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Volumn 5, Issue 1, 2013, Pages

Where killers meet-permeabilization of the outer mitochondrial membrane during apoptosis

Author keywords

[No Author keywords available]

Indexed keywords

MEMBRANE LIPID; MITOCHONDRIAL PROTEIN; PROTEIN BCL 2;

EID: 84872006971     PISSN: None     EISSN: 19430264     Source Type: Journal    
DOI: 10.1101/cshperspect.a011106     Document Type: Article
Times cited : (78)

References (75)
  • 4
    • 34247895697 scopus 로고    scopus 로고
    • Voltage-dependent anion channels are dispensable for mitochondrial-dependent cell death
    • Baines CP, Kaiser RA, Sheiko T, Craigen WJ, Molkentin JD. 2007. Voltage-dependent anion channels are dispensable for mitochondrial-dependent cell death. Nat Cell Biol 9: 550-555.
    • (2007) Nat Cell Biol , vol.9 , pp. 550-555
    • Baines, C.P.1    Kaiser, R.A.2    Sheiko, T.3    Craigen, W.J.4    Molkentin, J.D.5
  • 5
    • 0037147239 scopus 로고    scopus 로고
    • Bax-type apoptotic proteins porate pure lipid bilayers through a mechanism sensitive to intrinsic monolayer curvature
    • Basanez G, Sharpe JC, Galanis J, Brandt TB, Hardwick JM, Zimmerberg J. 2002. Bax-type apoptotic proteins porate pure lipid bilayers through a mechanism sensitive to intrinsic monolayer curvature. J Biol Chem 277: 49360-49365.
    • (2002) J Biol Chem , vol.277 , pp. 49360-49365
    • Basanez, G.1    Sharpe, J.C.2    Galanis, J.3    Brandt, T.B.4    Hardwick, J.M.5    Zimmerberg, J.6
  • 16
  • 17
    • 70449941949 scopus 로고    scopus 로고
    • Bak activation for apoptosis involves oligomerization of dimers via their a6 helices
    • Dewson G, Kratina T, Czabotar P, Day CL, Adams JM, Kluck RM. 2009. Bak activation for apoptosis involves oligomerization of dimers via their a6 helices. Mol Cell 36: 696-703.
    • (2009) Mol Cell , vol.36 , pp. 696-703
    • Dewson, G.1    Kratina, T.2    Czabotar, P.3    Day, C.L.4    Adams, J.M.5    Kluck, R.M.6
  • 20
    • 55949137911 scopus 로고    scopus 로고
    • Membrane lysis during biological membrane fusion: Collateral damage by misregulated fusion machines
    • Engel A, Walter P. 2008. Membrane lysis during biological membrane fusion: Collateral damage by misregulated fusion machines. J Cell Biol 183: 181-186.
    • (2008) J Cell Biol , vol.183 , pp. 181-186
    • Engel, A.1    Walter, P.2
  • 21
    • 0033981577 scopus 로고    scopus 로고
    • Bid induces the oligomerization and insertion of Bax into the outer mitochondrial membrane
    • Eskes R, Desagher S, Antonsson B, Martinou JC. 2000. Bid induces the oligomerization and insertion of Bax into the outer mitochondrial membrane. Mol Cell Biol 20: 929-935.
    • (2000) Mol Cell Biol , vol.20 , pp. 929-935
    • Eskes, R.1    Desagher, S.2    Antonsson, B.3    Martinou, J.C.4
  • 23
    • 34447255173 scopus 로고    scopus 로고
    • Pore formation by a Bax-derived peptide: Effect on the line tension of the membrane probed by AFM
    • Garcia-Saez AJ, Chiantia S, Salgado J, Schwille P. 2007. Pore formation by a Bax-derived peptide: Effect on the line tension of the membrane probed by AFM. Biophys J 93: 103-112.
    • (2007) Biophys J , vol.93 , pp. 103-112
    • Garcia-Saez, A.J.1    Chiantia, S.2    Salgado, J.3    Schwille, P.4
  • 25
    • 78149449341 scopus 로고    scopus 로고
    • BH3-triggered structural reorganization drives the activation of proapoptotic BAX
    • Gavathiotis E, Reyna DE, Davis ML, Bird GH, Walensky LD. 2010. BH3-triggered structural reorganization drives the activation of proapoptotic BAX. Mol Cell 40: 481-492.
    • (2010) Mol Cell , vol.40 , pp. 481-492
    • Gavathiotis, E.1    Reyna, D.E.2    Davis, M.L.3    Bird, G.H.4    Walensky, L.D.5
  • 26
    • 34547629939 scopus 로고    scopus 로고
