메뉴 건너뛰기




Volumn 285, Issue 3, 2018, Pages 416-431

Bax, Bak and beyond — mitochondrial performance in apoptosis

Author keywords

apoptosis; BAK; BAX; BCL 2 family; DRP1; mitochondria; mitochondrial outer membrane permeabilization

Indexed keywords

BH3 PROTEIN; DIMER; OLIGOMER; PROTEIN BAK; PROTEIN BAX; PROTEIN BCL 2; PROTEIN BOK; UNCLASSIFIED DRUG; APOPTOSIS REGULATORY PROTEIN; BAK1 PROTEIN, HUMAN; BAX PROTEIN, HUMAN; C22ORF29 PROTEIN, HUMAN;

EID: 85028880684     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/febs.14186     Document Type: Review
Times cited : (673)

References (130)
  • 1
    • 84890909335 scopus 로고    scopus 로고
    • Control of apoptosis by the BCL-2 protein family: implications for physiology and therapy
    • Czabotar PE, Lessene G, Strasser A & Adams JM (2014) Control of apoptosis by the BCL-2 protein family: implications for physiology and therapy. Nat Rev Mol Cell Biol 15, 49–63.
    • (2014) Nat Rev Mol Cell Biol , vol.15 , pp. 49-63
    • Czabotar, P.E.1    Lessene, G.2    Strasser, A.3    Adams, J.M.4
  • 2
    • 84956630703 scopus 로고    scopus 로고
    • Thirty years of BCL-2: translating cell death discoveries into novel cancer therapies
    • Delbridge AR, Grabow S, Strasser A & Vaux DL (2016) Thirty years of BCL-2: translating cell death discoveries into novel cancer therapies. Nat Rev Cancer 16, 99–109.
    • (2016) Nat Rev Cancer , vol.16 , pp. 99-109
    • Delbridge, A.R.1    Grabow, S.2    Strasser, A.3    Vaux, D.L.4
  • 3
    • 84860389354 scopus 로고    scopus 로고
    • Deciphering the rules of programmed cell death to improve therapy of cancer and other diseases
    • Strasser A, Cory S & Adams JM (2011) Deciphering the rules of programmed cell death to improve therapy of cancer and other diseases. EMBO J 30, 3667–3683.
    • (2011) EMBO J , vol.30 , pp. 3667-3683
    • Strasser, A.1    Cory, S.2    Adams, J.M.3
  • 5
    • 77956095537 scopus 로고    scopus 로고
    • Mitochondria and cell death: outer membrane permeabilization and beyond
    • Tait SW & Green DR (2010) Mitochondria and cell death: outer membrane permeabilization and beyond. Nat Rev Mol Cell Biol 11, 621–632.
    • (2010) Nat Rev Mol Cell Biol , vol.11 , pp. 621-632
    • Tait, S.W.1    Green, D.R.2
  • 6
    • 84870990121 scopus 로고    scopus 로고
    • The secrets of the Bcl-2 family
    • Garcia-Saez AJ (2012) The secrets of the Bcl-2 family. Cell Death Differ 19, 1733–1740.
    • (2012) Cell Death Differ , vol.19 , pp. 1733-1740
    • Garcia-Saez, A.J.1
  • 7
    • 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 Rev Mol Cell Biol 9, 47–59.
    • (2008) Nat Rev Mol Cell Biol , vol.9 , pp. 47-59
    • Youle, R.J.1    Strasser, A.2
  • 11
    • 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
  • 12
    • 0030963602 scopus 로고    scopus 로고
    • Cytosol-to-membrane redistribution of Bax and Bcl-XL during apoptosis
    • Hsu YT, Wolter KG & Youle RJ (1997) Cytosol-to-membrane redistribution of Bax and Bcl-XL during apoptosis. Proc Natl Acad Sci USA 94, 3668–3672.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 3668-3672
    • Hsu, Y.T.1    Wolter, K.G.2    Youle, R.J.3
  • 14
    • 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
  • 15
    • 85017026288 scopus 로고    scopus 로고
    • The mitochondria-endoplasmic reticulum contact sites: a signalling platform for cell death
    • Prudent J & McBride HM (2017) The mitochondria-endoplasmic reticulum contact sites: a signalling platform for cell death. Curr Opin Cell Biol 47, 52–63.
