A biochemical analysis of the activation of the Drosophila caspase DRONC

Cell Death and Differentiation

Volumn 15, Issue 3, 2008, Pages 461-470

  Dorstyn, L ^a   Kumar, S ^a  

^a INSTITUTE OF MEDICAL AND VETERINARY SCIENCE   (Australia)

Author keywords

[No Author keywords available]

Indexed keywords

APOPTOTIC PROTEASE ACTIVATING FACTOR 1; CASPASE 2; CASPASE 9; CASPASE RECRUITMENT DOMAIN PROTEIN 15; DROSOPHILA PROTEIN; PROTEASOME INHIBITOR; PROTEIN DRONC; UNCLASSIFIED DRUG; VITRONECTIN;

ANIMAL CELL; APOPTOSIS; ARTICLE; BINDING AFFINITY; CATALYSIS; CELL DEATH; DIMERIZATION; DROSOPHILA; ENZYME ACTIVATION; ENZYME ACTIVITY; ENZYME INHIBITION; GEL FILTRATION CHROMATOGRAPHY; IMMUNOBLOTTING; MOLECULAR CLONING; MUTATIONAL ANALYSIS; NONHUMAN; OLIGOMERIZATION; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN BINDING; PROTEIN DEGRADATION; PROTEIN MOTIF; PROTEIN PROTEIN INTERACTION; RNA INTERFERENCE;

ANIMALS; APOPTOSIS; ASPARTIC ACID; CASPASES; DROSOPHILA; DROSOPHILA PROTEINS; ENZYME ACTIVATION; ENZYME PRECURSORS; GLUTAMIC ACID; INHIBITOR OF APOPTOSIS PROTEINS; MUTATION; RECOMBINANT PROTEINS;

MAMMALIA;

EID: 39449094293     PISSN: 13509047     EISSN: 14765403     Source Type: Journal    
DOI: 10.1038/sj.cdd.4402288     Document Type: Article

References (41)

