Apoptotic Pathways: Ten Minutes to Dead

For more than a decade, it has been apparent that apoptosis and other forms of cell death are often controlled at one or more crucial steps involving the mitochondria. Recent findings, including an elegant investigation in a recent issue of Cell (Hao et al., 2005), have helped to elucidate fundamental aspects of this involvement while raising puzzling new questions about mitochondrial routes to cellular demise. The emerging, if preliminary, perspective these new studies provide may represent either a refinement of our views of how cells die or, perhaps, the beginnings of what amounts to a reformulation of our ideas.

[1]  T. Kuwana,et al.  BH3 domains of BH3-only proteins differentially regulate Bax-mediated mitochondrial membrane permeabilization both directly and indirectly. , 2005, Molecular cell.

[2]  M. Raff,et al.  Social controls on cell survival and cell death , 1992, Nature.

[3]  Brian J. Smith,et al.  Differential targeting of prosurvival Bcl-2 proteins by their BH3-only ligands allows complementary apoptotic function. , 2005, Molecular cell.

[4]  Tetsuya Watanabe,et al.  Cyclophilin D-dependent mitochondrial permeability transition regulates some necrotic but not apoptotic cell death , 2005, Nature.

[5]  Jeffrey Robbins,et al.  Loss of cyclophilin D reveals a critical role for mitochondrial permeability transition in cell death , 2005, Nature.

[6]  S. Korsmeyer,et al.  Review Cell Death: Critical Control Points Another Line of Evidence for the Importance of Caspases in Cell Death Came From , 2022 .

[7]  G. Salvesen,et al.  The protein structures that shape caspase activity, specificity, activation and inhibition. , 2004, The Biochemical journal.

[8]  D. Green,et al.  Do inducers of apoptosis trigger caspase-independent cell death? , 2005, Nature Reviews Molecular Cell Biology.

[9]  D. Newmeyer,et al.  A cytochrome c mutant with high electron transfer and antioxidant activities but devoid of apoptogenic effect. , 2002, The Biochemical journal.

[10]  A. Chadli THE CANCER CELL , 1924, La Presse medicale.

[11]  Chi Li,et al.  Growth Factor Regulation of Autophagy and Cell Survival in the Absence of Apoptosis , 2005, Cell.

[12]  Yigong Shi,et al.  Structure of the apoptotic protease-activating factor 1 bound to ADP , 2005, Nature.

[13]  T. Mak,et al.  Specific Ablation of the Apoptotic Functions of Cytochrome c Reveals a Differential Requirement for Cytochrome c and Apaf-1 in Apoptosis , 2005, Cell.

[14]  L. Buss,et al.  The evolution of individuality , 1987 .

[15]  David G. Watson,et al.  Succinate links TCA cycle dysfunction to oncogenesis by inhibiting HIF-alpha prolyl hydroxylase. , 2005, Cancer cell.

[16]  D. Green,et al.  Apaf-1 and caspase-9 do not act as tumor suppressors in myc-induced lymphomagenesis or mouse embryo fibroblast transformation , 2004, The Journal of cell biology.