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- W2605815386 abstract "The PIDDosome (PIDD–RAIDD–caspase-2 complex) is considered to be the primary signaling platform for caspase-2 activation in response to genotoxic stress. Yet studies of PIDD-deficient mice show that caspase-2 activation can proceed in the absence of PIDD. Here we show that DNA damage induces the assembly of at least two distinct activation platforms for caspase-2: a cytoplasmic platform that is RAIDD dependent but PIDD independent, and a nucleolar platform that requires both PIDD and RAIDD. Furthermore, the nucleolar phosphoprotein nucleophosmin (NPM1) acts as a scaffold for PIDD and is essential for PIDDosome assembly in the nucleolus after DNA damage. Inhibition of NPM1 impairs caspase-2 processing, apoptosis, and caspase-2–dependent inhibition of cell growth, demonstrating that the NPM1-dependent nucleolar PIDDosome is a key initiator of the caspase-2 activation cascade. Thus we have identified the nucleolus as a novel site for caspase-2 activation and function." @default.
- W2605815386 created "2017-04-28" @default.
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- W2605815386 date "2017-04-21" @default.
- W2605815386 modified "2023-10-15" @default.
- W2605815386 title "NPM1 directs PIDDosome-dependent caspase-2 activation in the nucleolus" @default.
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- W2605815386 doi "https://doi.org/10.1083/jcb.201608095" @default.
- W2605815386 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/5461015" @default.
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