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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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An induced proximity model for NF-kappa B activation in the Nod1/RICK and RIP signaling pathways.

Nod1 is an Apaf-1-like molecule composed of a caspase-recruitment domain (CARD), nucleotide-binding domain, and leucine-rich repeats that associates with the CARD-containing kinase RICK and activates nuclear factor kappaB (NF-kappaB). We show that self-association of Nod1 mediates proximity of RICK and the interaction of RICK with the gamma subunit of the IkappaB kinase (IKKgamma). Similarly, the RICK-related kinase RIP associated via its intermediate region with IKKgamma. A mutant form of IKKgamma deficient in binding to IKKalpha and IKKbeta inhibited NF-kappaB activation induced by RICK or RIP. Enforced oligomerization of RICK or RIP as well as of IKKgamma, IKKalpha, or IKKbeta was sufficient for induction of NF-kappaB activation. Thus, the proximity of RICK, RIP, and IKK complexes may play an important role for NF-kappaB activation during Nod1 oligomerization or trimerization of the tumor necrosis factor alpha receptor.[1]

References

  1. An induced proximity model for NF-kappa B activation in the Nod1/RICK and RIP signaling pathways. Inohara, N., Koseki, T., Lin, J., del Peso, L., Lucas, P.C., Chen, F.F., Ogura, Y., Núñez, G. J. Biol. Chem. (2000) [Pubmed]
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