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Sci. Signal., 13 October 2009
Vol. 2, Issue 92, p. pe64
[DOI: 10.1126/scisignal.292pe64]


IL-17 Receptor Signaling: Ubiquitin Gets In On the Act

Steven D. Levin*

Department of Immunology, ZymoGenetics Inc., 1201 Eastlake Avenue E, Seattle, WA 98102, USA.

Abstract: Engagement of the interleukin-17 (IL-17) receptor complex triggers activation of the transcription factor nuclear factor {kappa}B (NF-{kappa}B). A wide array of signaling molecules can contribute to the activation of NF-{kappa}B, 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-{kappa}B (I{kappa}B) subunits, which otherwise retain the inactive NF-{kappa}B complex in the cytosol. However, additional roles for ubiquitination in the assembly of signaling complexes and in enzyme activation are underappreciated aspects of NF-{kappa}B 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-{kappa}B.

* Corresponding author. E-mail, levins{at}

Citation: S. D. Levin, IL-17 Receptor Signaling: Ubiquitin Gets In On the Act. Sci. Signal. 2, pe64 (2009).

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