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

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ASC is an activating adaptor for NF-kappa B and caspase-8-dependent apoptosis.

ASC is a pro-apoptotic protein containing a pyrin domain (PD) and a caspase-recruitment domain (CARD). A previous study suggests that ASC interacts with Ipaf, a member of the Apaf-1/Nod1 protein family. However, the functional relevance of the interaction has not been determined. Here, we report that co-expression of ASC with Ipaf or oligomerization of ASC induces both apoptosis and NF-kappa B activation. Apoptosis induced through ASC was inhibited by a mutant form of Caspase-8 but not by that of Caspase-1. The PD of ASC physically interacted with Caspase-8 as well as with pyrin, the familial Mediterranean fever gene product. Caspase-8 deficiency rescued mouse fibroblasts from apoptosis induced by ASC oligomerization. Pyrin disrupted the interaction between ASC and Caspase-8, and inhibited both apoptosis and NF-kappa B activation induced by ASC. These findings suggest that ASC is a mediator of NF-kappa B activation and Caspase-8-dependent apoptosis in an Ipaf signaling pathway.[1]

References

  1. ASC is an activating adaptor for NF-kappa B and caspase-8-dependent apoptosis. Masumoto, J., Dowds, T.A., Schaner, P., Chen, F.F., Ogura, Y., Li, M., Zhu, L., Katsuyama, T., Sagara, J., Taniguchi, S., Gumucio, D.L., Núñez, G., Inohara, N. Biochem. Biophys. Res. Commun. (2003) [Pubmed]
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