    • (2017) Curr Opin Cell Biol , vol.47 , pp. 52-63
    • Prudent, J.1    McBride, H.M.2
  • 17
    • 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
  • 18
    • 84911412568 scopus 로고    scopus 로고
    • Conformational rearrangements in the pro-apoptotic protein, Bax, as it inserts into mitochondria: a cellular death switch
    • Gahl RF, He Y, Yu S & Tjandra N (2014) Conformational rearrangements in the pro-apoptotic protein, Bax, as it inserts into mitochondria: a cellular death switch. J Biol Chem 289, 32871–32882.
    • (2014) J Biol Chem , vol.289 , pp. 32871-32882
    • Gahl, R.F.1    He, Y.2    Yu, S.3    Tjandra, N.4
  • 22
    • 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
    • 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
  • 28
    • 79960235245 scopus 로고    scopus 로고
    • Transient binding of an activator BH3 domain to the Bak BH3-binding groove initiates Bak oligomerization
    • Dai H, Smith A, Meng XW, Schneider PA, Pang YP & Kaufmann SH (2011) Transient binding of an activator BH3 domain to the Bak BH3-binding groove initiates Bak oligomerization. J Cell Biol 194, 39–48.
    • (2011) J Cell Biol , vol.194 , pp. 39-48
    • Dai, H.1    Smith, A.2    Meng, X.W.3    Schneider, P.A.4    Pang, Y.P.5    Kaufmann, S.H.6
  • 32
    • 70449941949 scopus 로고    scopus 로고
    • Bak activation for apoptosis involves oligomerization of dimers via their alpha6 helices
    • Dewson G, Kratina T, Czabotar P, Day CL, Adams JM & Kluck RM (2009) Bak activation for apoptosis involves oligomerization of dimers via their alpha6 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
  • 36
  • 39
    • 84893480044 scopus 로고    scopus 로고
    • Organization of the mitochondrial apoptotic BAK pore: oligomerization of the BAK homodimers
    • Aluvila S, Mandal T, Hustedt E, Fajer P, Choe JY & Oh KJ (2014) Organization of the mitochondrial apoptotic BAK pore: oligomerization of the BAK homodimers. J Biol Chem 289, 2537–2551.
    • (2014) J Biol Chem , vol.289 , pp. 2537-2551
    • Aluvila, S.1    Mandal, T.2    Hustedt, E.3    Fajer, P.4    Choe, J.Y.5    Oh, K.J.6
  • 40
    • 84883690023 scopus 로고    scopus 로고
    • Assembly of the Bak apoptotic pore: a critical role for the Bak protein alpha6 helix in the multimerization of homodimers during apoptosis
    • Ma S, Hockings C, Anwari K, Kratina T, Fennell S, Lazarou M, Ryan MT, Kluck RM & Dewson G (2013) Assembly of the Bak apoptotic pore: a critical role for the Bak protein alpha6 helix in the multimerization of homodimers during apoptosis. J Biol Chem 288, 26027–26038.
    • (2013) J Biol Chem , vol.288 , pp. 26027-26038
    • Ma, S.1    Hockings, C.2    Anwari, K.3    Kratina, T.4    Fennell, S.5    Lazarou, M.6    Ryan, M.T.7    Kluck, R.M.8    Dewson, G.9
  • 43
    • 84859753178 scopus 로고    scopus 로고
    • Bak Conformational changes induced by ligand binding: insight into BH3 domain binding and Bak homo-oligomerization
    • Pang YP, Dai H, Smith A, Meng XW, Schneider PA & Kaufmann SH (2012) Bak Conformational changes induced by ligand binding: insight into BH3 domain binding and Bak homo-oligomerization. Sci Rep 2, 257.
    • (2012) Sci Rep , vol.2 , pp. 257
    • Pang, Y.P.1    Dai, H.2    Smith, A.3    Meng, X.W.4    Schneider, P.A.5    Kaufmann, S.H.6
  • 44
    • 0038025230 scopus 로고    scopus 로고
    • Association of Bax and Bak homo-oligomers in mitochondria. Bax requirement for Bak reorganization and cytochrome c release
    • Mikhailov V, Mikhailova M, Degenhardt K, Venkatachalam MA, White E & Saikumar P (2003) Association of Bax and Bak homo-oligomers in mitochondria. Bax requirement for Bak reorganization and cytochrome c release. J Biol Chem 278, 5367–5376.
