메뉴 건너뛰기




Volumn 22, Issue 17, 2003, Pages 4385-4399

Mitochondrial release of AIF and EndoG requires caspase activation downstream of Bax/Bak-mediated permeabilization

Author keywords

AIF; Cytochrome c; Diablo; EndoG; HtrA2; Omi; Smac

Indexed keywords

APOPTOSIS INDUCING FACTOR; APOPTOTIC PROTEASE ACTIVATING FACTOR 1; BENZYLOXYCARBONYLVALYLALANYLASPARTYL FLUOROMETHYL KETONE; CASPASE; CYTOCHROME C; ENDONUCLEASE G; PROTEIN BAK; PROTEIN BAX; PROTEIN BCL 2; SECOND MITOCHONDRIAL ACTIVATOR OF CASPASE; SERINE PROTEINASE OMI; UNCLASSIFIED DRUG;

EID: 0042237031     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/cdg423     Document Type: Article
Times cited : (395)

References (52)
  • 1
    • 0035803568 scopus 로고    scopus 로고
    • Apoptosis-associated release of Smac/DIABLO from mitochondria requires active caspases and is blocked by Bcl-2
    • Adrain, C., Creagh, E.M. and Martin, S.J. (2001) Apoptosis-associated release of Smac/DIABLO from mitochondria requires active caspases and is blocked by Bcl-2. EMBO J., 20, 6627-6636.
    • (2001) EMBO J. , vol.20 , pp. 6627-6636
    • Adrain, C.1    Creagh, E.M.2    Martin, S.J.3
  • 2
    • 0034650523 scopus 로고    scopus 로고
    • Bax oligomerization is required for channel-forming activity in liposomes and to trigger cytochrome c release from mitochondria
    • Antonsson, B., Montessuit, S., Lauper, S., Eskes, R. and Martinou, J.C. (2000) Bax oligomerization is required for channel-forming activity in liposomes and to trigger cytochrome c release from mitochondria. Biochem. J., 345, 271-278.
    • (2000) Biochem. J. , vol.345 , pp. 271-278
    • Antonsson, B.1    Montessuit, S.2    Lauper, S.3    Eskes, R.4    Martinou, J.C.5
  • 3
    • 0037164865 scopus 로고    scopus 로고
    • Mitochondrial release of apoptosis-inducing factor occurs downstream of cytochrome c release in response to several proapoptotic stimuli
    • Arnoult, D., Parone, P., Martinou, J.C., Antonsson, B., Estaquier, J. and Ameisen, J.C. (2002) Mitochondrial release of apoptosis-inducing factor occurs downstream of cytochrome c release in response to several proapoptotic stimuli. J. Cell Biol., 159, 923-929.
    • (2002) J. Cell Biol. , vol.159 , pp. 923-929
    • Arnoult, D.1    Parone, P.2    Martinou, J.C.3    Antonsson, B.4    Estaquier, J.5    Ameisen, J.C.6
  • 4
    • 0032544449 scopus 로고    scopus 로고
    • Apaf1 (CED-4 homolog) regulates programmed cell death in mammalian development
    • Cecconi, F., Alvarez-Bolado, G., Meyer, B.I., Roth, K.A. and Gruss, P. (1998) Apaf1 (CED-4 homolog) regulates programmed cell death in mammalian development. Cell, 94, 727-737.
    • (1998) Cell , vol.94 , pp. 727-737
    • Cecconi, F.1    Alvarez-Bolado, G.2    Meyer, B.I.3    Roth, K.A.4    Gruss, P.5
  • 5
    • 0034284637 scopus 로고    scopus 로고
    • Mitochondria as the central control point of apoptosis
    • Desagher, S. and Martinou, J.C. (2000) Mitochondria as the central control point of apoptosis. Trends Cell. Biol., 10, 369-377.
    • (2000) Trends Cell. Biol. , vol.10 , pp. 369-377
    • Desagher, S.1    Martinou, J.C.2
  • 7
    • 0034212442 scopus 로고    scopus 로고
    • Cytochrome c release from isolated rat liver mitochondria can occur independently of outer-membrane rupture: Possible role of contact sites
    • Doran, E. and Halestrap, A.P. (2000) Cytochrome c release from isolated rat liver mitochondria can occur independently of outer-membrane rupture: possible role of contact sites. Biochem. J., 348, 343-350.
