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Nod1, an Apaf-1-like activator of caspase-9 and nuclear factor-kappaB.

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-kappaB) and bound RICK, a CARD-containing kinase that also induces NF-kappaB activation. Nod1 mutants inhibited NF-kappaB activity induced by RICK, but not that resulting from tumor necrosis factor-alpha stimulation. Thus, Nod1 is a leucine-rich repeat-containing Apaf-1-like molecule that can regulate both apoptosis and NF-kappaB activation pathways.

Pubmed ID: 10329646


  • Inohara N
  • Koseki T
  • del Peso L
  • Hu Y
  • Yee C
  • Chen S
  • Carrio R
  • Merino J
  • Liu D
  • Ni J
  • Núñez G


The Journal of biological chemistry

Publication Data

May 21, 1999

Associated Grants

  • Agency: NCI NIH HHS, Id: K04 CA64421
  • Agency: NCI NIH HHS, Id: R01 CA64556

Mesh Terms

  • Adaptor Proteins, Signal Transducing
  • Amino Acid Sequence
  • Apoptosis
  • Apoptotic Protease-Activating Factor 1
  • Carrier Proteins
  • Caspase 9
  • Caspases
  • Chromosome Mapping
  • Humans
  • Molecular Sequence Data
  • Mutation
  • NF-kappa B
  • Nod1 Signaling Adaptor Protein
  • Proteins