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J Biol Chem, Vol. 274, Issue 21, 14560-14567, May 21, 1999
B
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From the Ced-4 and Apaf-1 belong to a major class of
apoptosis regulators that contain caspase-recruitment (CARD) and
nucleotide-binding oligomerization domains. Nod1, a protein with an
NH2-terminal CARD-linked to a nucleotide-binding
domain and a COOH-terminal segment with multiple leucine-rich repeats,
was identified. Nod-1 was found to bind to multiple caspases with long
prodomains, but specifically activated caspase-9 and promoted
caspase-9-induced apoptosis. As reported for Apaf-1, Nod1 required both
the CARD and P-loop for function. Unlike Apaf-1, Nod1 induced
activation of nuclear factor-kappa-B (NF- Department of Pathology and Comprehensive
Cancer Center, The University of Michigan Medical School, Ann Arbor,
Michigan 48109, the ** Unidad de Inmunologia, Departamento de Biologia
Molecular, Universidad de Cantabria, Santander 39011, Spain, and
§§ Human Genome Sciences,
Rockville, Maryland 20850
B) and bound RICK, a
CARD-containing kinase that also induces NF-B activation. Nod1
mutants inhibited NF-B activity induced by RICK, but not that
resulting from tumor necrosis factor-
stimulation. Thus, Nod1 is a
leucine-rich repeat-containing Apaf-1-like molecule that can regulate
both apoptosis and NF-B activation pathways.
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