    • (2000) Biochem. J. , vol.348 , pp. 343-350
    • Doran, E.1    Halestrap, A.P.2
  • 8
    • 0034616945 scopus 로고    scopus 로고
    • Smac, a mitochondrial protein that promotes cytochrome-c-dependent caspase activation by eliminating IAP inhibition
    • Du, C., Fang, M., Li, Y., Li, L. and Wang, X. (2000) Smac, a mitochondrial protein that promotes cytochrome-c-dependent caspase activation by eliminating IAP inhibition. Cell, 102, 33-42.
    • (2000) Cell , vol.102 , pp. 33-42
    • Du, C.1    Fang, M.2    Li, Y.3    Li, L.4    Wang, X.5
  • 10
    • 0033593230 scopus 로고    scopus 로고
    • Bax-induced caspase activation and apoptosis via cytochrome c release from mitochondria is inhibitable by Bcl-xL
    • Finucane, D.M., Bossy-Wetzel, E., Waterhouse, N.J., Cotter, T.G. and Green, D.R. (1999) Bax-induced caspase activation and apoptosis via cytochrome c release from mitochondria is inhibitable by Bcl-xL. J. Biol. Chem., 274, 2225-2233.
    • (1999) J. Biol. Chem. , vol.274 , pp. 2225-2233
    • Finucane, D.M.1    Bossy-Wetzel, E.2    Waterhouse, N.J.3    Cotter, T.G.4    Green, D.R.5
  • 11
    • 0028816881 scopus 로고
    • Endonuclease G from mammalian nuclei is identical to the major endonuclease of mitochondria
    • Gerschenson, M., Houmiel, K.L. and Low, R.L. (1995) Endonuclease G from mammalian nuclei is identical to the major endonuclease of mitochondria. Nucleic Acids Res., 23, 88-97.
    • (1995) Nucleic Acids Res. , vol.23 , pp. 88-97
    • Gerschenson, M.1    Houmiel, K.L.2    Low, R.L.3
  • 12
    • 0033781027 scopus 로고    scopus 로고
    • The coordinate release of cytochrome c during apoptosis is rapid, complete and kinetically invariant
    • Goldstein, J.C., Waterhouse, N.J., Juin, P., Evan, G.I. and Green, D.R. (2000) The coordinate release of cytochrome c during apoptosis is rapid, complete and kinetically invariant. Nat. Cell Biol., 2, 156-162.
    • (2000) Nat. Cell Biol. , vol.2 , pp. 156-162
    • Goldstein, J.C.1    Waterhouse, N.J.2    Juin, P.3    Evan, G.I.4    Green, D.R.5
  • 13
    • 0037636369 scopus 로고    scopus 로고
    • Mitochondrial membrane potential regulates matrix configuration and cytochrome c release during apoptosis
    • Gottlieb, E., Armour, S.M., Harris, M.H. and Thompson, C.B. (2003) Mitochondrial membrane potential regulates matrix configuration and cytochrome c release during apoptosis. Cell Death Differ., 10, 709-717.
    • (2003) Cell Death Differ. , vol.10 , pp. 709-717
    • Gottlieb, E.1    Armour, S.M.2    Harris, M.H.3    Thompson, C.B.4
  • 14
    • 0033179760 scopus 로고    scopus 로고
    • Bcl-2 family members and the mitochondria in apoptosis
    • Gross, A., McDonnell, J.M. and Korsmeyer, S.J. (1999) Bcl-2 family members and the mitochondria in apoptosis. Genes Dev., 13, 1899-1911.
    • (1999) Genes Dev. , vol.13 , pp. 1899-1911
    • Gross, A.1    McDonnell, J.M.2    Korsmeyer, S.J.3
  • 15
    • 18544386724 scopus 로고    scopus 로고
    • Identification of Omi/HtrA2 as a mitochondrial apoptotic serine protease that disrupts inhibitor of apoptosis protein-caspase interaction
    • Hegde, R. et al. (2002) 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) J. Biol. Chem. , vol.277 , pp. 432-438
    • Hegde, R.1
  • 16
    • 0034641918 scopus 로고    scopus 로고
    • The biochemistry of apoptosis
    • Hengartner, M.O. (2000) The biochemistry of apoptosis. Nature, 407, 770-776.
