Molecular mechanisms of DrICE inhibition by DIAP1 and removal of inhibition by Reaper, Hid and Grim

Nature Structural and Molecular Biology

Volumn 11, Issue 5, 2004, Pages 420-428

  Yan, Nieng ^a   Wu, Jia Wei ^b   Chai, Jijie ^a   Li, Wenyu ^a   Shi, Yigong ^a  

^a PRINCETON UNIVERSITY   (United States)

^b TSINGHUA UNIVERSITY   (China)

Author keywords

[No Author keywords available]

Indexed keywords

CASPASE; HEAD INVOLUTION DEFECTIVE PROTEIN; PROTEIN; PROTEIN DIAP1; PROTEIN GRIM; PROTEIN REAPER; UNCLASSIFIED DRUG;

AMINO TERMINAL SEQUENCE; APOPTOSIS; ARTICLE; CATALYSIS; DROSOPHILA MELANOGASTER; ENZYME ACTIVITY; ENZYME DEGRADATION; ENZYME INHIBITION; MOLECULAR BIOLOGY; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DEGRADATION; PROTEIN DOMAIN; PROTEIN FUNCTION; PROTEIN MOTIF;

ANIMALS; CASPASES; DROSOPHILA MELANOGASTER; DROSOPHILA PROTEINS; INHIBITOR OF APOPTOSIS PROTEINS; MODELS, MOLECULAR; MUTATION; NEUROPEPTIDES; PROTEIN CONFORMATION;

DROSOPHILA MELANOGASTER; MELANOGASTER;

EID: 2342617566     PISSN: 15459993     EISSN: None     Source Type: Journal    
DOI: 10.1038/nsmb764     Document Type: Article

References (41)

