메뉴 건너뛰기




Volumn 121, Issue 5, 2008, Pages 618-626

Evaluating cytochrome c diffusion in the intermembrane spaces of mitochondria during cytochrome c release

Author keywords

Apoptosis; Bak; Bid; Cytochrome c; Diffusion; Mitochondria

Indexed keywords

CYTOCHROME C; MITOCHONDRIAL PROTEIN; PROTEIN BAK; PROTEIN BID;

EID: 42149152141     PISSN: 00219533     EISSN: None     Source Type: Journal    
DOI: 10.1242/jcs.021303     Document Type: Article
Times cited : (16)

References (42)
  • 1
    • 33750526651 scopus 로고    scopus 로고
    • The mitochondrial fission protein hFisl requires the endoplasmic reticulum gateway to induce apoptosis
    • Alirol, E., James, D., Huber, D., Marchetto, A, Vergani, L., Martinou, J.-C. and Scorrano, L. (2006). The mitochondrial fission protein hFisl requires the endoplasmic reticulum gateway to induce apoptosis. Mol. Biol. Cell 17, 4593-4605.
    • (2006) Mol. Biol. Cell , vol.17 , pp. 4593-4605
    • Alirol, E.1    James, D.2    Huber, D.3    Marchetto, A.4    Vergani, L.5    Martinou, J.-C.6    Scorrano, L.7
  • 3
    • 33745186921 scopus 로고    scopus 로고
    • 2+ dependent control of the permeability properties of the mitochondrial outer membrane and voltage dependent anion channel
    • 2+ dependent control of the permeability properties of the mitochondrial outer membrane and voltage dependent anion channel. J. Biol. Chem. 281, 17347-17358.
    • (2006) J. Biol. Chem , vol.281 , pp. 17347-17358
    • Bathori, G.1    Csordas, G.2    Garcia-Perez, C.3    Davies, E.4    Hajnoczky, G.5
  • 4
    • 0019888247 scopus 로고
    • Cytochrome c as an electron shuttle between the outer and maer mitochondrial membranes
    • Bernardi, P. and Azzone, G. F. (1981). Cytochrome c as an electron shuttle between the outer and maer mitochondrial membranes. J. Biol. Chem. 256, 7187-7192.
    • (1981) J. Biol. Chem , vol.256 , pp. 7187-7192
    • Bernardi, P.1    Azzone, G.F.2
  • 5
    • 0036771787 scopus 로고    scopus 로고
    • 2+-dependent channel formed by recombinant ADP/ATP carrier from Neurospora crassa resembles the mitochondrial permeability transition pore
    • 2+-dependent channel formed by recombinant ADP/ATP carrier from Neurospora crassa resembles the mitochondrial permeability transition pore. Biochemistry 41, 11804-11811.
    • (2002) Biochemistry , vol.41 , pp. 11804-11811
    • Brustovetsky, N.1    Tropshug, M.2    Heimpel, S.3    Heidkaemper, D.4    Klingenberg, M.5
  • 6
    • 23844509124 scopus 로고    scopus 로고
    • Activation of calcium-independent phospholipase A(2) (iPIA(2)) in brain mitochondria and release of apoptogenic factors by BAX and truncated BID
    • Brustovetsky, T., Antonsson, B., Jemmerson, R., Dubinsky, K. M. and Brustovetsky, N. (2005). Activation of calcium-independent phospholipase A(2) (iPIA(2)) in brain mitochondria and release of apoptogenic factors by BAX and truncated BID. J. Neurochem. 94, 980-994.
    • (2005) J. Neurochem , vol.94 , pp. 980-994
    • Brustovetsky, T.1    Antonsson, B.2    Jemmerson, R.3    Dubinsky, K.M.4    Brustovetsky, N.5
  • 7
    • 0036799548 scopus 로고    scopus 로고
    • Biphasic translocation of Bax to mitochondria
    • Capano, M. and Crompton, M. (2002). Biphasic translocation of Bax to mitochondria. Biochem. J. 367, 169-178.
    • (2002) Biochem. J , vol.367 , pp. 169-178
    • Capano, M.1    Crompton, M.2
  • 8
    • 0033565557 scopus 로고    scopus 로고