    • (2003) J Biol Chem , vol.278 , pp. 5367-5376
    • Mikhailov, V.1    Mikhailova, M.2    Degenhardt, K.3    Venkatachalam, M.A.4    White, E.5    Saikumar, P.6
  • 46
    • 1642359643 scopus 로고    scopus 로고
    • Energetics of pore formation induced by membrane active peptides
    • Lee MT, Chen FY & Huang HW (2004) Energetics of pore formation induced by membrane active peptides. Biochemistry 43, 3590–3599.
    • (2004) Biochemistry , vol.43 , pp. 3590-3599
    • Lee, M.T.1    Chen, F.Y.2    Huang, H.W.3
  • 48
    • 85007493424 scopus 로고    scopus 로고
    • Bax and Bak pores: are we closing the circle?
    • Cosentino K & Garcia-Saez AJ (2017) Bax and Bak pores: are we closing the circle? Trends Cell Biol 27, 266–275.
    • (2017) Trends Cell Biol , vol.27 , pp. 266-275
    • Cosentino, K.1    Garcia-Saez, A.J.2
  • 49
    • 84994035499 scopus 로고    scopus 로고
    • Pro-apoptotic cBid and Bax exhibit distinct membrane remodeling activities: an AFM study
    • Unsay JD, Cosentino K, Sporbeck K & Garcia-Saez AJ (2017) Pro-apoptotic cBid and Bax exhibit distinct membrane remodeling activities: an AFM study. Biochem Biophys Acta 1859, 17–27.
    • (2017) Biochem Biophys Acta , vol.1859 , pp. 17-27
    • Unsay, J.D.1    Cosentino, K.2    Sporbeck, K.3    Garcia-Saez, A.J.4
  • 51
    • 22244493864 scopus 로고    scopus 로고
    • Peptides derived from apoptotic Bax and Bid reproduce the poration activity of the parent full-length proteins
    • Garcia-Saez AJ, Coraiola M, Dalla Serra M, Mingarro I, Menestrina G & Salgado J (2005) Peptides derived from apoptotic Bax and Bid reproduce the poration activity of the parent full-length proteins. Biophys J 88, 3976–3990.
    • (2005) Biophys J , vol.88 , pp. 3976-3990
    • Garcia-Saez, A.J.1    Coraiola, M.2    Dalla Serra, M.3    Mingarro, I.4    Menestrina, G.5    Salgado, J.6
  • 52
    • 33644946679 scopus 로고    scopus 로고
    • Peptides corresponding to helices 5 and 6 of Bax can independently form large lipid pores
    • Garcia-Saez AJ, Coraiola M, Serra MD, Mingarro I, Muller P & Salgado J (2006) Peptides corresponding to helices 5 and 6 of Bax can independently form large lipid pores. FEBS J 273, 971–981.
    • (2006) FEBS J , vol.273 , pp. 971-981
    • Garcia-Saez, A.J.1    Coraiola, M.2    Serra, M.D.3    Mingarro, I.4    Muller, P.5    Salgado, J.6
  • 53
    • 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 USA 105, 17379–17383.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 17379-17383
    • Qian, S.1    Wang, W.2    Yang, L.3    Huang, H.W.4
  • 54
    • 84887840021 scopus 로고    scopus 로고
    • Proapoptotic Bax and Bak Proteins form stable protein-permeable pores of tunable size
    • Bleicken S, Landeta O, Landajuela A, Basanez G & Garcia-Saez AJ (2013) Proapoptotic Bax and Bak Proteins form stable protein-permeable pores of tunable size. J Biol Chem 288, 33241–33252.
    • (2013) J Biol Chem , vol.288 , pp. 33241-33252
    • Bleicken, S.1    Landeta, O.2    Landajuela, A.3    Basanez, G.4    Garcia-Saez, A.J.5
  • 57
    • 84958604397 scopus 로고    scopus 로고
    • Bax assembles into large ring-like structures remodeling the mitochondrial outer membrane in apoptosis
    • Grosse L, Wurm CA, Bruser C, Neumann D, Jans DC & Jakobs S (2016) Bax assembles into large ring-like structures remodeling the mitochondrial outer membrane in apoptosis. EMBO J 35, 402–413.
