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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 
 
 
 
 

Substrate cleavage by caspases generates protein fragments with Smac/Diablo-like activities.

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.[1]

References

  1. Substrate cleavage by caspases generates protein fragments with Smac/Diablo-like activities. Hell, K., Saleh, M., Crescenzo, G.D., O'Connor-McCourt, M.D., Nicholson, D.W. Cell Death Differ. (2003) [Pubmed]
 
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