Death by design: Mechanism and control of apoptosis

Trends in Genetics

Volumn 15, Issue 12, 1999, Pages

  Song, Zhiwei ^a   Steller, Hermann ^a  

^a HOWARD HUGHES MEDICAL INSTITUTE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CASPASE; CYSTEINE PROTEINASE; PROTEIN BCL 2;

ACQUIRED IMMUNE DEFICIENCY SYNDROME; APOPTOSIS; CAENORHABDITIS ELEGANS; CANCER; CELL DEATH; CONTROL SYSTEM; DEGENERATIVE DISEASE; DEVELOPMENT; DROSOPHILA; GENE; HOMEOSTASIS; HUMAN; INSECT; MAMMAL; NONHUMAN; PRIORITY JOURNAL; PROTEIN FAMILY; REVIEW; STROKE;

EID: 0033437159     PISSN: 01689525     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0168-9525(99)01899-5     Document Type: Review

References (50)

1. Vaux D.L., Korsmeyer S.J. Cell death in development. Cell. 96:1999;245-254.
2. Rich Tet al. Apoptosis: the germs of death. Nat. Cell Biol. 1:1999;E69-E71.
3. Jacobson M.D. et al. Programmed cell death in animal development. Cell. 88:1997;347-354.
4. Thompson C.B. Apoptosis in the pathogenesis and treatment of disease. Science. 267:1995;1456-1462.
5. Ellis H.M., Horvitz H.R. Genetic control of programmed cell death in the nematode C. elegans. Cell. 44:1986;817-829.
6. Horvitz H.R. Genetic control of programmed cell death in the nematode Caenorhabditis elegans. Cancer Res. 59(Suppl.):1999;1701s-1706s.
7. Nicholson D.W., Thornberry N.A. Caspases: killer proteases. Trends Biochem. Sci. 22:1997;299-306.
8. Steller H. Mechanisms and genes of cellular suicide. Science. 267:1995;1445-1449.
9. Thornberry N.A., Lazebnik Y. Caspases: enemies within. Science. 281:1998;1312-1316.
10. Yuan J. et al. The C. elegans cell death gene ced-3 encodes a protein similar to mammalian interleukin-1β-converting enzyme. Cell. 75:1993;641-652.
11. Nagata S. Apoptosis by death factor. Cell. 88:1997;355-365.
12. Ashkenazi A., Dixit V.M. Death receptors: signaling and modulation. Science. 281:1998;1305-1308.
13. Li H. et al. Cleavage of BID by caspase 8 mediates the mitochondrial damage in the Fas pathway of apoptosis. Cell. 94:1998;491-501.
14. Luo X. et al. Bid, a Bcl2 interacting protein, mediates cytochrome c release from mitochondria in response to activation of cell surface death receptors. Cell. 94:1998;481-490.
15. Yuan J., Horvitz H.R. The Caenorhabditis elegans cell death gene ced-4 encodes a novel protein and is expressed during the period of extensive programmed cell death. Development. 116:1992;309-320.
16. Zou H. et al. Apaf-1, a human protein homologous to C. elegans CED-4, participates in cytochrome c-dependent activation of caspase-3. Cell. 90:1997;405-413.
17. Chinnaiyan A.M. et al. Interaction of CED-4 with CED-3 and CED-9: a molecular framework for cell death. Science. 275:1997;1122-1126.
18. Li P. et al. Cytochrome c and dATP-dependent formation of Apaf-1/Caspase-9 complex initiates an apoptotic protease cascade. Cell. 91:1997;479-489.
19. Liu X. et al. Induction of apoptotic program in cell-free extracts: requirement of dATP and cytochrome c. Cell. 86:1996;147-157.
20. Qin H. et al. Structural basis of procaspase-9 recruitment by the apoptotic protease-activating factor 1. Nature. 399:1999;549-557.
21. Hengartner M.O., Horvitz H.R. C. elegans cell survival gene ced-9 encodes a functional homolog of the mammalian proto-oncogene bcl-2. Cell. 76:1994;665-676.
22. White E. Life, death, and the pursuit of apoptosis. Genes Dev. 10:1996;1-15.
23. Vaux D.L., Korsmeyer S.J. Cell death in development. Cell. 96:1999;245-254.
24. Reed J.C. Double identity for proteins of the Bcl-2 family. Nature. 387:1997;773-776.