    • (2016) EMBO J , vol.35 , pp. 402-413
    • Grosse, L.1    Wurm, C.A.2    Bruser, C.3    Neumann, D.4    Jans, D.C.5    Jakobs, S.6
  • 58
    • 84973397950 scopus 로고    scopus 로고
    • Pro-apoptotic Bax molecules densely populate the edges of membrane pores
    • Kuwana T, Olson NH, Kiosses WB, Peters B & Newmeyer DD (2016) Pro-apoptotic Bax molecules densely populate the edges of membrane pores. Sci Rep 6, 27299.
    • (2016) Sci Rep , vol.6 , pp. 27299
    • Kuwana, T.1    Olson, N.H.2    Kiosses, W.B.3    Peters, B.4    Newmeyer, D.D.5
  • 60
    • 84974814522 scopus 로고    scopus 로고
    • In situ characterization of bak clusters responsible for cell death using single molecule localization microscopy
    • Nasu Y, Benke A, Arakawa S, Yoshida GJ, Kawamura G, Manley S, Shimizu S & Ozawa T (2016) In situ characterization of bak clusters responsible for cell death using single molecule localization microscopy. Sci Rep 6, 27505.
    • (2016) Sci Rep , vol.6 , pp. 27505
    • Nasu, Y.1    Benke, A.2    Arakawa, S.3    Yoshida, G.J.4    Kawamura, G.5    Manley, S.6    Shimizu, S.7    Ozawa, T.8
  • 63
    • 34247527336 scopus 로고    scopus 로고
    • Mitochondrial permeabilization relies on BH3 ligands engaging multiple prosurvival Bcl-2 relatives, not Bak
    • Uren RT, Dewson G, Chen L, Coyne SC, Huang DC, Adams JM & Kluck RM (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.5    Adams, J.M.6    Kluck, R.M.7
  • 64
    • 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
  • 66
    • 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
  • 68
    • 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
  • 69
    • 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
  • 70
    • 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
  • 73
    • 84963864250 scopus 로고    scopus 로고
    • Inactivation of prosurvival Bcl-2 proteins activates Bax/Bak through the outer mitochondrial membrane
    • O'Neill KL, Huang K, Zhang J, Chen Y & Luo X (2016) Inactivation of prosurvival Bcl-2 proteins activates Bax/Bak through the outer mitochondrial membrane. Genes Dev 30, 973–988.
    • (2016) Genes Dev , vol.30 , pp. 973-988
    • O'Neill, K.L.1    Huang, K.2    Zhang, J.3    Chen, Y.4    Luo, X.5
  • 75
    • 68949136900 scopus 로고    scopus 로고
    • Computational analysis of dynamical responses to the intrinsic pathway of programmed cell death
    • Zhang T, Brazhnik P & Tyson JJ (2009) Computational analysis of dynamical responses to the intrinsic pathway of programmed cell death. Biophys J 97, 415–434.
    • (2009) Biophys J , vol.97 , pp. 415-434
    • Zhang, T.1    Brazhnik, P.2    Tyson, J.J.3
  • 76
    • 33748941571 scopus 로고    scopus 로고
    • Systems analysis of effector caspase activation and its control by X-linked inhibitor of apoptosis protein
    • Rehm M, Huber HJ, Dussmann H & Prehn JH (2006) Systems analysis of effector caspase activation and its control by X-linked inhibitor of apoptosis protein. EMBO J 25, 4338–4349.
    • (2006) EMBO J , vol.25 , pp. 4338-4349
    • Rehm, M.1    Huber, H.J.2    Dussmann, H.3    Prehn, J.H.4
  • 79
    • 85024100749 scopus 로고    scopus 로고
    • Quantitative interactome of a membrane Bcl-2 network identifies a hierarchy of complexes for apoptosis regulation
    • Bleicken S, Hantusch A, Das KK, Frickey T & Garcia-Saez AJ (2017) Quantitative interactome of a membrane Bcl-2 network identifies a hierarchy of complexes for apoptosis regulation. Nat Commun 8, 73.
