Signal-dependent protection from apoptosis in mice expressing caspase-resistant Rb

Nature Cell Biology

Volumn 4, Issue 10, 2002, Pages 757-765

  Chau, B Nelson ^a   Borges, Helena Lobo ^a   Chen, Tung Ti ^b   Marselli, Anja ^a   Hunton, Irina C ^a   Wang, Jean Y J ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b AmProx Incorporated   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CASPASE; CASPASE 3; CYTOCHROME C; RETINOBLASTOMA PROTEIN; TUMOR NECROSIS FACTOR ALPHA RECEPTOR;

ALLELE; ANIMAL CELL; ANIMAL EXPERIMENT; ANIMAL TISSUE; APOPTOSIS; ARTICLE; CARBOXY TERMINAL SEQUENCE; CELL DEATH; CELL PROTECTION; CONTROLLED STUDY; DNA DAMAGE; EMBRYO; ENZYME ACTIVATION; FEMALE; FIBROBLAST; GENE EXPRESSION; GERM LINE; INTESTINE; MALE; MOUSE; MUTATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN EXPRESSION; PROTEIN SECRETION; SEPTIC SHOCK; SIGNAL TRANSDUCTION; SPLEEN; SURVIVAL;

3T3 CELLS; ALLELES; ANIMALS; ANIMALS, NEWBORN; ANTIGENS, CD; APOPTOSIS; CASPASE 3; CASPASES; CYTOCHROME C GROUP; EUKARYOTIC CELLS; FIBROBLASTS; GENE EXPRESSION REGULATION; LIPOPOLYSACCHARIDES; MICE; MICE, KNOCKOUT; MUTATION; RECEPTORS, TUMOR NECROSIS FACTOR; RECEPTORS, TUMOR NECROSIS FACTOR, TYPE I; RECEPTORS, TUMOR NECROSIS FACTOR, TYPE II; RETINA; RETINOBLASTOMA PROTEIN; SHOCK, SEPTIC; SIGNAL TRANSDUCTION; TOXINS, BIOLOGICAL; TUMOR NECROSIS FACTOR-ALPHA;

ANIMALIA; MURINAE;

EID: 0036800351     PISSN: 14657392     EISSN: None     Source Type: Journal    
DOI: 10.1038/ncb853     Document Type: Article

References (45)

