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Caspase‐2 is resistant to inhibition by inhibitor of apoptosis proteins (IAPs) and can activate caspase‐7
Author(s) -
Ho Poki,
Jabbour Anissa M.,
Ekert Paul G.,
Hawkins Christine J.
Publication year - 2005
Publication title -
the febs journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.981
H-Index - 204
eISSN - 1742-4658
pISSN - 1742-464X
DOI - 10.1111/j.1742-4658.2005.04573.x
Subject(s) - caspase , apoptosis , microbiology and biotechnology , caspase 2 , proteases , caspase 3 , caspase 8 , cysteine , caspase 10 , caspase 9 , xiap , recombinant dna , inhibitor of apoptosis domain , chemistry , signal transduction , biology , biochemistry , enzyme , programmed cell death , gene
Caspases are a family of cysteine proteases with roles in cytokine maturation or apoptosis. Caspase‐2 was the first pro‐apoptotic caspase identified, but its functions in apoptotic signal transduction are still being elucidated. This study examined the regulation of the activity of caspase‐2 using recombinant proteins and a yeast‐based system. Our data suggest that for human caspase‐2 to be active its large and small subunits must be separated. For maximal activity its prodomain must also be removed. Consistent with its proposed identity as an upstream caspase, caspase‐2 could provoke the activation of caspase‐7. Caspase‐2 was not subject to inhibition by members of the IAP family of apoptosis inhibitors.