    • (2017) Nat Commun , vol.8 , pp. 73
    • Bleicken, S.1    Hantusch, A.2    Das, K.K.3    Frickey, T.4    Garcia-Saez, A.J.5
  • 80
    • 33845486323 scopus 로고    scopus 로고
    • Bim, Bad and Bmf: intrinsically unstructured BH3-only proteins that undergo a localized conformational change upon binding to prosurvival Bcl-2 targets
    • Hinds MG, Smits C, Fredericks-Short R, Risk JM, Bailey M, Huang DC & Day CL (2007) Bim, Bad and Bmf: intrinsically unstructured BH3-only proteins that undergo a localized conformational change upon binding to prosurvival Bcl-2 targets. Cell Death Differ 14, 128–136.
    • (2007) Cell Death Differ , vol.14 , pp. 128-136
    • Hinds, M.G.1    Smits, C.2    Fredericks-Short, R.3    Risk, J.M.4    Bailey, M.5    Huang, D.C.6    Day, C.L.7
  • 82
    • 84859056673 scopus 로고    scopus 로고
    • Differences in the mechanisms of proapoptotic BH3 proteins binding to Bcl-XL and Bcl-2 quantified in live MCF-7 cells
    • Aranovich A, Liu Q, Collins T, Geng F, Dixit S, Leber B & Andrews DW (2012) Differences in the mechanisms of proapoptotic BH3 proteins binding to Bcl-XL and Bcl-2 quantified in live MCF-7 cells. Mol Cell 45, 754–763.
    • (2012) Mol Cell , vol.45 , pp. 754-763
    • Aranovich, A.1    Liu, Q.2    Collins, T.3    Geng, F.4    Dixit, S.5    Leber, B.6    Andrews, D.W.7
  • 86
    • 85018503144 scopus 로고    scopus 로고
    • Determinants of BH3 Sequence Specificity for the Disruption of Bcl-xL/cBid Complexes in Membranes
    • Das KK, Shalaby R & Garcia-Saez AJ (2017) Determinants of BH3 Sequence Specificity for the Disruption of Bcl-xL/cBid Complexes in Membranes. ACS Chem Biol 12, 989–1000.
    • (2017) ACS Chem Biol , vol.12 , pp. 989-1000
    • Das, K.K.1    Shalaby, R.2    Garcia-Saez, A.J.3
  • 93
    • 85014572582 scopus 로고    scopus 로고
    • The membrane activity of BOK involves formation of large, stable toroidal pores and is promoted by cBID
    • Fernandez-Marrero Y, Bleicken S, Das KK, Bachmann D, Kaufmann T & Garcia-Saez AJ (2017) The membrane activity of BOK involves formation of large, stable toroidal pores and is promoted by cBID. FEBS J 284, 711–724.
    • (2017) FEBS J , vol.284 , pp. 711-724
    • Fernandez-Marrero, Y.1    Bleicken, S.2    Das, K.K.3    Bachmann, D.4    Kaufmann, T.5    Garcia-Saez, A.J.6
  • 98
    • 0035844867 scopus 로고    scopus 로고
    • Bax and Bak coalesce into novel mitochondria-associated clusters during apoptosis
    • Nechushtan A, Smith CL, Lamensdorf I, Yoon SH & Youle RJ (2001) Bax and Bak coalesce into novel mitochondria-associated clusters during apoptosis. J Cell Biol 153, 1265–1276.
    • (2001) J Cell Biol , vol.153 , pp. 1265-1276
    • Nechushtan, A.1    Smith, C.L.2    Lamensdorf, I.3    Yoon, S.H.4    Youle, R.J.5
  • 101
    • 84866728707 scopus 로고    scopus 로고
    • Endoplasmic reticulum-mitochondria contacts: function of the junction
    • Rowland AA & Voeltz GK (2012) Endoplasmic reticulum-mitochondria contacts: function of the junction. Nat Rev Mol Cell Biol 13, 607–625.
