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  • Title: Substrate cleavage by caspases generates protein fragments with Smac/Diablo-like activities.
    Author: Hell K, Saleh M, Crescenzo GD, O'Connor-McCourt MD, Nicholson DW.
    Journal: Cell Death Differ; 2003 Nov; 10(11):1234-9. PubMed ID: 14576775.
    Abstract:
    Smac/Diablo and HtrA2/Omi promote apoptosis by binding to and antagonizing IAP proteins, including the 'X chromosome-linked inhibitor of apoptosis' (XIAP). Here we show that caspase-mediated proteolysis of a limited subset of cell death substrates exposes functional Smac/Diablo-like N-termini after cleavage, which are able to bind to and antagonize XIAP. We propose that this mechanism may establish a feedforward sensitization of the apoptotic pathway and contribute to the functional redundancy of IAP antagonism. In addition, this may be particularly relevant in Alzheimer's disease since the caspase-generated C31 peptide, an established cytotoxin, acquires Smac/Diablo-like properties after apoptotic processing.
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