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Identification and analysis of dominant negative mutants of RAIDD and PIDD

Cited 12 time in Web of Science Cited 12 time in Scopus
Authors
Jang, Tae-Ho; Bae, Ju Young; Park, Ok Kyoung; Kim, Ji Hoe; Park, Hyun Ho; Jeon, Ju-Hong; Cho, Kyung-Hyun
Issue Date
2010-07
Publisher
ELSEVIER SCIENCE BV
Citation
BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS; Vol.1804 7; 1557-1563
Keywords
ApoptosisRAIDDDominant negative mutantPIDD PIDDosomeDISCInflammationApoptosomeCaspase-2
Abstract
Caspases are cysteine proteases that are essential during the initiation and execution of apoptosis and inflammation. The formation of large oligomeric protein complexes is critical to the activation of caspases in apoptotic and inflammatory signaling pathways. These oligomeric protein complexes function as a platform to recruit caspases, which leads to caspase activation via a proximity-induced mechanism. One well-known oligomeric caspase-activating complex is the PIDDosome for caspase-2 activation, which is composed of 3 protein components, PIDD, RAIDD and Caspase-2. Despite the significant role that caspase-2 activated by PIDDosome plays during genotoxic stress-induced apoptosis, the oligomerization mechanism and the method by which the caspase-activating process is mediated by the formation of PIDDosome is currently not well understood. Here, we show that the assembly mechanism of the core of PIDDosome is time-dependent and salt concentration-dependent. In addition, we demonstrate that point mutations on RAIDD (R147E) and on PLOD (Y814A) exert a dominant negative effect on the formation of the PIDDosome, and that this effect cannot be applied after the PIDDosome has been formed. Crown Copyright (C) 2010 Published by Elsevier B.V. All rights reserved.
ISSN
1570-9639
Language
English
URI
http://hdl.handle.net/10371/76220
DOI
https://doi.org/10.1016/j.bbapap.2010.04.006
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College of Medicine/School of Medicine (의과대학/대학원)Dept. of Physiology (생리학교실)Journal Papers (저널논문_생리학교실)
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