PIDD mediates and stabilizes the interaction between RAIDD and Caspase-2 for the PIDDosome assembly

Title
PIDD mediates and stabilizes the interaction between RAIDD and Caspase-2 for the PIDDosome assembly
Author(s)
박현호장태호
Keywords
PROGRAMMED CELL-DEATH; CRYSTAL-STRUCTURE; THERAPEUTIC TARGETS; SIGNALING PATHWAY; APOPTOSIS; DOMAIN; ACTIVATION; PROTEIN; CANCER; COMPLEX
Issue Date
201309
Publisher
KOREAN SOCIETY BIOCHEMISTRY & MOLECULAR BIOLOGY
Citation
BMB REPORTS, v.46, no.9, pp.471 - 476
Abstract
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.
URI
http://hdl.handle.net/YU.REPOSITORY/29000http://dx.doi.org/10.5483/BMBRep.2013.46.9.021
ISSN
1976-6696
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이과대학 > 화학생화학부 > Articles
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