Breaking the mitochondrial barrier

Pro- and anti-apoptotic members of the Bcl-2 family control the permeability of the outer mitochondrial membrane. They could do this either by forming autonomous pores in the membrane or by collaborating with components of the permeability transition pore. Here we discuss why we favour the first of these possibilities.

[1]  Robert L Moritz,et al.  Identification of DIABLO, a Mammalian Protein that Promotes Apoptosis by Binding to and Antagonizing IAP Proteins , 2000, Cell.

[2]  Xiaodong Wang,et al.  Smac, a Mitochondrial Protein that Promotes Cytochrome c–Dependent Caspase Activation by Eliminating IAP Inhibition , 2000, Cell.

[3]  S. Korsmeyer,et al.  Enforced dimerization of BAX results in its translocation, mitochondrial dysfunction and apoptosis , 1998, The EMBO journal.

[4]  S. Korsmeyer,et al.  Biochemical and Genetic Analysis of the Mitochondrial Response of Yeast to BAX and BCL-XL , 2000, Molecular and Cellular Biology.

[5]  D. Bredesen,et al.  Expression of bcl‐2 inhibits necrotic neural cell death , 1995, Journal of neuroscience research.

[6]  A. Strasser,et al.  The proapoptotic activity of the Bcl-2 family member Bim is regulated by interaction with the dynein motor complex. , 1999, Molecular cell.

[7]  M. V. Heiden,et al.  Bcl-xL prevents cell death following growth factor withdrawal by facilitating mitochondrial ATP/ADP exchange. , 1999, Molecular cell.

[8]  Ruedi Aebersold,et al.  Molecular characterization of mitochondrial apoptosis-inducing factor , 1999, Nature.

[9]  S. Korsmeyer,et al.  BAX-dependent transport of cytochrome c reconstituted in pure liposomes , 2000, Nature Cell Biology.

[10]  J C Reed,et al.  Bax and adenine nucleotide translocator cooperate in the mitochondrial control of apoptosis. , 1998, Science.

[11]  D. Green,et al.  Mitochondrial cytochrome c release in apoptosis occurs upstream of DEVD‐specific caspase activation and independently of mitochondrial transmembrane depolarization , 1998, The EMBO journal.

[12]  P. Polčic,et al.  The cytotoxic action of Bax on yeast cells does not require mitochondrial ADP/ATP carrier but may be related to its import to the mitochondria , 2000, FEBS letters.

[13]  P. Nicotera,et al.  Energy supply and the shape of death in neurons and lymphoid cells , 1997, Cell Death and Differentiation.

[14]  Sten Orrenius,et al.  Injected cytochrome c induces apoptosis , 1998, Nature.

[15]  Masashi Narita,et al.  Bcl-2 family proteins regulate the release of apoptogenic cytochrome c by the mitochondrial channel VDAC , 1999, Nature.

[16]  Nico Tjandra,et al.  Structure of Bax Coregulation of Dimer Formation and Intracellular Localization , 2000, Cell.

[17]  M. Priault,et al.  Investigation of bax-induced release of cytochrome c from yeast mitochondria permeability of mitochondrial membranes, role of VDAC and ATP requirement. , 1999, European journal of biochemistry.

[18]  Junying Yuan,et al.  Solution Structure of BID, an Intracellular Amplifier of Apoptotic Signaling , 1999, Cell.

[19]  Y. Tsujimoto,et al.  Proapoptotic BH3-only Bcl-2 family members induce cytochrome c release, but not mitochondrial membrane potential loss, and do not directly modulate voltage-dependent anion channel activity. , 2000, Proceedings of the National Academy of Sciences of the United States of America.

[20]  Gerard I. Evan,et al.  The coordinate release of cytochrome c during apoptosis is rapid, complete and kinetically invariant , 2000, Nature Cell Biology.

[21]  J. Farber,et al.  The Overexpression of Bax Produces Cell Death upon Induction of the Mitochondrial Permeability Transition* , 1998, The Journal of Biological Chemistry.

[22]  J. Martinou,et al.  Mitochondria as the central control point of apoptosis. , 2000, Trends in cell biology.

[23]  S. Korsmeyer,et al.  Solution Structure of the Proapoptotic Molecule BID A Structural Basis for Apoptotic Agonists and Antagonists , 1999, Cell.