    • (2000) Nature , vol.407 , pp. 770-776
    • Hengartner, M.O.1
  • 17
    • 0033119367 scopus 로고    scopus 로고
    • Genetic control of programmed cell death in the nematode Caenorhabditis elegans
    • Horvitz, H.R. (1999) Genetic control of programmed cell death in the nematode Caenorhabditis elegans. Cancer Res., 59, 1701s-1706s.
    • (1999) Cancer Res. , vol.59
    • Horvitz, H.R.1
  • 18
    • 0030947095 scopus 로고    scopus 로고
    • Programmed cell death in animal development
    • Jacobson, M.D., Weil, M. and Raff, M.C. (1997) Programmed cell death in animal development. Cell, 88, 347-354.
    • (1997) Cell , vol.88 , pp. 347-354
    • Jacobson, M.D.1    Weil, M.2    Raff, M.C.3
  • 20
    • 0031037897 scopus 로고    scopus 로고
    • The release of cytochrome c from mitochondria: A primary site for Bcl-2 regulation of apoptosis
    • Kluck, R.M., Bossy-Wetzel, E., Green, D.R. and Newmeyer, D.D. (1997) The release of cytochrome c from mitochondria: a primary site for Bcl-2 regulation of apoptosis. Science, 275, 1132-1136.
    • (1997) Science , vol.275 , pp. 1132-1136
    • Kluck, R.M.1    Bossy-Wetzel, E.2    Green, D.R.3    Newmeyer, D.D.4
  • 21
    • 0034068601 scopus 로고    scopus 로고
    • Mitochondrial control of cell death
    • Kroemer, G. and Reed, J.C. (2000) Mitochondrial control of cell death. Nat. Med., 6, 513-519.
    • (2000) Nat. Med. , vol.6 , pp. 513-519
    • Kroemer, G.1    Reed, J.C.2
  • 23
    • 0035811496 scopus 로고    scopus 로고
    • Endonuclease G is an apoptotic DNase when released from mitochondria
    • Li, L.Y., Luo, X. and Wang, X. (2001) Endonuclease G is an apoptotic DNase when released from mitochondria. Nature, 412, 95-99.
    • (2001) Nature , vol.412 , pp. 95-99
    • Li, L.Y.1    Luo, X.2    Wang, X.3
  • 24
    • 0030715323 scopus 로고    scopus 로고
    • Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade
    • Li, P., Nijhawan, D., Budihardjo, I., Srinivasula, S.M., Ahmad, M., Alnemri, E.S. and Wang, X. (1997) Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade. Cell, 91, 479-489.
    • (1997) Cell , vol.91 , pp. 479-489
    • Li, P.1    Nijhawan, D.2    Budihardjo, I.3    Srinivasula, S.M.4    Ahmad, M.5    Alnemri, E.S.6    Wang, X.7
  • 25
    • 0033377511 scopus 로고    scopus 로고
    • Apoptosis-related functional features of the DNaseI-like family of nucleases
    • Liu, Q.Y., Ribecco, M., Pandey, S., Walker, P.R. and Sikorska, M. (1999) Apoptosis-related functional features of the DNaseI-like family of nucleases. Ann. N.Y. Acad. Sci., 887, 60-76.
    • (1999) Ann. N.Y. Acad. Sci. , vol.887 , pp. 60-76
    • Liu, Q.Y.1    Ribecco, M.2    Pandey, S.3    Walker, P.R.4    Sikorska, M.5
  • 26
    • 0037184113 scopus 로고    scopus 로고
    • Proteasome-mediated degradation of Smac during apoptosis: XIAP promotes Smac ubiquitination in vitro
    • MacFarlane, M., Merrison, W., Bratton, S.B. and Cohen, G.M. (2002) Proteasome-mediated degradation of Smac during apoptosis: XIAP promotes Smac ubiquitination in vitro. J. Biol. Chem., 277, 36611-36616.
    • (2002) J. Biol. Chem. , vol.277 , pp. 36611-36616
    • MacFarlane, M.1    Merrison, W.2    Bratton, S.B.3    Cohen, G.M.4
  • 28
    • 0032566649 scopus 로고    scopus 로고
    • Bax and adenine nucleotide translocator cooperate in the mitochondrial control of apoptosis
    • Marzo, I. et al. (1998) Bax and adenine nucleotide translocator cooperate in the mitochondrial control of apoptosis. Science, 281, 2027-2031.
    • (1998) Science , vol.281 , pp. 2027-2031
    • Marzo, I.1
  • 30
    • 0034630317 scopus 로고    scopus 로고
    • Apoptotic DNA fragmentation
    • Nagata, S. (2000) Apoptotic DNA fragmentation. Exp. Cell Res., 256, 12-18.
