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J Biol Chem, Vol. 274, Issue 15, 9955-9961, April 9, 1999
B-activating Protein Containing a Caspase
Recruitment Domain with Homology to Herpesvirus-2 Protein
E10
,,,
From the 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- Department of Pathology and Comprehensive
Cancer Center and the ** Howard Hughes Medical Institute and
Departments of Internal Medicine and Biological Chemistry, The
University of Michigan Medical School, Ann Arbor, Michigan 48109, and the ¶ Unidad de Inmunologia, Departamento de Biologia
Molecular, Universidad de Cantabria, Santander 39011, Spain
B activation, which was
inhibited by dominant-negative NIK and a nonphosphorylable IB-
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-B-inducing activity. Point mutations
in highly conserved residues in the CARD of CIPER disrupted the ability
of CIPER to activate NF-B and to form homodimers, indicating that
the CARD is essential for NF-B activation and dimerization. We
propose that CIPER acts in a NIK-dependent pathway of
NF-B activation.
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