    • The mitochondrial permeability transition pore and its role in cell death
    • Crompton, M. (1999). The mitochondrial permeability transition pore and its role in cell death. Biochem. J. 341, 233-249.
    • (1999) Biochem. J , vol.341 , pp. 233-249
    • Crompton, M.1
  • 9
    • 0042526700 scopus 로고    scopus 로고
    • On the involvement of mitochondrial intermembrane junctional complexes in apoptosis
    • Crompton, M. (2003). On the involvement of mitochondrial intermembrane junctional complexes in apoptosis. Curr. Med. Chem. 10, 1473-1484.
    • (2003) Curr. Med. Chem , vol.10 , pp. 1473-1484
    • Crompton, M.1
  • 10
    • 0842281645 scopus 로고    scopus 로고
    • Cell death; critical control points
    • Danial, N. N. and Korsmeyer, S. J. (2004). Cell death; critical control points. Cell 116, 205-219.
    • (2004) Cell , vol.116 , pp. 205-219
    • Danial, N.N.1    Korsmeyer, S.J.2
  • 17
    • 33947608068 scopus 로고    scopus 로고
    • Intersection between mitochondrial permeability transition pores and mitochondrial fusion/ fission
    • Gazaryan, I. G. and Brown, A. M. (2007). Intersection between mitochondrial permeability transition pores and mitochondrial fusion/ fission. Neurochem. Res. 32, 917-929.
    • (2007) Neurochem. Res , vol.32 , pp. 917-929
    • Gazaryan, I.G.1    Brown, A.M.2
  • 18
    • 18444400187 scopus 로고    scopus 로고
    • Endoplasmic reticulum Bik initiates DRP-1 regulated remodeling of mitochondrial cristae during apoptosis
    • Germain, M., Mathai, J. P., McBride, H. M. and Shore, G. C. (2005). Endoplasmic reticulum Bik initiates DRP-1 regulated remodeling of mitochondrial cristae during apoptosis. EMBO J. 24, 1546-1556.
    • (2005) EMBO J , vol.24 , pp. 1546-1556
    • Germain, M.1    Mathai, J.P.2    McBride, H.M.3    Shore, G.C.4
  • 19
    • 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
  • 21
    • 0033535347 scopus 로고    scopus 로고
    • Cell damage-induced conformational changes of the pro-apoptotic protein Bak in vivo precede the onset of apoptosis
    • Griffiths, G. J., Dubrez, L., Morgan, C. P., Jones, N. A., Whitehouse, J., Corfe, B. M., Dive, C. and Hickman, J. A. (1999). Cell damage-induced conformational changes of the pro-apoptotic protein Bak in vivo precede the onset of apoptosis. J. Cell Biol. 144, 903-914.
    • (1999) J. Cell Biol , vol.144 , pp. 903-914
    • Griffiths, G.J.1    Dubrez, L.2    Morgan, C.P.3    Jones, N.A.4    Whitehouse, J.5    Corfe, B.M.6    Dive, C.7    Hickman, J.A.8
  • 23
    • 33744933705 scopus 로고    scopus 로고
    • The course of etoposide-induced apoptosis in Jurkat cells lacking p53 and Bax
    • Karpinich, N. O., Tafani, N., Schneider, T., Russo, M. A. and Farber, J. L. (2006). The course of etoposide-induced apoptosis in Jurkat cells lacking p53 and Bax. J. Cell. Physiol. 208, 55-63.
    • (2006) J. Cell. Physiol , vol.208 , pp. 55-63
    • Karpinich, N.O.1    Tafani, N.2    Schneider, T.3    Russo, M.A.4    Farber, J.L.5
  • 25
    • 3042723249 scopus 로고    scopus 로고
    • Bid-cardiolipin interaction at mitochondrial contact site contributes to mitochondrial cristae reorganization and cytochrome c release
    • Kim, T., Zhao, Y., Ding, W., Shin, J. N., He, X., Seo, Y., Chen, J., Rabinowich, H., Amoscato, A. A. and Yin, X. (2004). Bid-cardiolipin interaction at mitochondrial contact site contributes to mitochondrial cristae reorganization and cytochrome c release. Mol. Biol. Cell 15, 3061-3072.
