CIPER, a novel NF κB-activating protein containing a caspase recruitment domain with homology to Herpesvirus-2 protein E10

Takeyoshi Koseki, Naohiro Inohara, Shu Chen, Roberto Carrio, Jesus Merino, Michael O. Hottiger, Gary J. Nabel, Gabriel Núñez

Research output: Contribution to journalArticle

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-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.

Original languageEnglish (US)
Pages (from-to)9955-9961
Number of pages7
JournalJournal of Biological Chemistry
Volume274
Issue number15
DOIs
StatePublished - Apr 9 1999
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry

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    Koseki, T., Inohara, N., Chen, S., Carrio, R., Merino, J., Hottiger, M. O., Nabel, G. J., & Núñez, G. (1999). CIPER, a novel NF κB-activating protein containing a caspase recruitment domain with homology to Herpesvirus-2 protein E10. Journal of Biological Chemistry, 274(15), 9955-9961. https://doi.org/10.1074/jbc.274.15.9955