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KMID : 0624620130460090471
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BMB Reports
2013 Volume.46 No. 9 p.471 ~ p.476
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PIDD mediates and stabilizes the interaction between RAIDD and Caspase-2 for the PIDDosome assembly
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Jang Tae-Ho
Park Hyun-Ho
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Abstract
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The PIDDosome, which is an oligomeric signaling complex composed of PIDD, RAIDD and caspase-2, can induce proximity-based dimerization and activation of caspase-2. In the PIDDosome assembly, the adaptor protein RAIDD interacts with PIDD and caspase-2 via CARD:CARD and DD:DD, respectively. To analyze the PIDDosome assembly, we purified all of the DD superfamily members and performed biochemical analyses. The results revealed that caspase-2 CARD is an insoluble protein that can be solubilized by its binding partner, RAIDD CARD, but not by full-length RAIDD; this indicates that full-length RAIDD in closed states cannot interact with caspase-2 CARD. Moreover, we found that caspase-2 CARD can be solubilized and interact with full-length RAIDD in the presence of PIDD DD, indicating that PIDD DD initially binds to RAIDD, after which caspase-2 can be recruited to RAIDD via a CARD:CARD interaction. Our study will be useful in determining the order of assembly of the PIDDosome.
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KEYWORD
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Apoptosis, CARD, Caspase-2, DD, PIDD, PIDDosome, RAIDD
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