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    Trends Biochem Sci. 2008 Apr;33(4):171-80. Epub 2008 Mar 18.

    Are the IKKs and IKK-related kinases TBK1 and IKK-epsilon similarly activated?

    Chau TL, Gioia R, Gatot JS, Patrascu F, Carpentier I, Chapelle JP, O'Neill L, Beyaert R, Piette J, Chariot A.

    Source

    Interdisciplinary Cluster for Applied Genoproteomics, University of Liège, Sart-Tilman, 4000 Liège, Belgium.

    Abstract

    The IkappaB kinases (IKKs) IKK-alpha and IKK-beta, and the IKK-related kinases TBK1 and IKK-epsilon, have essential roles in innate immunity through signal-induced activation of NF-kappaB, IRF3 and IRF7, respectively. Although the signaling events within these pathways have been extensively studied, the mechanisms of IKK and IKK-related complex assembly and activation remain poorly defined. Recent data provide insight into the requirement for scaffold proteins in complex assembly; NF-kappaB essential modulator coordinates some IKK complexes, whereas TANK, NF-kappaB-activating kinase-associated protein 1 (NAP1) or similar to NAP1 TBK1 adaptor (SINTBAD) assemble TBK1 and IKK-epsilon complexes. The different scaffold proteins undergo similar post-translational modifications, including phosphorylation and non-degradative polyubiquitylation. Moreover, increasing evidence indicates that distinct scaffold proteins assemble IKK, and potentially TBK1 and IKK-epsilon subcomplexes, in a stimulus-specific manner, which might be a mechanism to achieve specificity.

    PMID:
    18353649
    [PubMed - indexed for MEDLINE]

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