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Receptor interacting protein is ubiquitinated by cellular inhibitor of apoptosis proteins (c‐IAP1 and c‐IAP2) in vitro
Author(s) -
Park Sun-Mi,
Yoon Jong-Bok,
Lee Tae H.
Publication year - 2004
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2004.04.021
Subject(s) - ubiquitin ligase , ubiquitin , traf2 , microbiology and biotechnology , inhibitor of apoptosis , proteasome , apoptosis , biology , receptor , in vitro , xiap , protein degradation , tumor necrosis factor receptor 1 , programmed cell death , biochemistry , caspase , tumor necrosis factor receptor , gene
Receptor interacting protein (RIP) is recruited to tumor necrosis factor‐α receptor 1 (TNFR1) complex upon stimulation and plays a crucial role in the receptor‐mediated NF‐κB activation. Among the components of the TNFR1 complex are proteins that possess ubiquitin‐protein isopeptide ligase (E3) activities, such as TNFR1‐associated factor 2 (TRAF2), cellular inhibitor of apoptosis proteins (c‐IAPs) namely, c‐IAP1 and c‐IAP2. Here, we showed that ectopically expressed RIP is ubiquitinated, and either the intermediate or death domain of RIP is required for this modification. Expression of c‐IAP1 and c‐IAP2 decreased the steady‐state level of RIP, which was blocked by inhibition of the 26S proteasome. RIP degradation requires intact c‐IAP2 containing the RING domain. Our in vitro ubiquitination assay revealed that while TRAF2 had no effect, both c‐IAP1 and c‐IAP2‐mediated RIP ubiquitination with similar efficiency, indicating that c‐IAPs can function as E3 toward RIP.