    • A three-helix homooligomerization domain containing BH3 and BH1 is responsible for the apoptotic activity of Bax
    • George NM, Evans JJ, Luo X. 2007. A three-helix homooligomerization domain containing BH3 and BH1 is responsible for the apoptotic activity of Bax. Genes Dev 21: 1937-1948.
    • (2007) Genes Dev , vol.21 , pp. 1937-1948
    • George, N.M.1    Evans, J.J.2    Luo, X.3
  • 27
    • 0031007644 scopus 로고    scopus 로고
    • Nonionic detergents induce dimerization among members of the Bcl-2 family
    • Hsu YT, Youle RJ. 1997. Nonionic detergents induce dimerization among members of the Bcl-2 family. J Biol Chem 272: 13829-13834.
    • (1997) J Biol Chem , vol.272 , pp. 13829-13834
    • Hsu, Y.T.1    Youle, R.J.2
  • 28
    • 0030963602 scopus 로고    scopus 로고
    • Cytosol-to-membrane redistribution of Bax and Bcl-X(L) during apoptosis
    • Hsu YT, Wolter KG, Youle RJ. 1997. Cytosol-to-membrane redistribution of Bax and Bcl-X(L) during apoptosis. Proc Natl Acad Sci 94: 3668-3672.
    • (1997) Proc Natl Acad Sci , vol.94 , pp. 3668-3672
    • Hsu, Y.T.1    Wolter, K.G.2    Youle, R.J.3
  • 33
    • 13944277343 scopus 로고    scopus 로고
    • BH3 domains of BH3-only proteins differentially regulate Bax-mediated mitochondrial membrane permeabilization both directly and indirectly
    • Kuwana T, Bouchier-Hayes L, Chipuk JE, Bonzon C, Sullivan BA, Green DR, Newmeyer DD. 2005. BH3 domains of BH3-only proteins differentially regulate Bax-mediated mitochondrial membrane permeabilization both directly and indirectly. Mol Cell 17: 525-535.
    • (2005) Mol Cell , vol.17 , pp. 525-535
    • Kuwana, T.1    Bouchier-Hayes, L.2    Chipuk, J.E.3    Bonzon, C.4    Sullivan, B.A.5    Green, D.R.6    Newmeyer, D.D.7
  • 34
    • 34247497716 scopus 로고    scopus 로고
    • Embedded together: The life and death consequences of interaction of the Bcl-2 family with membranes
    • Leber B, Lin J, Andrews DW. 2007. Embedded together: The life and death consequences of interaction of the Bcl-2 family with membranes. Apoptosis 12: 897-911.
    • (2007) Apoptosis , vol.12 , pp. 897-911
    • Leber, B.1    Lin, J.2    Andrews, D.W.3
  • 35
    • 77957141008 scopus 로고    scopus 로고
    • Still embedded together binding to membranes regulates Bcl-2 protein interactions
    • Leber B, Lin J, Andrews DW. 2010. Still embedded together binding to membranes regulates Bcl-2 protein interactions. Oncogene 29: 5221-5230.
    • (2010) Oncogene , vol.29 , pp. 5221-5230
    • Leber, B.1    Lin, J.2    Andrews, D.W.3
  • 36
    • 0036728834 scopus 로고    scopus 로고
    • Distinct BH3 domains either sensitize or activate mitochondrial apoptosis, serving as prototype cancer therapeutics
    • Letai A, Bassik MC, Walensky LD, Sorcinelli MD, Weiler S, Korsmeyer SJ. 2002. Distinct BH3 domains either sensitize or activate mitochondrial apoptosis, serving as prototype cancer therapeutics. Cancer Cell 2: 183-192.
    • (2002) Cancer Cell , vol.2 , pp. 183-192
    • Letai, A.1    Bassik, M.C.2    Walensky, L.D.3    Sorcinelli, M.D.4    Weiler, S.5    Korsmeyer, S.J.6
  • 37
    • 33750347347 scopus 로고    scopus 로고
    • Mitochondrial dysfunction and oxidative stress in neurodegenerative diseases
    • Lin MT, Beal MF. 2006. Mitochondrial dysfunction and oxidative stress in neurodegenerative diseases. Nature 443: 787-795.
    • (2006) Nature , vol.443 , pp. 787-795
    • Lin, M.T.1    Beal, M.F.2
  • 38
    • 79952700828 scopus 로고    scopus 로고
    • Bcl-2 proteins and mitochondria-Specificity in membrane targeting for death
    • 532-529
    • Lindsay J, EspostiMD, Gilmore AP. 2011. Bcl-2 proteins and mitochondria-Specificity in membrane targeting for death. Biochim Biophys Acta 1813: 532-529.
    • (2011) Biochim Biophys Acta , vol.1813