1. Shi, Y. Mechanisms of caspase inhibition and activation during apoptosis. Mol. Cell 9, 459-470 (2002).
2. Thornberry, N.A. & Lazebnik, Y. Caspases: Enemies within. Science 281, 1312-1316 (1998).
3. Deveraux, Q.L. & Reed, J.C. IAP family proteins-suppressors of apoptosis. Genes Dev. 13, 239-252 (1999).
4. Salvesen, G.S. & Duckett, C.S. IAP proteins: blocking the road to death's door. Nat. Rev. Mol. Cell Biol. 3, 401-410 (2002).
5. Hay, B.A., Wassarman, D.A. & Rubin, G.M. D. melanogaster homologs of baculoviral inhibitor of apoptosis proteins function to block cell death. Cell 83, 1253-1262 (1995).
6. Shi, Y. A conserved tetrapeptide motif: Potentiating apoptosis through IAP-binding. Cell Death Differ. 9, 93-95 (2002).
7. Shiozaki, E.N. et al. Mechanism of XIAP-mediated inhibition of caspase-9. Mol. Cell 11, 519-527 (2003).
8. Srinivasula, S.M. et al. A conserved XIAP-interaction motif in caspase-9 and Smac/DIABLO mediates opposing effects on caspase activity and apoptosis. Nature 409, 112-116 (2001).
9. Chai, J. et al. Structural and biochemical basis of apoptotic activation by Smac/DIABLO. Nature 406, 855-862 (2000).
10. Wu, G. et al. Structural basis of IAP recognition by Smac/DIABLO. Nature 408, 1008-1012 (2000).
11. Liu, Z. et al. Structural basis for binding of Smac/DIABLO to the XIAP BIR3 domain. Nature 408, 1004-1008 (2000).
12. Chai, J. et al. Structural basis of caspase-7 inhibition by XIAP. Cell 104, 769-780 (2001).
13. Huang, Y. et al. Structural basis of caspase inhibition by XIAP: differential roles of the linker versus the BIR domain. Cell 104, 781-790 (2001).
14. Riedl, S.J. et al. Structural basis for the inhibition of caspase-3 by XIAP. Cell 104, 791-800 (2001).
15. Chai, J. et al. Molecular mechanism of Reaper/Grim/Hid-mediated suppression of DIAP1-dependent Dronc ubiquitination. Nat. Struct. Biol. 10, 892-898 (2003).
16. Wilson, R. et al. The DIAP1 RING finger mediates ubiquitination of Dronc and is indispensable for regulating apoptosis. Nat. Cell Biol. 4, 445-450 (2002).
17. Fraser, A.G. & Evan, G.I. Identification of a D. melanogaster ICE/CED-3-related protease, drICE. EMBO J. 16, 2805-2813 (1997).
18. Fraser, A.G., McCarthy, N.J. & Evan, G.I. drICE is an essential caspase required for apoptotic activity in D. melanogaster cells. EMBO J. 16, 6192-6199 (1997).
19. Hawkins, C.J. et al. The D. melanogaster caspase DRONC cleaves following glutamate or aspartate and is regulated by DIAP1, HID, and GRIM. J. Biol. Chem. 275, 27084-27093 (2000).
20. Meier, P., Silke, J., Leevers, S.J. & Evan, G.I. The D. melanogaster caspase DRONC is regulated by DIAP1. EMBO J. 19, 598-611 (2000).
21. Kaiser, W., Vucic, D. & Miller, L. The D. melanogaster inhibitor of apoptosis DIAP1 suppresses cell death induced by the caspase drICE. FEBS Lett. 440, 243-248 (1998).
22. Goyal, L., McCall, K., Agapite, J., Hartwieg, E. & Steller, H. Induction of apoptosis by D. melanogaster reaper, hid and grim through inhibition of IAP function. EMBO J. 19, 589-597 (2000).
23. Wang, S., Hawkins, C., Yoo, S., Muller, H.-A. & Hay, B. The D. melanogaster caspase inhibitor DIAP1 is essential for cell survival and is negatively regulated by HID. Cell 98, 453-463 (1999).
24. Lisi, S., Mazzon, I. & White, K. Diverse domains of THREAD/DIAP1 are required to inhibit apoptosis induced by REAPER and HID in D. melanogaster. Genetics 154, 669-678 (2000).
25. Vucic, D., Kaiser, W.J. & Miller, L.K. Inhibitor of apoptosis proteins physically interact with and block apoptosis induced by D. melanogaster proteins HID and GRIM. Mol. Cell. Biol. 18, 3300-3309 (1998).
26. Song, Z. et al. Biochemical and genetic interactions between D. melanogaster caspases and the proapoptotic genes rpr, hid, and grim. Mol. Cell Biol. 20, 2907-2914 (2000).
27. Hawkins, C., Wang, S. & Hay, B.A. A cloning method to identify caspases and their regulators in yeast: identification of D. melanogaster IAP1 as an inhibitor of the D. melanogaster caspase DCP-1. Proc. Natl. Acad. Sci. USA 96, 2885-2890 (1999).
28. Vucic, D., Kaiser, W.J., Harvey, A.J. & Miller, L.K. Inhibition of reaper-induced apoptosis by interaction with inhibitor of apoptosis proteins (IAPs). Proc. Natl. Acad. Sci. USA 94, 10183-10188 (1997).
29. Dorstyn, L., Colussi, P.A., Quinn, L.M., Richardson, H. & Kumar, S. DRONC, an ecdysone-inducible D. melanogaster caspase. Proc. Natl. Acad. Sci. USA 96, 4307-4312 (1999).
30. Sun, C. et al. NMR structure and mutagenesis of the third BIR domain of the inhibitor of apoptosis protein XIAP. J. Biol. Chem. 275, 33777-33781 (2000).
31. Fesik, S.W. Insights into programmed cell death through structural biology. Cell 103, 273-282 (2000).
32. Wu, J.-W., Cocina, A.E., Chai, J., Hay, B.A. & Shi, Y. Structural analysis of a functional DIAP1 fragment bound to Grim and Hid peptides. Mol. Cell 8, 95-104 (2001).
33. Vernooy, S.Y. et al. Cell death regulation in D. melanogaster: conservation of mechanism and unique insights. J. Cell Biol. 150, F69-F76 (2000).
34. Ditzel, M. et al. Degradation of DIAP1 by the N-end rule pathway is essential for regulating apoptosis. Nat. Cell Biol. 5, 467-473 (2003).
35. Zachariou, A. et al. IAP-antagonists exhibit non-redundant modes of action through differential DIAP1 binding. EMBO J. 22, 6642-6652 (2003).
36. Chai, J. et al. Crystal Structure of a procaspase-7 zymogen: mechanisms of activation and substrate binding. Cell 107, 399-407 (2001).
37. Otwinowski, Z. & Minor, W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307-326 (1997).
38. Navaza, J. AMoRe and automated package for molecular replacement. Acta Crystallogr. A 50, 157-163 (1994).
39. Jones, T.A., Zou, J.-Y., Cowan, S.W. & Kjeldgaard, M. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A 47, 110-119 (1991).
40. Terwilliger, T.C. & Berendzen, J. Correlated phasing of multiple isomorphous replacement data. Acta Crystallogr. D 52, 749-757 (1996).
41. Kraulis, P.J. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24, 946-950 (1991).