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Abstract
Engagement of the interleukin-17 (IL-17) receptor complex triggers activation of the transcription factor nuclear factor κB (NF-κB). A wide array of signaling molecules can contribute to the activation of NF-κB, but a number of common themes link the receptors engaged to activate it with the translocation of the active complex to the nucleus; among these is a clear role for ubiquitination. Ubiquitination is essential to the degradation of the inhibitor of NF-κB (IκB) subunits, which otherwise retain the inactive NF-κB complex in the cytosol. However, additional roles for ubiquitination in the assembly of signaling complexes and in enzyme activation are underappreciated aspects of NF-κB induction pathways. These roles require a form of ubiquitination biochemically distinct from that which targets proteins for degradation. The identification of Act1, an adaptor protein of the IL-17 receptor, as an E3 ubiquitin ligase capable of initiating this modification provides an impressive connection between the IL-17 receptor complex and pathways that activate NF-κB.
