Abstract: The control of caspase activity has emerged as being crucial for achieving cellular homeostasis. Apoptotic signals from both outside and inside the cell converge on the caspase cascade, which ultimately results in the orderly disassembly of the apoptotic cell. It is important for the cell to keep caspases in check. Members of the inhibitor of apoptosis (IAP) family of genes fulfil the role of cellular caspase inhibitors because they can bind to and inhibit both the initiator and effector caspases and thus prevent amplification of the caspase cascade. However, the uncontrolled inhibition of caspases would prevent the execution of cell death when needed. A mitochondrial protein called Smac/DIABLO prevents IAPs from binding to caspases and therefore promotes cell death. However, it normally resides in the mitochondria and is only released concomitantly with cytochrome c following an apoptotic stimulus. Therefore, pathways of apoptosis that do not involve mitochondria cannot be modulated by the activity of Smac/DIABLO.
Publication Year: 2001
Publication Date: 2001-08-01
Language: en
Type: article
Indexed In: ['crossref', 'pubmed']
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Cited By Count: 1
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