    • (2012) Nat Rev Mol Cell Biol , vol.13 , pp. 607-625
    • Rowland, A.A.1    Voeltz, G.K.2
  • 102
    • 38849099158 scopus 로고    scopus 로고
    • Chemical inhibition of the mitochondrial division dynamin reveals its role in Bax/Bak-dependent mitochondrial outer membrane permeabilization
    • Cassidy-Stone A, Chipuk JE, Ingerman E, Song C, Yoo C, Kuwana T, Kurth MJ, Shaw JT, Hinshaw JE, Green DR et al. (2008) Chemical inhibition of the mitochondrial division dynamin reveals its role in Bax/Bak-dependent mitochondrial outer membrane permeabilization. Dev Cell 14, 193–204.
    • (2008) Dev Cell , vol.14 , pp. 193-204
    • Cassidy-Stone, A.1    Chipuk, J.E.2    Ingerman, E.3    Song, C.4    Yoo, C.5    Kuwana, T.6    Kurth, M.J.7    Shaw, J.T.8    Hinshaw, J.E.9    Green, D.R.10
  • 103
    • 34249019899 scopus 로고    scopus 로고
    • Inhibiting Drp1-mediated mitochondrial fission selectively prevents the release of cytochrome c during apoptosis
    • Estaquier J & Arnoult D (2007) Inhibiting Drp1-mediated mitochondrial fission selectively prevents the release of cytochrome c during apoptosis. Cell Death Differ 14, 1086–1094.
    • (2007) Cell Death Differ , vol.14 , pp. 1086-1094
    • Estaquier, J.1    Arnoult, D.2
  • 106
    • 49349105966 scopus 로고    scopus 로고
    • Bax- or Bak-induced mitochondrial fission can be uncoupled from cytochrome C release
    • Sheridan C, Delivani P, Cullen SP & Martin SJ (2008) Bax- or Bak-induced mitochondrial fission can be uncoupled from cytochrome C release. Mol Cell 31, 570–585.
    • (2008) Mol Cell , vol.31 , pp. 570-585
    • Sheridan, C.1    Delivani, P.2    Cullen, S.P.3    Martin, S.J.4
  • 107
    • 6344274848 scopus 로고    scopus 로고
    • Roles of the mammalian mitochondrial fission and fusion mediators Fis1, Drp1, and Opa1 in apoptosis
    • Lee YJ, Jeong SY, Karbowski M, Smith CL & Youle RJ (2004) Roles of the mammalian mitochondrial fission and fusion mediators Fis1, Drp1, and Opa1 in apoptosis. Mol Biol Cell 15, 5001–5011.
    • (2004) Mol Biol Cell , vol.15 , pp. 5001-5011
    • Lee, Y.J.1    Jeong, S.Y.2    Karbowski, M.3    Smith, C.L.4    Youle, R.J.5
  • 108
    • 18444400187 scopus 로고    scopus 로고
    • Endoplasmic reticulum BIK initiates DRP1-regulated remodelling of mitochondrial cristae during apoptosis
    • Germain M, Mathai JP, McBride HM & Shore GC (2005) Endoplasmic reticulum BIK initiates DRP1-regulated remodelling 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
  • 110
    • 84960428273 scopus 로고    scopus 로고
    • Drp1-dependent mitochondrial fission via MiD49/51 is essential for apoptotic cristae remodeling
    • Otera H, Miyata N, Kuge O & Mihara K (2016) Drp1-dependent mitochondrial fission via MiD49/51 is essential for apoptotic cristae remodeling. J Cell Biol 212, 531–544.
    • (2016) J Cell Biol , vol.212 , pp. 531-544
    • Otera, H.1    Miyata, N.2    Kuge, O.3    Mihara, K.4
  • 111
    • 84941799317 scopus 로고    scopus 로고
    • MAPL SUMOylation of Drp1 Stabilizes an ER/Mitochondrial Platform Required for Cell Death
    • Prudent J, Zunino R, Sugiura A, Mattie S, Shore GC & McBride HM (2015) MAPL SUMOylation of Drp1 Stabilizes an ER/Mitochondrial Platform Required for Cell Death. Mol Cell 59, 941–955.
    • (2015) Mol Cell , vol.59 , pp. 941-955
    • Prudent, J.1    Zunino, R.2    Sugiura, A.3    Mattie, S.4    Shore, G.C.5    McBride, H.M.6
  • 112
    • 34248182897 scopus 로고    scopus 로고
    • Bax/Bak promote sumoylation of DRP1 and its stable association with mitochondria during apoptotic cell death
    • Wasiak S, Zunino R & McBride HM (2007) Bax/Bak promote sumoylation of DRP1 and its stable association with mitochondria during apoptotic cell death. J Cell Biol 177, 439–450.
