Molecular characterization of mitochodrial apoptosis-inducing factor

Nature

Volumn 397, Issue 6718, 1999, Pages 441-446

  Susin, Santos A ^a   Lorenzo, Hans K ^b   Zamzami, Naoufal ^a   Marzo, Isabel ^a   Snow, Bryan E ^c   Brothers, Greg M ^c   Mangion, Joan ^c   Jacotot, Etienne ^a   Costantini, Paola ^a   Loeffler, Markus ^a   Larochette, Nathanael ^a   Goodlett, David R ^d   Aebersold, Ruedi ^d   Siderovski, David P ^c   Penninger, Josef M ^c   Kroemer, Guido ^a  

^a CNRS   (France)

^b INSTITUT PASTEUR   (France)

^c AMGEN INSTITUTE   (Canada)

^d UNIVERSITY OF WASHINGTON   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

DNA FRAGMENT; FLAVOPROTEIN; ANTIBODY; APOPTOSIS INDUCING FACTOR; CYTOCHROME C; MEMBRANE PROTEIN; PDCD8 PROTEIN, HUMAN; PDCD8 PROTEIN, MOUSE; PDCD8 PROTEIN, RAT; PROTEIN BCL 2; RECOMBINANT PROTEIN;

APOPTOSIS; ARTICLE; CHROMATIN CONDENSATION; HUMAN; MEMBRANE PERMEABILITY; MITOCHONDRION; MOLECULAR CLONING; MOUSE; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN PURIFICATION; SEQUENCE ANALYSIS; AMINO ACID SEQUENCE; ANIMAL; CELL FREE SYSTEM; CELL LINE; CELL NUCLEUS; CHROMATIN; GENETICS; HELA CELL; IMMUNOLOGY; INTRACELLULAR MEMBRANE; ISOLATION AND PURIFICATION; MICROINJECTION; MOLECULAR GENETICS; PHYSIOLOGY; RAT;

BACTERIA (MICROORGANISMS);

AMINO ACID SEQUENCE; ANIMALS; ANTIBODIES; APOPTOSIS; APOPTOSIS INDUCING FACTOR; CELL LINE; CELL NUCLEUS; CELL-FREE SYSTEM; CHROMATIN; CYTOCHROME C GROUP; FLAVOPROTEINS; HELA CELLS; HUMANS; INTRACELLULAR MEMBRANES; MEMBRANE PROTEINS; MICE; MICROINJECTIONS; MITOCHONDRIA; MOLECULAR SEQUENCE DATA; PROTO-ONCOGENE PROTEINS C-BCL-2; RATS; RECOMBINANT PROTEINS;

EID: 0033521741     PISSN: 00280836     EISSN: None     Source Type: Journal    
DOI: 10.1038/17135     Document Type: Article

References (30)