    • (2000) Exp. Cell Res. , vol.256 , pp. 12-18
    • Nagata, S.1
  • 32
    • 0035811511 scopus 로고    scopus 로고
    • Mitochondrial endonuclease G is important for apoptosis in Celegans
    • Parrish, J., Li, L., Klotz, K., Ledwich, D., Wang, X. and Xue, D. (2001) Mitochondrial endonuclease G is important for apoptosis in Celegans. Nature, 412, 90-94.
    • (2001) Nature , vol.412 , pp. 90-94
    • Parrish, J.1    Li, L.2    Klotz, K.3    Ledwich, D.4    Wang, X.5    Xue, D.6
  • 33
    • 0037421221 scopus 로고    scopus 로고
    • Caspase-mediated loss of mitochondrial function and generation of reactive oxygen species during apoptosis
    • Ricci, J.E., Gottlieb, R.A. and Green, D.R. (2003) Caspase-mediated loss of mitochondrial function and generation of reactive oxygen species during apoptosis. J. Cell Biol., 160, 65-75.
    • (2003) J. Cell Biol. , vol.160 , pp. 65-75
    • Ricci, J.E.1    Gottlieb, R.A.2    Green, D.R.3
  • 34
    • 0033539067 scopus 로고    scopus 로고
    • Acinus is a caspase-3-activated protein required for apoptotic chromatin condensation
    • Sahara, S., Aoto, M., Eguchi, Y., Imamoto, N., Yoneda, Y. and Tsujimoto, Y. (1999) Acinus is a caspase-3-activated protein required for apoptotic chromatin condensation. Nature, 401, 168-173.
    • (1999) Nature , vol.401 , pp. 168-173
    • Sahara, S.1    Aoto, M.2    Eguchi, Y.3    Imamoto, N.4    Yoneda, Y.5    Tsujimoto, Y.6
  • 36
    • 0033521741 scopus 로고    scopus 로고
    • Molecular characterization of mitochondrial apoptosis-inducing factor
    • Susin, S.A., et al. (1999) Molecular characterization of mitochondrial apoptosis-inducing factor. Nature, 397, 441-446.
    • (1999) Nature , vol.397 , pp. 441-446
    • Susin, S.A.1
  • 37
    • 0034698733 scopus 로고    scopus 로고
    • Two distinct pathways leading to nuclear apoptosis
    • Susin, S.A., et al. (2000) Two distinct pathways leading to nuclear apoptosis. J. Exp. Med., 192, 571-580.
    • (2000) J. Exp. Med. , vol.192 , pp. 571-580
    • Susin, S.A.1
  • 38
    • 0033713002 scopus 로고    scopus 로고
    • Structure of Bax: Coregulation of dimer formation and intracellular localization
    • Suzuki, M., Youle, R.J. and Tjandra, N. (2000) Structure of Bax: coregulation of dimer formation and intracellular localization. Cell, 103, 645-654.
    • (2000) Cell , vol.103 , pp. 645-654
    • Suzuki, M.1    Youle, R.J.2    Tjandra, N.3
  • 39
    • 0034785591 scopus 로고    scopus 로고
    • A serine protease, HtrA2, is released from the mitochondria and interacts with XIAP, inducing cell death
    • Suzuki, Y., Imai, Y., Nakayama, H., Takahashi, K., Takio, K. and Takahashi, R. (2001) A serine protease, HtrA2, is released from the mitochondria and interacts with XIAP, inducing cell death. Mol. Cell, 8, 613-621.
    • (2001) Mol. Cell , vol.8 , pp. 613-621
    • Suzuki, Y.1    Imai, Y.2    Nakayama, H.3    Takahashi, K.4    Takio, K.5    Takahashi, R.6
  • 40
    • 0028943734 scopus 로고
    • Apoptosis in the pathogenesis and treatment of disease
    • Thompson, C.B. (1995) Apoptosis in the pathogenesis and treatment of disease. Science, 267, 1456-1462.
    • (1995) Science , vol.267 , pp. 1456-1462
    • Thompson, C.B.1
  • 41
    • 0032575750 scopus 로고    scopus 로고
    • Caspases: Enemies within
    • Thornberry, N.A. and Lazebnik, Y. (1998) Caspases: enemies within. Science, 281, 1312-1316.
