Conclusions
Mitochondria are now appreciated as being important in the control of cell survival and cell death. Most apoptotic signaling processes converge on the mitochondria, which releases cytochrome c, leading to the activation of effector caspases. The response of mitochondria to upstream proapoptotic signals is a critical control point for the regulation of cell death. It certainly involves phospholipids which provide specificity to target proapoptotic proteins to mitochondria and enable them to interact with Bcl-2 members or with other proteins to release cytochrome c. Despite these successes, we are mostly in the dark at the mechanism of how phospholipids regulate such interactions. The challenge in the future will be to explore how phospholipids control such interaction. This implies that more specific interactions between individual lipids and proteins associated with apoptosis have to be established and their molecular base to be identified. Given the importance of phospholipid/protein interactions for the maintenance of mitochondrial hoemostasis, it would be not surprising if they serve as useful targets for drug intervention. For instance anticancer drugs could be designed that prevent such interactions resulting in loss of mitochondrial integrity and ultimately in cell death.
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Lehmann, V., Shatrov, V. (2004). Lipid Metabolism and Release of Cytochrome c from Mitochondria. In: Quinn, P.J., Kagan, V.E. (eds) Phospholipid Metabolism in Apoptosis. Subcellular Biochemistry, vol 36. Springer, Boston, MA. https://doi.org/10.1007/0-306-47931-1_1
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