TY - JOUR
T1 - CIPER, a novel NF κB-activating protein containing a caspase recruitment domain with homology to Herpesvirus-2 protein E10
AU - Koseki, Takeyoshi
AU - Inohara, Naohiro
AU - Chen, Shu
AU - Carrio, Roberto
AU - Merino, Jesus
AU - Hottiger, Michael O.
AU - Nabel, Gary J.
AU - Núñez, Gabriel
PY - 1999/4/9
Y1 - 1999/4/9
N2 - We have identified and characterized CIPER, a novel protein containing a caspase recruitment domain (CARD) in its N terminus and a C-terminal region rich in serine and threonine residues. The CARD of CIPER showed striking similarity to E10, a product of the equine herpesvirus-2. CIPER formed homodimers via its CARD and interacted with viral E10 but not with several apoptosis regulators containing CARDs including ARC, RAIDD, RICK, caspase-2, caspase-9, or Apaf-1. Expression of CIPER induced NF-κB activation, which was inhibited by dominant-negative NIK and a nonphosphorylable IκB-α mutant but not by dominant-negative RIP. Mutational analysis revealed that the N- terminal region of CIPER containing the CARD was sufficient and necessary for NF-κB-inducing activity. Point mutations in highly conserved residues in the CARD of CIPER disrupted the ability of CIPER to activate NF-κB and to form homodimers, indicating that the CARD is essential for NF-κB activation and dimerization. We propose that CIPER acts in a NIK-dependent pathway of NF- κB activation.
AB - We have identified and characterized CIPER, a novel protein containing a caspase recruitment domain (CARD) in its N terminus and a C-terminal region rich in serine and threonine residues. The CARD of CIPER showed striking similarity to E10, a product of the equine herpesvirus-2. CIPER formed homodimers via its CARD and interacted with viral E10 but not with several apoptosis regulators containing CARDs including ARC, RAIDD, RICK, caspase-2, caspase-9, or Apaf-1. Expression of CIPER induced NF-κB activation, which was inhibited by dominant-negative NIK and a nonphosphorylable IκB-α mutant but not by dominant-negative RIP. Mutational analysis revealed that the N- terminal region of CIPER containing the CARD was sufficient and necessary for NF-κB-inducing activity. Point mutations in highly conserved residues in the CARD of CIPER disrupted the ability of CIPER to activate NF-κB and to form homodimers, indicating that the CARD is essential for NF-κB activation and dimerization. We propose that CIPER acts in a NIK-dependent pathway of NF- κB activation.
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U2 - 10.1074/jbc.274.15.9955
DO - 10.1074/jbc.274.15.9955
M3 - Article
C2 - 10187770
AN - SCOPUS:0033537840
SN - 0021-9258
VL - 274
SP - 9955
EP - 9961
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 15
ER -