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RIP2 is a novel NF-kappaB-activating and cell death-inducing kinase.

Through specific interactions with members of the tumor necrosis receptor (TNFR) family, adapter molecules such as the serine/threonine (Ser/Thr) kinase RIP mediate divergent signaling pathways including NF-kappaB activation and cell death. In this study, we have identified and characterized a novel 61-kDa protein kinase related to RIP that is a component of both the TNFR-1 and the CD40 signaling complexes. Receptor interacting protein-2 (RIP2) contains an N-terminal domain with homology to Ser/Thr kinases and a C-terminal caspase activation and recruitment domain (CARD), a homophilic interaction motif that mediates the recruitment of caspase death proteases. Overexpression of RIP2 signaled both NF-kappaB activation and cell death. Mutational analysis revealed the pro-apoptotic function of RIP2 to be restricted to its C-terminal CARD domain, whereas the intact molecule was necessary for NF-kappaB activation. RIP2 interacted with other members of the TNFR-1 signaling complex, including inhibitor of apoptosis protein cIAP1 and with members of the TNFR-associated factor (TRAF) family, specifically TRAF1, TRAF5, and TRAF6, but not with TRAF2, TRAF3, or TRAF4. These TRAF interactions mediate the recruitment of RIP2 to receptor signaling complexes.

Pubmed ID: 9642260


  • McCarthy JV
  • Ni J
  • Dixit VM


The Journal of biological chemistry

Publication Data

July 3, 1998

Associated Grants


Mesh Terms

  • Amino Acid Sequence
  • Animals
  • Apoptosis
  • Cloning, Molecular
  • Humans
  • Inhibitor of Apoptosis Proteins
  • Mice
  • Molecular Sequence Data
  • NF-kappa B
  • Phosphotransferases
  • Protein-Serine-Threonine Kinases
  • Proteins
  • Receptor-Interacting Protein Serine-Threonine Kinase 2
  • Receptor-Interacting Protein Serine-Threonine Kinases
  • Sequence Homology, Amino Acid