1. Kumar S. Caspase function in programmed cell death. Cell Death Differ 2007; 14: 32-43.
2. Boatright KM, Salvesen GS. Mechanisms of caspase activation. Curr Opin Cell Biol 2003; 15: 725-731.
3. Walker NP, Talanian RV, Brady KD, Dang LG, Bump NJ, Ferenz CR et al Crystal structure of the cysteine protease interleukin-1 beta converting enzyme: A (p20/p10)2 homodimer. Cell 1994; 78: 343-352.
4. Wilson KR, Black JA, Thomson JA, Kim EE, Griffith JP, Navia MA et al Structure and mechanism of interleukin-1 beta converting enzyme. Nature 1994; 370: 270-275.
5. Rotonda J, Nicholson DW, Fazil KM, Gallant M, Gareau Y, Labelle M et al. The three-dimensional structure of apopain/CPP32, a key mediator of apoptosis. Nat Stuct Biol 1996; 3: 619-625.
6. Fuentes-Prior P, Salvesen GS. The protein structures that shape caspase activity, specificity, activation and inhibition. Biochem J 2004; 384: 201-232.
7. Saikumar P, Mikhailova M, Pandeswara SL. Regulation of caspase-9 activity by differential binding to the apoptosome complex. Front Biosci 2007; 12: 3343-3354.
8. Bao Q, Shi Y. Apoptosome: A platform for the activation of initiator caspases. Cell Death Differ 2007; 14: 56-65.
9. Timmer JC, Salvesen GS. Caspase substrates. Cell Death Differ 2007; 14: 66-72.
10. Wang X. The expanding role of mitochondria in apoptosis. Genes Dev 2001; 15: 2922-2933.
11. Rodriguez J, Lazebnik Y. Caspase-9 and APAF-1 form an active holoenzyme. Genes Dev 1999; 13: 3179-3184.
12. Zou H, Li Y, Liu X, Wang X. An APAF-1 cytochrome c multimeric complex is a functional apoptosome that activates procaspase-9. J Biol Chem 1999; 274: 11549-11556.
13. Guerrero AD, Chen M, Wang J. Delineation of the caspase-9 signaling cascade. Apoptosis 2007 in press (doi:10.1007/s10495-007-0139-8).
14. Stennicke HR, Deveraux QL, Humke EW, Reed JC, Dixit VM, Salvesen GS. Caspase-9 can be activated without proteolytic processing. J Biol Chem 1999; 274: 8359-8362.
15. Acehan D, Jiang X, Morgan DG, Heuser JE, Wang X, Akey CW. Three-dimensional structure of the apoptosome: Implications for assembly, procaspase-9 binding, and activation. Mol Cell 2002; 9: 423-432.
16. Pop C, Timmer J, Sperandio S, Salvesen GS. The apoptosome activates caspase-9 by dimerization. Mol Cell 2006; 22: 269-275.
17. Yin Q, Park HH, Chung JY, Lin SC, Lo YC, da Graca LS et al. Caspase-9 holoenzyme is a specific and optimal procaspase-3 processing machine. Mol Cell 2006; 22: 259-268.
18. Chao Y, Shiozaki EN, Srinivasula SM, Rigotti DJ, Fairman R, Shi Y. Engineering a dimeric caspase-9: A re-evaluation of the induced proximity model for caspase activation. PLoS Biol 2005; 3: e183.
19. Denault JB, Eckelman BP, Shin H, Pop C, Salvesen GS. Caspase 3 attenuates XIAP (X-linked inhibitor of apoptosis protein)-mediated inhibition of caspase 9. Biochem J 2007; 405: 11-19.
20. Bratton SB, Walker G, Srinivasula SM, Sun XM, Butterworth M, Alnemri ES et al. Recruitment, activation and retention of caspases-9 and -3 by Apaf-1 apoptosome and associated XIAP complexes. EMBO J 2001; 20: 998-1009.
21. Daish TJ, Mills K, Kumar S. Drosophila caspase DRONC is required for specific developmental cell death pathways and stress-induced apoptosis. Dev Cell 2004; 7: 909-915.
22. Chew SK, Akdemir F, Chen P, Lu WJ, Mills K, Daish T et al. The apical caspase dronc governs programmed and unprogrammed cell death in Drosophila. Dev Cell 2004; 7: 897-907.
23. Mills K, Daish T, Kulmar S. The function of the Drosophila caspase DRONC in cell death and development. Cell Cycle 2005; 4: 744-746.
24. Waldhuber M, Emoto K, Petritsch C. The Drosophila caspase DRONC is required for metamorphosis and cell death in response to irradiation and developmental signals. Mech Dev 2005; 122: 914-927.
25. Xu D, Li Y, Arcaro M, Lackey M, Bergmann A. The CARD-carrying caspase Dronc is essential for most, but not all, developmental cell death in Drosophila. Development 2005; 132: 2125-2134.
26. Dorstyn L, Read S, Cakouros D, Huh JR, Hay BA, Kumar S. The role of cytochrome c in caspase activation in Drosophila melanogaster cells. J Cell Biol 2002; 156: 1089-1098.
27. Zimmermann KC, Ricci JE, Droin NM, Green DR. The role of ARK in stress-induced apoptosis in Drosophila cells. J. Cell Biol 2002; 156: 1077-1087.
28. Mills K, Daish T, Harvey KF, Pfleger CM, Hariharan IK, Kumar S. The Drosophila melanogaster Apaf-1 homologue ARK is required for most, but not all, programmed cell death. J Cell Biol 2006; 172: 809-815.
29. Yu X, Wang L, Acehan D, Wang X, Akey CW. Three-dimensional structure of a double apoptosome formed by the Drosophila Apaf-1 related killer. J Mol Biol 2006; 355: 577-589.
30. Yan N, Huh JR, Schirf V, Demeler B, Hay BA, Shi Y. Structure and activation mechanism of the Drosophila initiator caspase Dronc. J Biol Chem 2006; 281: 8667-8674.
31. Hawkins CJ, Yoo SJ, Peterson EP, Wang SL, Vemooy SY, Hay BA. The Drosophila caspase DRONC cleaves following glutamate or aspartate and is regulated by DIAP1, HID, and GRIM. J Biol Chem 2000; 275: 27084-27093.
32. Muro I, Monser K, Clem RJ. Mechanism of Dronc activation in Drosophila cells. J Cell Sci 2004; 117: 5035-5041.
33. Meier P, Silke J, Leevers SJ, Evan GI. The Drosophila caspase DRONC is regulated by DIAP1. EMBO J 2000; 19: 598-611.
34. Muro I, Hay BA, Clem RJ. The Drosophila DIAP1 protein is required to prevent accumulation of a continuously generated, processed form of the apical caspase DRONC. J Biol Chem 2002; 277: 49644-49650.
35. Yoo SJ, Huh JR, Muro I, Yu H, Wang L, Wang SL et al. Hid, Rpr and Grim negatively regulate DIAP1 levels through distinct mechanism. Nat Cell Biol 2002; 4: 416-424.
36. Halley CL, Olson MR, Colon-Ramos DA, Kornbluth S. Reaper eliminates IAP proteins through stimulated IAP degradation and generalized translational inhibition. Nat Cell Biol 2002; 4: 439-444.
37. Muro I, Means JC, Clem RJ. Cleavage of the apoptosis inhibitor DIAP1 by the apical caspase DRONC in both normal and apoptotic Drosophila cells. J Biol Chem 2005; 280: 18683-18688.
38. Baliga BC, Read SH, Kumar S. The biochemical mechanism of caspase-2 activation. Cell Death Differ 2004; 11: 1234-1241.
39. Dorstyn L, Colussi PA, Quinn LM, Richardson H, Kumar S. DRONC, an ecdysone-inducible Drosophila caspase. Proc Natl Acad Sci USA 1999; 96: 4307-4312.
40. Yan N, Wu JW, Chai J, Li W, Shi Y. Molecular mechanisms of DrICE inhibition by DIAP1 and removal of inhibition by Reaper, Hid and Grim. Nat Struct Mol Biol 2004; 11: 420-428.
41. Renatus M, Stennicke HR, Scott FL, Liddington RC, Salvesen GS. Dimer formation drives the activation of the cell death protease caspase 9. Proc Natl Acad Sci US4 2001; 98: 14250-14255.