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Comment
. 2009 Apr 20;185(2):189-91.
doi: 10.1083/jcb.200903134.

Puma strikes Bax

Anthony Letai  1
Affiliations
Comment

Puma strikes Bax

Anthony Letai. J Cell Biol. .

Abstract

The commitment to programmed cell death via apoptosis is largely made upon activation of the proapoptotic mitochondrial proteins Bax or Bak. In this issue, Gallenne et al. (Gallenne, C., F. Gautier, L. Oliver, E. Hervouet, B. Noël, J.A. Hickman, O. Geneste, P.-F. Cartron, F.M. Vallette, S. Manon, and P. Juin. 2009. J. Cell Biol. 185:279-290) provide evidence that the p53 up-regulated modulator of apoptosis (Puma) protein can directly activate Bax.

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Figures

Figure 1.
Figure 1.
Control of mitochondrial permeabilization by Bcl-2 family proteins. Activated Bax or Bak are available to oligomerize either when they are directly activated by activating factors, including activator BH3-only proteins (top), or when preactivated Bax or Bak are displaced from antiapoptotic proteins by either activator or sensitizer BH3-only proteins (bottom). Gallenne et al. (2009) provide evidence that Puma is an activator rather than a sensitizer. Oligomerized Bax or Bak participate in forming a pore that allows egress of proapoptotic factors like cytochrome c. Cytochrome c promotes formation of the apoptosome complex, which causes activation of effector caspases. These proteases cleave many key cellular proteins to bring about the apoptotic phenotype. Figure adapted with permission from the Journal of Cell Science (Brunelle, J.K., and A. Letai. 2009. J. Cell Sci. 122:437–441).
See this image and copyright information in PMC

Comment on

References

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