    • (2007) J Cell Biol , vol.177 , pp. 439-450
    • Wasiak, S.1    Zunino, R.2    McBride, H.M.3
  • 113
    • 84899510806 scopus 로고    scopus 로고
    • Mitochondrial alterations in apoptosis
    • Cosentino K & Garcia-Saez AJ (2014) Mitochondrial alterations in apoptosis. Chem Phys Lipids 181, 62–75.
    • (2014) Chem Phys Lipids , vol.181 , pp. 62-75
    • Cosentino, K.1    Garcia-Saez, A.J.2
  • 116
    • 79953152683 scopus 로고    scopus 로고
    • Reconstitution of proapoptotic BAK function in liposomes reveals a dual role for mitochondrial lipids in the BAK-driven membrane permeabilization process
    • Landeta O, Landajuela A, Gil D, Taneva S, Di Primo C, Sot B, Valle M, Frolov VA & Basanez G (2011) Reconstitution of proapoptotic BAK function in liposomes reveals a dual role for mitochondrial lipids in the BAK-driven membrane permeabilization process. J Biol Chem 286, 8213–8230.
    • (2011) J Biol Chem , vol.286 , pp. 8213-8230
    • Landeta, O.1    Landajuela, A.2    Gil, D.3    Taneva, S.4    Di Primo, C.5    Sot, B.6    Valle, M.7    Frolov, V.A.8    Basanez, G.9
  • 118
    • 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
  • 120
    • 2442711625 scopus 로고    scopus 로고
    • Mitochondrial ceramide increases in UV-irradiated HeLa cells and is mainly derived from hydrolysis of sphingomyelin
    • Dai Q, Liu J, Chen J, Durrant D, McIntyre TM & Lee RM (2004) Mitochondrial ceramide increases in UV-irradiated HeLa cells and is mainly derived from hydrolysis of sphingomyelin. Oncogene 23, 3650–3658.
    • (2004) Oncogene , vol.23 , pp. 3650-3658
    • Dai, Q.1    Liu, J.2    Chen, J.3    Durrant, D.4    McIntyre, T.M.5    Lee, R.M.6
  • 121
    • 77951665317 scopus 로고    scopus 로고
    • Ceramide and activated Bax act synergistically to permeabilize the mitochondrial outer membrane
    • Ganesan V, Perera MN, Colombini D, Datskovskiy D, Chadha K & Colombini M (2010) Ceramide and activated Bax act synergistically to permeabilize the mitochondrial outer membrane. Apoptosis 15, 553–562.
    • (2010) Apoptosis , vol.15 , pp. 553-562
    • Ganesan, V.1    Perera, M.N.2    Colombini, D.3    Datskovskiy, D.4    Chadha, K.5    Colombini, M.6
  • 123
    • 85010903661 scopus 로고    scopus 로고
    • Diverting CERT-mediated ceramide transport to mitochondria triggers Bax-dependent apoptosis
    • Jain A, Beutel O, Ebell K, Korneev S & Holthuis JC (2017) Diverting CERT-mediated ceramide transport to mitochondria triggers Bax-dependent apoptosis. J Cell Sci 130, 360–371.
    • (2017) J Cell Sci , vol.130 , pp. 360-371
    • Jain, A.1    Beutel, O.2    Ebell, K.3    Korneev, S.4    Holthuis, J.C.5
  • 125
    • 84876889930 scopus 로고    scopus 로고
    • BAK activation is necessary and sufficient to drive ceramide synthase-dependent ceramide accumulation following inhibition of BCL2-like proteins
    • Beverly LJ, Howell LA, Hernandez-Corbacho M, Casson L, Chipuk JE & Siskind LJ (2013) BAK activation is necessary and sufficient to drive ceramide synthase-dependent ceramide accumulation following inhibition of BCL2-like proteins. Biochem J 452, 111–119.
    • (2013) Biochem J , vol.452 , pp. 111-119
    • Beverly, L.J.1    Howell, L.A.2    Hernandez-Corbacho, M.3    Casson, L.4    Chipuk, J.E.5    Siskind, L.J.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.