摘要：

Presents a study showing that X-linked inhibitor-of-apoptosis protein (XIAP) associates with the active caspase-9-Apaf-1 holoenzyme complex through binding to the amino terminus of the linker peptide on the small subunit of caspase-9, which becomes exposed after proteolytic processing of procaspase-9 at Asp 315. Finding of a mechanism in which binding to the BIR3 domain by two conserved peptides, one from Smac and one from caspase-9, has opposing effects on caspase activity and apoptosis.

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