    • Lindsay, J.1    Esposti, M.D.2    Gilmore, A.P.3
  • 39
    • 79551620159 scopus 로고    scopus 로고
    • Apoptosis and oncogenesis: Give and take in the BCL-2 family
    • Llambi F, Green DR. 2011. Apoptosis and oncogenesis: Give and take in the BCL-2 family. Curr Opin Genet Dev 21: 12-20.
    • (2011) Curr Opin Genet Dev , vol.21 , pp. 12-20
    • Llambi, F.1    Green, D.R.2
  • 41
    • 57149135309 scopus 로고    scopus 로고
    • Membrane binding by tBid initiates an ordered series of events culminating in membrane permeabilization by Bax
    • Lovell JF, Billen LP, Bindner S, Shamas-Din A, Fradin C, Leber B, Andrews DW. 2008. Membrane binding by tBid initiates an ordered series of events culminating in membrane permeabilization by Bax. Cell 135: 1074-1084.
    • (2008) Cell , vol.135 , pp. 1074-1084
    • Lovell, J.F.1    Billen, L.P.2    Bindner, S.3    Shamas-Din, A.4    Fradin, C.5    Leber, B.6    Andrews, D.W.7
  • 42
    • 39449130146 scopus 로고    scopus 로고
    • Bax activation and stress-induced apoptosis delayed by the accumulation of cholesterol in mitochondrial membranes
    • Lucken-Ardjomande S, Montessuit S, Martinou JC. 2008a. Bax activation and stress-induced apoptosis delayed by the accumulation of cholesterol in mitochondrial membranes. Cell Death Differ 15: 484-493.
    • (2008) Cell Death Differ , vol.15 , pp. 484-493
    • Lucken-Ardjomande, S.1    Montessuit, S.2    Martinou, J.C.3
  • 43
    • 42149094346 scopus 로고    scopus 로고
    • Contributions to Bax insertion and oligomerization of lipids of the mitochondrial outer membrane
    • Lucken-Ardjomande S, Montessuit S, Martinou JC. 2008b. Contributions to Bax insertion and oligomerization of lipids of the mitochondrial outer membrane. Cell Death Differ 15: 929-937.
    • (2008) Cell Death Differ , vol.15 , pp. 929-937
    • Lucken-Ardjomande, S.1    Montessuit, S.2    Martinou, J.C.3
  • 44
    • 0034306169 scopus 로고    scopus 로고
    • Cardiolipin provides specificity for targeting of tBid to mitochondria
    • Lutter M, Fang M, Luo X, Nishijima M, Xie X, Wang X. 2000. Cardiolipin provides specificity for targeting of tBid to mitochondria. Nat Cell Biol 2: 754-761.
    • (2000) Nat Cell Biol , vol.2 , pp. 754-761
    • Lutter, M.1    Fang, M.2    Luo, X.3    Nishijima, M.4    Xie, X.5    Wang, X.6
  • 45
    • 18744374204 scopus 로고    scopus 로고
    • The pro-apoptotic Bcl-2 family member tBid localizes to mitochondrial contact sites
    • Lutter M, Perkins GA, Wang X. 2001. The pro-apoptotic Bcl-2 family member tBid localizes to mitochondrial contact sites. BMC Cell Biol 2: 22.
    • (2001) BMC Cell Biol , vol.2 , pp. 22
    • Lutter, M.1    Perkins, G.A.2    Wang, X.3
  • 47
    • 79960230433 scopus 로고    scopus 로고
    • Mitochondria in apoptosis: Bcl-2 family members and mitochondrial dynamics
    • Martinou JC, Youle RJ. 2011. Mitochondria in apoptosis: Bcl-2 family members and mitochondrial dynamics. Dev Cell 21: 92-101.
    • (2011) Dev Cell , vol.21 , pp. 92-101
    • Martinou, J.C.1    Youle, R.J.2
  • 48
    • 33751544565 scopus 로고    scopus 로고
    • The X-ray structure of a BAK homodimer reveals an inhibitory zinc binding site
    • Moldoveanu T, Liu Q, Tocilj A, Watson M, Shore G, Gehring K. 2006. The X-ray structure of a BAK homodimer reveals an inhibitory zinc binding site. Mol Cell 24: 677-688.
    • (2006) Mol Cell , vol.24 , pp. 677-688
    • Moldoveanu, T.1    Liu, Q.2    Tocilj, A.3    Watson, M.4    Shore, G.5    Gehring, K.6
  • 53
    • 77956523192 scopus 로고    scopus 로고
    • Conformational changes in BAK, a pore-forming proapoptotic Bcl-2 family member, upon membrane insertion and direct evidence for the existence of BH3-BH3 contact interface in BAK homo-oligomers