25. L regulates the membrane potential and volume homeostasis of mitochondria. Cell. 91:1997;627-637.
26. L forms an ion channel in synthetic lipid membranes. Nature. 385:1997;353-357.
27. Kluck R.M. et al. The release of cytochrome c from mitochondria: a primary site for Bcl-2 regulation of apoptosis. Science. 275:1997;1132-1136.
28. L inhibits Ara-C-induced mitochondrial loss of cytochrome c and other perturbations that activate the molecular cascade of apoptosis. Cancer Res. 57:1997;3115-3120.
29. Yang J. et al. Prevention of apoptosis by Bcl-2: release of cytochrome c from mitochondria blocked. Science. 275:1997;1129-1132.
30. Oltvai Z.N. et al. Bcl-2 heterodimerizes in vivo with a conserved homolog, Bax, that accelerates programmed cell death. Cell. 74:1993;609-619.
31. Conradt B., Horvitz H.R. The C. elegans protein EGL-1 is required for programmed cell death and interacts with the Bcl-2-like protein CED-9. Cell. 93:1998;519-529.
32. Uren A. et al. Conservation of baculovirus inhibitor of apoptosis repeat proteins (BIRs) in virus, nematodes, vertebrates and yeasts. Trends Biochem. Sci. 23:1998;159-162.
33. Miller L.K. An exegesis of IAPs: salvation and surprises from BIR motifs. Trends Cell Biol. 9:1999;323-328.
34. Fraser A.G. et al. Caenorhabditis elegans inhibitor of apoptosis protein (IAP) homologue BIR-1 plays a conserved role in cytokinesis. Curr. Biol. 9:1999;292-301.
35. Hawkins C.J. et al. A cloning method to identify caspases and their regulators in yeast: identification of Drosophila IAP1 as an inhibitor of the Drosophila caspase DCP-1. Proc. Natl. Acad. Sci. U. S. A. 96:1999;2885-2890.
36. Abrams J.M. An emerging blueprint for apoptosis in Drosophila. Trends Cell Biol. 9:1999;435-440.
37. Bergmann A. et al. The Drosophila gene hid is a direct molecular target of Ras-dependent survival signaling. Cell. 95:1998;331-341.
38. Kurada P., White K. Ras promotes cell survival in Drosophila by downregulating hid expression. Cell. 95:1998;319-329.
39. Wang S.L. et al. The Drosophila caspase inhibitor DIAP1 is essential for cell survival and is negatively regulated by HID. Cell. 98:1999;453-463.
40. Vucic D. et al. Inhibitor of apoptosis proteins physically interact with and block apoptosis induced by Drosophila proteins HID and GRIM. Mol. Cell. Biol. 18:1998;3300-3309.
41. Vucic D. et al. Inhibition of Reaper-induced apoptosis by interaction with inhibitor of apoptosis proteins (IAPs). Proc. Natl. Acad. Sci. U. S. A. 94:1997;10183-10188.
42. McCarthy J.V., Dixit V.M. Apoptosis induced by Drosophila Reaper and Grim in a human system. J. Biol. Chem. 23:1998;24009-24015.
43. Meier P., Evan G. Dying like flies. Cell. 95:1998;295-298.
44. Rich T. et al. Apoptosis: the germs of death. Nat. Cell Biol. 1:1999;69-71.
45. Rodriguez A. et al. Dark is a Drosophila homologue of Apaf-1/CED-4 and functions in an evolutionary conserved death pathway. Nat. Cell Biol. 1:1999;272-279.
46. Zhou L. et al. HAC-1, a Drosophila homolog of APAF-1 and CED-4 functions in developmental and radiation-induced apoptosis. Mol. Cell. 1999;. in press.
47. Evans E.K. et al. Reaper-induced apoptosis in a vertebrate system. EMBO J. 16:1997;7372-7381.
48. Claveria C. et al. Drosophila grim induces apoptosis in mammalian cells. EMBO J. 17:1998;7199-7208.
49. Haining W.N. et al. The proapoptotic function of Drosophila Hid is conserved in mammalian cells. Proc. Natl. Acad. Sci. U. S. A. 96:1999;4936-4941.
50. Hay B.A. et al. Drosophila homologs of baculovirus inhibitor of apoptosis proteins function to block cell death. Cell. 83:1995;1253-1262.