    • (1998) Science , vol.281 , pp. 1312-1316
    • Thornberry, N.A.1    Lazebnik, Y.2
  • 43
    • 0033258120 scopus 로고    scopus 로고
    • Bcl-2 proteins: Regulators of apoptosis or of mitochondrial homeostasis?
    • Van der Heiden, M.G. and Thompson, C.B. (1999) Bcl-2 proteins: regulators of apoptosis or of mitochondrial homeostasis? Nat. Cell Biol., 1, E209-216.
    • (1999) Nat. Cell Biol. , vol.1
    • Van der Heiden, M.G.1    Thompson, C.B.2
  • 44
  • 45
    • 0037016686 scopus 로고    scopus 로고
    • HtrA2 promotes cell death through its serine protease activity and its ability to antagonize inhibitor of apoptosis proteins
    • Verhagen, A.M., et al. (2002) HtrA2 promotes cell death through its serine protease activity and its ability to antagonize inhibitor of apoptosis proteins. J. Biol. Chem., 277, 445-454.
    • (2002) J. Biol. Chem. , vol.277 , pp. 445-454
    • Verhagen, A.M.1
  • 46
    • 0035890085 scopus 로고    scopus 로고
    • The expanding role of mitochondria in apoptosis
    • Wang, X. (2001) The expanding role of mitochondria in apoptosis. Genes Dev., 15, 2922-2933.
    • (2001) Genes Dev. , vol.15 , pp. 2922-2933
    • Wang, X.1
  • 47
    • 0037159784 scopus 로고    scopus 로고
    • Mechanisms of AIF-mediated apoptotic DNA degradation in Caenorhabditis elegans
    • Wang, X., Yang, C., Chai, J., Shi, Y. and Xue, D. (2002) Mechanisms of AIF-mediated apoptotic DNA degradation in Caenorhabditis elegans. Science, 298, 1587-1592.
    • (2002) Science , vol.298 , pp. 1587-1592
    • Wang, X.1    Yang, C.2    Chai, J.3    Shi, Y.4    Xue, D.5
  • 48
    • 0035897408 scopus 로고    scopus 로고
    • Cytochrome c maintains mitochondrial transmembrane potential and ATP generation after outer mitochondrial membrane permeabilization during the apoptotic process
    • Waterhouse, N.J., Goldstein, J.C., von Ahsen, O., Schuler, M., Newmeyer, D.D. and Green, D.R. (2001) Cytochrome c maintains mitochondrial transmembrane potential and ATP generation after outer mitochondrial membrane permeabilization during the apoptotic process. J. Cell Biol., 153, 319-328.
    • (2001) J. Cell Biol. , vol.153 , pp. 319-328
    • Waterhouse, N.J.1    Goldstein, J.C.2    Von Ahsen, O.3    Schuler, M.4    Newmeyer, D.D.5    Green, D.R.6
  • 49
    • 0035957653 scopus 로고    scopus 로고
    • Proapoptotic BAX and BAK: A requisite gateway to mitochondrial dysfunction and death
    • Wei, M.C., et al. (2001) Proapoptotic BAX and BAK: a requisite gateway to mitochondrial dysfunction and death. Science, 292, 727-730.
    • (2001) Science , vol.292 , pp. 727-730
    • Wei, M.C.1
  • 50
    • 0035930523 scopus 로고    scopus 로고
    • Action of recombinant human apoptotic endonuclease G on naked DNA and chromatin substrates: Cooperation with exonuclease and DNase I
    • Widlak, P., Li, L.Y., Wang, X. and Garrard, W.T. (2001) Action of recombinant human apoptotic endonuclease G on naked DNA and chromatin substrates: cooperation with exonuclease and DNase I. J. Biol. Chem., 276, 48404-48409.
    • (2001) J. Biol. Chem. , vol.276 , pp. 48404-48409
    • Widlak, P.1    Li, L.Y.2    Wang, X.3    Garrard, W.T.4
  • 52
    • 0035229427 scopus 로고    scopus 로고
    • The mitochondrion in apoptosis: How Pandora's box opens
    • Zamzami, N. and Kroemer, G. (2001) The mitochondrion in apoptosis: how Pandora's box opens. Nat. Rev. Mol. Cell. Biol., 2, 67-71.
    • (2001) Nat. Rev. Mol. Cell. Biol. , vol.2 , pp. 67-71
    • Zamzami, N.1    Kroemer, G.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.