 7602–7608 (2001).
20. Deveraux, Q. L. et al. EMBO J. 18, 5242–5251 (1999).
21. Evans, E. K. et al. EMBO J. 16, 7372–7381 (1997).
22. Swenson, K. I., Jordan, J. R., Beyer, E. C. & Paul, D. L. Cell 57, 145–155 (1989).
23. Ryoo, H.D. et al. Nature Cell Biol. DOI:10.1038/ncb795.
24. Hays, R. et al. Nature Cell Biol. DOI:10.1038/ncb794.
25. Wing, J.P. et al. Nature Cell Biol. DOI:10.1038/ncb800.
26. Yoo, S.J. et al. Nature Cell Biol. DOI:10.1038/ncb793.