1. Kroemer, G. The proto-oncogene Bcl-2 and its role in regulating apoptosis. Nature Med. 3, 614-620 (1997).
2. Green, D. R. & Reed, J. C. Mitochondria and apoptosis. Science 281, 1309-1312 (1998).
3. Zamzami, N. et al. Mitochondrial control of nuclear apoptosis. J. Exp. Med. 183, 1533-1544 (1996).
4. Liu, X. S., Kim, C. N., Yang, J., Jemmerson, R. & Wang, X. Induction of apoptotic program in cell-free extracts: requirement for dATP and cytochrome c. Cell 86, 147-157 (1996).
5. Susin, S. A. et al. Bcl-2 inhibits the mitochondrial release of an apoptogenic protease. J. Exp. Med. 184, 1331-1342 (1996).
6. Kluck, R. M., Bossy-Wetzel, E., Green, D. R. & Newmeyer, D. D. The release of cytochrome c from mitochondria: a primary site for Bcl-2 regulation of apoptosis. Science 275, 1132-1136 (1997).
7. Vander Heiden, M. G., Chandal, N. S., Williamson, E. K., Schumacker, P. T. & Thompson, C. B. Bcl-XL regulates the membrane potential and volume homeostasis of mitochondria. Cell 91, 627-637 (1997).
8. Mancini, M. et al. The caspase-3 precursor has a cytosolic and mitochondrial distribution: Implications for apoptotic signaling. J. Cell Biol. 140, 1485-1495 (1998).
9. Susin, S. A. et al Mitochondrial release of caspases-2 and -9 during the apoptotic process, J. Exp. Med. 189, 381-394 (1999).
10. Ducret, A., Van Ostveen, I., Eng, J. K., Yates, J. R. & Aebersold, R. High-throughput protein characterization by automated reverse-phase chromatography electrospray tandem mass spectrometry. Protein Sci. 7, 706-719 (1998).
11. Claros, M. G. & Vincens, P. Computation method to predict mitochondrially imported proteins and their targeting sequences. Eur. J. Biochem. 241, 779-786 (1996).
12. Cedano, J., Aloy, P., Perez-Pons, J. A. & Quero, E. Relation between amino acid composition and cellular location of proteins. J. Mol. Biol. 266, 594-600 (1997).
13. Boulikas, T. Nuclear localization signals (NLS). Crit. Rev. Euk. Gene Exp. 3, 193-227 (1993).
14. Li, P. et al. Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apopotic protease cascade. Cell 91, 479-489 (1997).
15. Yasuhara, N. et al. Essential role of active nuclear transport in apoptosis. Genes to Cells 2, 55-64 (1997).
16. Enari, M. et al. A caspase-activated DNase that degrades DNA during apoptosis, and its inhibitor ICAD. Nature 391, 43-50 (1998).
17. Scaffidi, C. et al. Two CD95 (APO-1/Fas) signalling pathways. EMBO J. 17, 1675-1687 (1998).
18. Kluck, R. M. et al. Cytochrome c activation of CPP32-like proteolysis plays a critical role in a Xenopus cell-free apoptosis system. EMBO J. 16, 4639-4649 (1997).
19. Robinson, K. M. & Lemire, B. D. A requirement for matrix processing peptidase but not for mitochondrial chaperonin in the covalent attachment of FAD to yeast succinate dehydrogenase flavoprotein. J. Biol. Chem. 271, 4061-4067 (1996).
20. Liu, X., Zou, H., Slaughter, C. & Wang, X. DFF, a heterodimeric protein that functions downstream of caspase 3 to trigger DNA fragmentation during apoptosis. Cell 89, 175-184 (1997).
21. Samejima, K. et al. Transition from caspase-dependent to caspase-independent mechanisms at the onset of apoptotic execution.J. Cell Biol. 143, 225-239 (1998).
22. Oberhammer, F. et al. Apoptotic death in epithelial cells: cleavage of DNA to 300 and/or 50 kb fragments prior to or in the absence of internucleosomal fragmentation. EMBO J. 12, 3679-3684 (1993).
23. Lagarkova, M. A., Iarvaia, O. V. & Razin, S. V. Large-scale fragmentation of mammalian DNA in the course of apoptosis proceeds via excision of chromosomal DNA loops and their oligomers. J. Biol. Chem. 270, 20239-20241 (1995).
24. Trbovich, A. M. et al. High and low molecular weight DNA cleavage in ovarian granulosa cells: characterization and protease modulation in intact cells and in cell-free nuclear autodigestion assays. Cell Death Differ. 5, 38-49 (1998).
25. Susin, S. A. et al. The central executioner of apoptosis. Multiple links between protease activation and mitochondria in Fas/Apo-1/CD95- and ceramide-induced apoptosis. J. Exp. Med. 186, 25-37 (1997).
26. Bossy-Wetzel, E., Newmeyer, D. D. & Green, D. R. Mitochondrial cytochrome c release in apoptosis occurs upstream of DEVD-specific caspase activation and independently of mitochondrial trans-membrane depolarization. EMBO J. 17, 37-49 (1998).
27. Marzo, I. et al. Bax and adenine nucleotide translocator cooperate in the mitochondrial control of apoptosis. Science 281, 2027-2031 (1998).
28. Enari, M., Hase, A. & Nagata, S. Apoptosis by a cytosolic extract from Fas-activated cells. EMBO J. 14, 5201-5208 (1995).
29. Wada, J. & Kanwar, Y. S. Characterization of mammalian translocase of inner mitochondrial membrane (Tim44) isolated from diabetic newborn mouse kidney. Proc. Natl Acad. Sci. USA 95, 144-149 (1998).
30. Zhu, W. et al. Bcl-2 mutants with restricted subcellular localization reveal spatially distinct pathways for apoptosis in different cell types. EMBO J. 15, 4130-4141 (1996).