[The role of the interaction between signaling protein domains and of the complexes of signaling proteins in apoptosis initiation].
The data of recent years on apoptosis were revisited to demonstrate that the functioning of signaling proteins during apoptosis depends on their localization on mitochondria or in the cytosol. The major effect of signaling proteins depends on the number of pro- and antiapoptotic domains in their structure, which is observed after cleavage, oligomerization, and complexing with other proteins. The structure of known signaling proteins was analyzed. The effect of complexing with phosphatases and 14-3-3 proteins was demonstrated by the example of Bad protein. Detailed data on the proapoptotic factors and their inhibitors affecting caspase activation and released from mitochondria with cytochrome c are given.
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D048948:14-3-3 Proteins / Q000378:metabolism*; D000818:Animals; D017209:Apoptosis / Q000502:physiology*; D006801:Humans; D010749:Phosphoprotein Phosphatases / Q000378:metabolism*; D017434:Protein Structure, Tertiary / Q000502:physiology; D015398:Signal Transduction / Q000502:physiology*; D051025:bcl-Associated Death Protein / Q000378:metabolism*
D048948:14-3-3 Proteins; D051025:bcl-Associated Death Protein; D010749:Phosphoprotein Phosphatases