    • Oh KJ, Singh P, Lee K, Foss K, Lee S, Park M, Aluvila S, Kim RS, Symersky J, Walters DE. 2010. Conformational changes in BAK, a pore-forming proapoptotic Bcl-2 family member, upon membrane insertion and direct evidence for the existence of BH3-BH3 contact interface in BAK homo-oligomers. J Biol Chem 285: 28924-28937.
    • (2010) J Biol Chem , vol.285 , pp. 28924-28937
    • Oh, K.J.1    Singh, P.2    Lee, K.3    Foss, K.4    Lee, S.5    Park, M.6    Aluvila, S.7    Kim, R.S.8    Symersky, J.9    Walters, D.E.10
  • 54
    • 67650741483 scopus 로고    scopus 로고
    • Mitochondrial targeting of tBid/Bax: A role for the TOM complex
    • Ott M, Norberg E, Zhivotovsky B, Orrenius S. 2009. Mitochondrial targeting of tBid/Bax: A role for the TOM complex? Cell Death Differ 16: 1075-1082.
    • (2009) Cell Death Differ , vol.16 , pp. 1075-1082
    • Ott, M.1    Norberg, E.2    Zhivotovsky, B.3    Orrenius, S.4
  • 56
    • 56249132688 scopus 로고    scopus 로고
    • Structure of transmembrane pore induced by Bax-derived peptide: Evidence for lipidic pores
    • Qian S, Wang W, Yang L, Huang HW. 2008. Structure of transmembrane pore induced by Bax-derived peptide: Evidence for lipidic pores. Proc Natl Acad Sci 105: 17379-17383.
    • (2008) Proc Natl Acad Sci , vol.105 , pp. 17379-17383
    • Qian, S.1    Wang, W.2    Yang, L.3    Huang, H.W.4
  • 57
    • 0141768255 scopus 로고    scopus 로고
    • Real-time single cell analysis of Smac/DIABLO release during apoptosis
    • Rehm M, Dussmann H, Prehn JH. 2003. Real-time single cell analysis of Smac/DIABLO release during apoptosis. J Cell Biol 162: 1031-1043.
    • (2003) J Cell Biol , vol.162 , pp. 1031-1043
    • Rehm, M.1    Dussmann, H.2    Prehn, J.H.3
  • 63
    • 0033713002 scopus 로고    scopus 로고
    • Structure of Bax: Coregulation of dimer formation and intracellular localization
    • Suzuki M, Youle RJ, 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
  • 64
    • 33744953583 scopus 로고    scopus 로고
    • Auto-activation of the apoptosis protein Bax increases mitochondrial membrane permeability and is inhibited by Bcl-2
    • Tan C, Dlugosz PJ, Peng J, Zhang Z, Lapolla SM, Plafker SM, Andrews DW, Lin J. 2006. Auto-activation of the apoptosis protein Bax increases mitochondrial membrane permeability and is inhibited by Bcl-2. J Biol Chem 281: 14764-14775.
    • (2006) J Biol Chem , vol.281 , pp. 14764-14775
    • Tan, C.1    Dlugosz, P.J.2    Peng, J.3    Zhang, Z.4    Lapolla, S.M.5    Plafker, S.M.6    Andrews, D.W.7    Lin, J.8
  • 66
    • 0037014586 scopus 로고    scopus 로고
    • Direct addition of BimL to mitochondria does not lead to cytochrome c release
    • Terradillos O, Montessuit S, Huang DC, Martinou JC. 2002. Direct addition of BimL to mitochondria does not lead to cytochrome c release. FEBS Lett 522: 29-34.
    • (2002) FEBS Lett , vol.522 , pp. 29-34
    • Terradillos, O.1    Montessuit, S.2    Huang, D.C.3    Martinou, J.C.4
  • 71
    • 22244464818 scopus 로고    scopus 로고
    • Proapoptotic Bak is sequestered by Mcl-1 and Bcl-xL, but not Bcl-2, until displaced by BH3-only proteins
    • Willis SN, Chen L, Dewson G, Wei A, Naik E, Fletcher JI, Adams JM, Huang DC. 2005. Proapoptotic 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, L.2    Dewson, G.3    Wei, A.4    Naik, E.5    Fletcher, J.I.6    Adams, J.M.7    Huang, D.C.8
  • 73
    • 37549048249 scopus 로고    scopus 로고
    • The BCL-2 protein family: Opposing activities that mediate cell death
    • Youle RJ, Strasser A. 2008. The BCL-2 protein family: Opposing activities that mediate cell death. Nat RevMol Cell Biol 9: 47-59.
    • (2008) Nat RevMol Cell Biol , vol.9 , pp. 47-59
    • Youle, R.J.1    Strasser, A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.