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Caspase‐3 and inhibitor of apoptosis protein(s) interactions in Saccharomyces cerevisiae and mammalian cells
Author(s) -
Wright Michael E,
Han David K,
Hockenbery David M
Publication year - 2000
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(00)01962-1
Subject(s) - xiap , inhibitor of apoptosis , apoptosis , caspase , survivin , microbiology and biotechnology , biology , inhibitor of apoptosis domain , camptothecin , saccharomyces cerevisiae , transfection , programmed cell death , yeast , biochemistry , gene
Using a heterologous yeast expression assay, we show that inhibitor of apoptosis proteins (IAPs) suppress caspase‐3‐mediated cytotoxicity in the order of XIAP>c‐IAP2>c‐IAP1>survivin. The same ordering of IAP activities was demonstrated in mammalian cells expressing an auto‐activating caspase‐3. The relative anti‐apoptotic activities of each IAP depended on the particular death stimulus. For IAP‐expressing cells treated with camptothecin, survival correlated with their intrinsic anti‐caspase‐3 activity. However, c‐IAP1‐transfected cells were disproportionately resistant to tumor necrosis factor‐α, suggesting that its anti‐apoptotic activities extend beyond caspase‐3 or ‐7 inhibition. Yeast‐based caspase assays provide rapid, reliable information on specificity and activity of the IAPs and aid in identifying critical targets in mammalian apoptotic pathways.