    • (2004) Mol. Biol. Cell , vol.15 , pp. 3061-3072
    • Kim, T.1    Zhao, Y.2    Ding, W.3    Shin, J.N.4    He, X.5    Seo, Y.6    Chen, J.7    Rabinowich, H.8    Amoscato, A.A.9    Yin, X.10
  • 26
    • 0034523818 scopus 로고    scopus 로고
    • Proapoptotic cascade activates Bid which oligomerizes Bak or Bax into pores that result in the release of cytochrome c
    • Korsmeyer, S. J., Wei, M. C., Saito, M., Weiler, S., Oh, K. J. and Schlesinger, P. H. (2000). Proapoptotic cascade activates Bid which oligomerizes Bak or Bax into pores that result in the release of cytochrome c. Cell Death Differ. 7, 1166-1173.
    • (2000) Cell Death Differ , vol.7 , pp. 1166-1173
    • Korsmeyer, S.J.1    Wei, M.C.2    Saito, M.3    Weiler, S.4    Oh, K.J.5    Schlesinger, P.H.6
  • 28
    • 6344287496 scopus 로고    scopus 로고
    • Cyclophilin-D promotes the mitochondrial permeability transition but has opposite effects on apoptosis and necrosis
    • Li, Y., Johnson, N., Capano, M., Edwards, M. and Crompton, M. (2004). Cyclophilin-D promotes the mitochondrial permeability transition but has opposite effects on apoptosis and necrosis. Biochem. J. 383, 101-109.
    • (2004) Biochem. J , vol.383 , pp. 101-109
    • Li, Y.1    Johnson, N.2    Capano, M.3    Edwards, M.4    Crompton, M.5
  • 30
    • 15844407874 scopus 로고    scopus 로고
    • Cyclophilin D-dependent mitochondrial permeability transition regulates some necrotic but not apoptotic cell death
    • Nakagawa, T., Shimizu, S., Watanabe, T., Yamaguchi, O., Otsu, K., Yamagata, H., Inohara, H., Kubo, T. and Tsujimoto, Y. (2005). Cyclophilin D-dependent mitochondrial permeability transition regulates some necrotic but not apoptotic cell death. Nature 434, 652-657.
    • (2005) Nature , vol.434 , pp. 652-657
    • Nakagawa, T.1    Shimizu, S.2    Watanabe, T.3    Yamaguchi, O.4    Otsu, K.5    Yamagata, H.6    Inohara, H.7    Kubo, T.8    Tsujimoto, Y.9
  • 31
    • 0032504708 scopus 로고    scopus 로고
    • Mitochondria and neuronal glutamate toxicity
    • Nicholls, D. G. and Budd, S. L. (1998). Mitochondria and neuronal glutamate toxicity. Biochim. Biophys. Acta 1366, 97-112.
    • (1998) Biochim. Biophys. Acta , vol.1366 , pp. 97-112
    • Nicholls, D.G.1    Budd, S.L.2
  • 32
    • 0042090307 scopus 로고    scopus 로고
    • Bcl-2 selectively interacts with the Bid-induced open conformer of Bak, inhibiting Bak auto-oligomerisation
    • Ruffolo, S. C. and Shore, G. C. (2003). Bcl-2 selectively interacts with the Bid-induced open conformer of Bak, inhibiting Bak auto-oligomerisation. J. Biol. Chem. 278, 25039-25045.
    • (2003) J. Biol. Chem , vol.278 , pp. 25039-25045
    • Ruffolo, S.C.1    Shore, G.C.2
  • 33
    • 0036007116 scopus 로고    scopus 로고
    • A distinct pathway remodels mitochondria cristae and mobilizes cytochrome c during apoptosis
    • Scorrano, L., Ashiya, M., Buttle, K., Weiler, S., Oakes, S. A., Mannella, C. and Korsmeyer, S. J. (2002). A distinct pathway remodels mitochondria cristae and mobilizes cytochrome c during apoptosis. Dev. Cell 2, 55-67.
    • (2002) Dev. Cell , vol.2 , pp. 55-67
    • Scorrano, L.1    Ashiya, M.2    Buttle, K.3    Weiler, S.4    Oakes, S.A.5    Mannella, C.6    Korsmeyer, S.J.7
  • 34
    • 34247527336 scopus 로고    scopus 로고
    • Mitochondrial permeabilization relies on BH3 ligands engaging multiple prosurvival Bcl-2 relatives, not Bak
