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J Biol Chem, Vol. 274, Issue 25, 17946-17954, June 18, 1999
From the Center for Apoptosis Research and the Department of
Microbiology and Immunology, Kimmel Cancer Institute, Thomas Jefferson
University, Philadelphia, Pennsylvania 19107
Molecules that regulate NF-
CLAP, a Novel Caspase Recruitment Domain-containing Protein
in the Tumor Necrosis Factor Receptor Pathway, Regulates NF-
B
Activation and Apoptosis
B activation play
critical roles in apoptosis and inflammation. We describe the cloning
of the cellular homolog of the equine herpesvirus-2 protein E10 and
show that both proteins regulate apoptosis and NF-B activation.
These proteins were found to contain N-terminal caspase-recruitment domains (CARDs) and novel C-terminal domains (CTDs) and were therefore named CLAPs (CARD-like apoptotic
proteins). The cellular and viral CLAPs induce apoptosis
downstream of caspase-8 by activating the Apaf-1-caspase-9 pathway and
activate NF-B by acting upstream of the NF-B-inducing kinase,
NIK, and the IkB kinase, IKK
. Deletion of either the CARD or the CTD
domain inhibits both activities. The CARD domain was found to be
important for homo- and heterodimerization of CLAPs. Substitution of
the CARD domain with an inducible FKBP12 oligomerization domain
produced a molecule that can induce NF-B activation, suggesting that
the CARD domain functions as an oligomerization domain, whereas the CTD
domain functions as the effector domain in the NF-B activation
pathway. Expression of the CARD domain of human CLAP abrogates tumor
necrosis factor--induced NF-B activation, suggesting that
cellular CLAP plays an essential role in this pathway of NF-B activation.
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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