1. Cryns, V. & Yuan, J. Proteases to die for. Genes Dev. 12, 1551-1570 (1998).
2. Budihardjo, I., Oliver, H., Lutter, M., Luo, X. & Wang, X. Biochemical pathways of caspase activation during apoptosis. Annu. Rev. Cell. Dev. Biol. 15, 269-290 (1999).
3. Wolf, B. B. & Green, D. R. Suicidal tendencies: apoptotic cell death by caspase family proteinases. J. Biol. Chem. 274, 20049-20052 (1999).
4. Clem, R. J. et al. c-IAP1 is cleaved by caspases to produce a proapoptotic C-terminal fragment. J. Biol. Chem. 276, 7602-7608 (2001).
5. L through caspase interaction. Proc. Natl Acad. Sci. USA 95, 554-559 (1998).
6. Luo, X., Budihardjo, L, Zou, H., Slaughter, C. & Wang, X. Bid, a Bcl2 interacting protein, mediates cytochrome c release from mitochondria in response to activation of cell surface death receptors. Cell 94, 481-490 (1998).
7. Li, H., Zhu, H., Xu, C. J. & Yuan, J. Cleavage of BID by caspase 8 mediates the mitochondrial damage in the Fas pathway of apoptosis. Cell 94, 491-501 (1998).
8. Srinivasula, S. M. et al. The Ced-3/interleukin 1β converting enzyme-like homolog Mch6 and the lamin-cleaving enzyme Mch2α are substrates for the apoptotic mediator CPP32. J. Biol. Chem. 271, 27099-27106 (1996).
9. Janicke, R. U., Ng, P., Sprengart, M. L. & Porter, A. G. Caspase-3 is required for α-fodrin cleavage but dispensable for cleavage of other death substrates in apoptosis. J. Biol. Chem. 273, 15540-15545 (1998).
10. Janicke, R. U., Walker, P. A., Lin, X. Y. & Porter, A. G. Specific cleavage of the retinoblastoma protein by an ICE-like protease in apoptosis. EMBO J. 15, 6969-6978 (1996).
11. Tan, X., Martin, S. J., Green, D. R. & Wang, J. Y. Degradation of retinoblastoma protein in tumor necrosis factor- and CD95-induced cell death. J. Biol. Chem. 272, 9613-9616 (1997).
12. An, B. & Dou, Q. P. Cleavage of retinoblastoma protein during apoptosis: an interleukin 1 beta-converting enzyme-like protease as candidate. Cancer Res. 56, 438-442 (1996).
13. Harbour, J. W. & Dean, D. C. The Rb/E2F pathway: expanding roles and emerging paradigms. Genes Dev. 14, 2393-2409 (2000).
14. Jacks, T. et al. Effects of an Rb mutation in the mouse. Nature 359, 295-300 (1992).
15. Clarke, A. R. et al. Requirement for a functional Rb-1 gene in murine development. Nature 359, 328-330 (1992).
16. Lee, E. Y. et al. Mice deficient for Rb are nonviable and show defects in neurogenesis and haematopoiesis. Nature 359, 288-294 (1992).
17. Almasan, A. et al. Deficiency of retinoblastoma protein leads to inappropriate S-phase entry, activation of E2F-responsive genes, and apoptosis. Proc. Natl Acad. Sci. USA 92, 5436-5440 (1995).
18. Phillips, A. C., Ernst, M. K., Bates, S., Rice, N. R. & Vousden, K. H. E2F-1 potentiates cell death by blocking antiapoptotic signaling pathways. Mol. Cell 4, 771-781 (1999).
19. Tan, X. & Wang, J. Y. The caspase-Rb connection in cell death. Trends Cell Biol. 8, 116-120 (1998).
20. Boutillier, A. L., Trinh, E. & Loeffler, J. P. Caspase-dependent cleavage of the retinoblastoma protein is an early step in neuronal apoptosis. Oncogene 19, 2171-2178 (2000).
21. Deng, C., Zhang, P., Harper, J. W., Elledge, S. J. & Leder, P. Mice lacking p21CIP1/WAF1 undergo normal development, but are defective in G1 checkpoint control. Cell 82, 675-684 (1995).
22. Hu, N. et al. Heterozygous Rb-1Δ20/+ mice are predisposed to tumors of the pituitary gland with a nearly complete penetrance. Oncogene 9, 1021-1027 (1994).
23. Pfeffer, K. et al. Mice deficient for the 55 kD tumor necrosis factor receptor are resistant to endotoxic shock, yet succumb to L. monocytogenes infection. Cell 73, 457-467 (1993).
24. Piguet, P. F., Vesin, C., Guo, J., Donati, Y. & Barazzone, C. TNF-induced enterocytes apoptosis in mice is mediated by TNF receptor I and does not require p53. Eur. J. Immunol. 28, 3499-3505 (1998).
25. Borges, H. L. & Linden, R. Gamma irradiation leads to two waves of apoptosis in distinct cell populations of the retina of newborn rats. J. Cell Sci. 112, 4315-4324 (1999).
26. Rehen, S. K., Varella, M. H., Freitas, F. G., Moraes, M. O. & Linden, R. Contrasting effects of protein synthesis inhibition and of cyclic AMP on apoptosis in the developing retina. Development 122, 1439-1448 (1996).
27. Lewis, M. et al. Cloning and expression of cDNAs for two distinct murine tumor necrosis factor receptors demonstrate one receptor is species specific. Proc. Natl Acad. Sci. USA 88, 2830-2834 (1991).
28. Acehan, D. et al. Three-dimensional structure of the apoptosome: implications for assembly, pro-caspase-9 binding, and activation. Mol. Cell 9, 423-432 (2002).
29. Wang, X. The expanding role of mitochondria in apoptosis. Genes Dev. 15, 2922-2933 (2001).
30. Du, C., Fang, M., Li, Y., Li, L. & Wang, X. Smac, a mitochondrial protein that promotes cytochrome c-dependent caspase activation by eliminating IAP inhibition. Cell 102, 33-42 (2000).
31. Martins, L. M. et al. The serine protease Omi/HtrA2 regulates apoptosis by binding XIAP through a reaper-like motif. J. Biol. Chem. 277, 439-444 (2002).
32. Hegde, R. et al. Identification of Omi/HtrA2 as a mitochondrial apoptotic serine protease that disrupts inhibitor of apoptosis protein-caspase interaction. J. Biol. Chem. 277, 432-438 (2002).
33. 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. 274, 11549-11556 (1999).
34. Goldstein, J. C., Waterhouse, N. J., Juin, P., Evan, G. I. & Green, D. R. The coordinate release of cytochrome c during apoptosis is rapid, complete and kinetically invariant. Nature Cell Biol. 2, 156-162 (2000).
35. Wallach, D. et al. Tumor necrosis factor receptor and Fas signaling mechanisms. Annu. Rev. Immunol. 17, 331-367 (1999).
36. Li, K. et al. Cytochrome c deficiency causes embryonic lethality and attenuates stress-induced apoptosis. Cell 101, 389-399 (2000).
37. Erickson, S. L. et al. Decreased sensitivity to tumour-necrosis factor but normal T-cell development in TNF receptor-2-deficient mice. Nature 372, 560-563 (1994).
38. Jupp, O. J. et al. Type II tumour necrosis factor-α receptor (TNFR2) activates c-Jun N- terminal kinase (JNK) but not mitogen-activated protein kinase (MAPK) or p38 MAPK pathways. Biochem. J. 359, 525-535. (2001).
39. Macleod, K. F., Hu, Y. & Jacks, T. Loss of Rb activates both p53-dependent and independent cell death pathways in the developing mouse nervous system. EMBO J. 15, 6178-6188 (1996).
40. Tsai, K. Y. et al. Mutation of E2f-1 suppresses apoptosis and inappropriate S phase entry and extends survival of Rb-deficient mouse embryos. Mol. Cell 2, 293-304 (1998).
41. Moroni, M. C. et al. Apaf-1 is a transcriptional target for E2F and p53. Nature Cell Biol. 3, 552-558 (2001).
42. Muller, H. et al. E2Fs regulate the expression of genes involved in differentiation, development, proliferation, and apoptosis. Genes Dev. 15, 267-285 (2001).
43. Guo, Z., Yikang, S., Yoshida, H., Mak, T. W. & Zacksenhaus, E. Inactivation of the retinoblastoma tumor suppressor induces apoptosis protease-activating factor-1 dependent and independent apoptotic pathways during embryogenesis. Cancer Res. 61, 8395-8400 (2001).
44. Simpson, M. T. et al. Caspase 3 deficiency rescues peripheral nervous system defect in retinoblastoma nullizygous mice. J. Neurosci. 21, 7089-7098 (2001).
45. Morris, E. J. & Dyson, N. J. Retinoblastoma protein partners. Adv. Cancer Res. 82, 1-54 (2001).