    • Uren, R. T., Dewson, G., Chen, L., Coyne, S. C., Huang, D. C. S., Adams, J. M. and Muck, R. M. (2007). Mitochondrial permeabilization relies on BH3 ligands engaging multiple prosurvival Bcl-2 relatives, not Bak. J. Cell Biol. 177, 277-287.
    • (2007) J. Cell Biol , vol.177 , pp. 277-287
    • Uren, R.T.1    Dewson, G.2    Chen, L.3    Coyne, S.C.4    Huang, D.C.S.5    Adams, J.M.6    Muck, R.M.7
  • 36
    • 22244464818 scopus 로고    scopus 로고
    • Pro-apoptotic Bak is sequestered by Mcl-1 and Bcl-xL, but not Bcl-2, until displaced by BH3-only proteins
    • Willis, S. N., Chen, I., Dewson, G., Wei, A., Naik, E., Fletcher, J. I., Adams, J. M. and Huang, D. C. (2005). Pro-apoptotic Bak is sequestered by Mcl-1 and Bcl-xL, but not Bcl-2, until displaced by BH3-only proteins. Genes Dev. 19, 1294-1305.
    • (2005) Genes Dev , vol.19 , pp. 1294-1305
    • Willis, S.N.1    Chen, I.2    Dewson, G.3    Wei, A.4    Naik, E.5    Fletcher, J.I.6    Adams, J.M.7    Huang, D.C.8
  • 37
    • 0030780106 scopus 로고    scopus 로고
    • Movement of Bax from the cytosol to mitochondria during apoptosis
    • Wolter, G., Hsu, Y. T., Smith, C. L., Nechushtan, A., Xi, X. and Youle, R. J. (1997). Movement of Bax from the cytosol to mitochondria during apoptosis. J. Cell Biol. 139, 1281-1291
    • (1997) J. Cell Biol , vol.139 , pp. 1281-1291
    • Wolter, G.1    Hsu, Y.T.2    Smith, C.L.3    Nechushtan, A.4    Xi, X.5    Youle, R.J.6
  • 38
    • 33644657517 scopus 로고    scopus 로고
    • Bid, a BH3-only multifunctional molecule, is at the cross road of life and death
    • Yin, X. (2006). Bid, a BH3-only multifunctional molecule, is at the cross road of life and death. Gene 369, 7-19.
    • (2006) Gene , vol.369 , pp. 7-19
    • Yin, X.1
  • 40
    • 33947394480 scopus 로고    scopus 로고
    • Bax and the mitochondrial permeability transition cooperate in the release of cytochrome c during endoplasmic reticulum-stress-induced apoptosis
    • Zhang, D. and Armstrong, J. S. (2007). Bax and the mitochondrial permeability transition cooperate in the release of cytochrome c during endoplasmic reticulum-stress-induced apoptosis. Cell Death Differ. 14, 703-715.
    • (2007) Cell Death Differ , vol.14 , pp. 703-715
    • Zhang, D.1    Armstrong, J.S.2
  • 41
    • 0042324618 scopus 로고    scopus 로고
    • Bid activates multiple mitochondrial apoptotic mechanisms in primary hepatocytes after death receptor engagement
    • Zhao, Y., Ding, W., Qian, T., Watkins, S., Lemasters, J. J. and Yin, X. (2003). Bid activates multiple mitochondrial apoptotic mechanisms in primary hepatocytes after death receptor engagement. Gastroenterology 125, 845-867.
    • (2003) Gastroenterology , vol.125 , pp. 845-867
    • Zhao, Y.1    Ding, W.2    Qian, T.3    Watkins, S.4    Lemasters, J.J.5    Yin, X.6
  • 42
    • 0035876483 scopus 로고    scopus 로고
    • BH3 only proteins that bind pro-survival Bcl-2 family members fail to induce apoptosis in the absence of Bax and Bak
    • Zong, W. X., Lindsten, T., Ross, A. J., MacGregor, G. R. and Thompson, C. B. (2001). BH3 only proteins that bind pro-survival Bcl-2 family members fail to induce apoptosis in the absence of Bax and Bak. Genes Dev. 15, 1481-1486.
    • (2001) Genes Dev , vol.15 , pp. 1481-1486
    • Zong, W.X.1    Lindsten, T.2    Ross, A.J.3    MacGregor, G.R.4    Thompson, C.B.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.