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PMID:10187770
| Citation |
Koseki, T, Inohara, N, Chen, S, Carrio, R, Merino, J, Hottiger, MO, Nabel, GJ and Núñez, G (1999) CIPER, a novel NF kappaB-activating protein containing a caspase recruitment domain with homology to Herpesvirus-2 protein E10. J. Biol. Chem. 274:9955-61 |
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| Abstract |
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-kappaB activation, which was inhibited by dominant-negative NIK and a nonphosphorylable IkappaB-alpha 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-kappaB-inducing activity. Point mutations in highly conserved residues in the CARD of CIPER disrupted the ability of CIPER to activate NF-kappaB and to form homodimers, indicating that the CARD is essential for NF-kappaB activation and dimerization. We propose that CIPER acts in a NIK-dependent pathway of NF-kappaB activation. |
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| Keywords |
Adaptor Proteins, Signal Transducing; Amino Acid Sequence; Animals; Apoptosis; Apoptotic Protease-Activating Factor 1; Blotting, Northern; Caenorhabditis elegans Proteins; Carrier Proteins/chemistry; Carrier Proteins/metabolism; Caspase 2; Caspase 9; Caspases/chemistry; Caspases/metabolism; Cysteine Endopeptidases/chemistry; Enzyme Activation; Expressed Sequence Tags; Humans; Jurkat Cells; Mice; Molecular Sequence Data; NF-kappa B/metabolism; Neoplasm Proteins/chemistry; Neoplasm Proteins/genetics; Neoplasm Proteins/physiology; Point Mutation; Proteins/chemistry; Sequence Homology, Amino Acid |
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Significance
Annotations
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