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. 2016 Sep 15;9:84. doi: 10.3389/fnmol.2016.00084

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Copyright © 2016 Leibowitz and Yan.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution and reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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The IL-1β-activated canonical NF-κB signaling pathway. The receptor is activated by IL-1β and recruits MyD88 through homophilic interactions between toll/interleukin-1 receptor (TIR) domains. MyD88 interacts with IRAK1, IRAK2, IRAKM and IRAK4. IRAK4 is phosphorylated and then phosphorylates and activates IRAK1. IRAK1 and IRAK4 interact with TRAF6 which self-ubiquitinates and also ubiquitinates NEMO through Ubc13-Uev1a, in complex with TRAF6. NEMO and TRAF6 recruit TAK1 in complex with TABs1–3. TAK1, activates IKKβ, which then phosphorylates IκB-α. IκB-α is then ubiquitinated and degraded, releasing NF-κB and allowing translocation into the nucleus. P, phosphate; U, ubiquitin.