Phosphorylation of IkappaB-alpha inhibits its cleavage by caspase CPP32 in vitro - PubMed (original) (raw)
. 1997 Nov 21;272(47):29419-22.
doi: 10.1074/jbc.272.47.29419.
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- PMID: 9367996
- DOI: 10.1074/jbc.272.47.29419
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Phosphorylation of IkappaB-alpha inhibits its cleavage by caspase CPP32 in vitro
M Barkett et al. J Biol Chem. 1997.
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Abstract
IkappaB proteins function as direct regulators of Rel/NF-kappaB transcription complexes. We show that the cell-death protease CPP32 (caspase-3) in vitro specifically cleaved chicken and human IkappaB-alpha at a conserved Asp-Ser sequence. This cleavage site appears to be identical to the site at which chicken IkappaB-alpha is cleaved in vivo in temperature-sensitive v-Rel-transformed chicken spleen cells undergoing apoptosis. Other caspases, namely interleukin-1beta-converting enzyme (caspase-1) and Ich-1 (caspase-2), did not cleave IkappaB-alpha. CPP32 also cleaved mammalian IkappaB-beta in vitro at the analogous Asp-Ser sequence. Cleavage of IkappaB-alpha by CPP32 was blocked by serine phosphorylation of IkappaB-alpha. Cleavage of IkappaB-alpha by a CPP32- like protease could generate a constitutive inhibitor of Rel transcription complexes. This report provides evidence for a direct biochemical interaction between the NF-kappaB signaling pathway and a cell-death protease signaling pathway.
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