[24]  G. Kroemer,et al.  The mitochondrial death/life regulator in apoptosis and necrosis. , 1998, Annual review of physiology.

[25]  R. Meadows,et al.  X-ray and NMR structure of human Bcl-xL, an inhibitor of programmed cell death , 1996, Nature.

[26]  T. Yanagida,et al.  Electrophysiological Study of a Novel Large Pore Formed by Bax and the Voltage-dependent Anion Channel That Is Permeable to Cytochrome c * , 2000, The Journal of Biological Chemistry.

[27]  M. V. Heiden,et al.  Outer mitochondrial membrane permeability can regulate coupled respiration and cell survival. , 2000, Proceedings of the National Academy of Sciences of the United States of America.

[28]  J. Martinou,et al.  Bax oligomerization is required for channel-forming activity in liposomes and to trigger cytochrome c release from mitochondria. , 2000, The Biochemical journal.

[29]  E. White,et al.  TNF-alpha signals apoptosis through a bid-dependent conformational change in Bax that is inhibited by E1B 19K. , 2000, Molecular cell.

[30]  G. Cohen,et al.  Apoptosis, in human monocytic THP.1 cells, results in the release of cytochrome c from mitochondria prior to their ultracondensation, formation of outer membrane discontinuities and reduction in inner membrane potential , 1998, Cell Death and Differentiation.

[31]  J. Martinou,et al.  Bid Induces the Oligomerization and Insertion of Bax into the Outer Mitochondrial Membrane , 2000, Molecular and Cellular Biology.

[32]  S. Korsmeyer,et al.  Bcl-2 and Bax function independently to regulate cell death , 1997, Nature Genetics.

[33]  M. Priault,et al.  Comparison of the effects of bax‐expression in yeast under fermentative and respiratory conditions: investigation of the role of adenine nucleotides carrier and cytochrome c , 1999, FEBS letters.

[34]  Luca Scorrano,et al.  Mitochondria and cell death , 1999 .

[35]  Y. Tsujimoto,et al.  BH4 domain of antiapoptotic Bcl-2 family members closes voltage-dependent anion channel and inhibits apoptotic mitochondrial changes and cell death. , 2000, Proceedings of the National Academy of Sciences of the United States of America.

[36]  P. Gruss,et al.  Interdigital cell death can occur through a necrotic and caspase-independent pathway , 1999, Current Biology.

[37]  H. Saibil,et al.  Two Structural Transitions in Membrane Pore Formation by Pneumolysin, the Pore-Forming Toxin of Streptococcus pneumoniae , 1999, Cell.

[38]  Christian Renken,et al.  Preservation of Mitochondrial Structure and Function after Bid- or Bax-Mediated Cytochrome c Release , 2000, The Journal of cell biology.

[39]  D. Green.  Apoptotic Pathways Paper Wraps Stone Blunts Scissors , 2000, Cell.

[40]  M Crompton,et al.  The mitochondrial permeability transition pore and its role in cell death. , 1999, The Biochemical journal.

[41]  Jean-Claude Martinou,et al.  Bid-induced Conformational Change of Bax Is Responsible for Mitochondrial Cytochrome c Release during Apoptosis , 1999, The Journal of cell biology.

[42]  Xiaodong Wang,et al.  Structural and biochemical basis of apoptotic activation by Smac/DIABLO , 2000, Nature.

[43]  V. Mootha,et al.  tBID, a membrane-targeted death ligand, oligomerizes BAK to release cytochrome c. , 2000, Genes & development.

[44]  Y. Tsujimoto,et al.  BH 4 domain of antiapoptotic Bcl-2 family members closes voltage-dependent anion channel and inhibits apoptotic mitochondrial changes and cell death , 2000 .

[45]  Y. Hsu,et al.  Cytosol-to-membrane redistribution of Bax and Bcl-X(L) during apoptosis. , 1997, Proceedings of the National Academy of Sciences of the United States of America.

[46]  Eugene M. Johnson,et al.  Evidence of a Novel Event during Neuronal Death Development of Competence-to-Die in Response to Cytoplasmic Cytochrome c , 1998, Neuron.

[47]  E. Cheng,et al.  Conversion of Bcl-2 to a Bax-like death effector by caspases. , 1997, Science.

[48]  D. Green,et al.  Surviving the Cytochrome Seas , 1998, Neuron.