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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 TNF-α-activated canonical nuclear factor kappa-light-chain-enhancer of activated B cells (NF-κB) signaling pathway. TNF-α triggers TNF-R1 receptor trimerization. TNF receptor type 1-associated death domain protein (TRADD) is then recruited which, in turn, recruits TNF receptor-associated factor 2 (TRAF2) and receptor-interacting protein 1 (RIP1). TRAF2 mediates K63-linked polyubiquitination of RIP1 which allows recruitment of TAB2 and NF-κB essential modulator (NEMO). Following this, TAB2 recruits transforming growth factor beta-activated kinase 1 (TAK1) while NEMO and TRAF2 recruit the IKK complex. TAK1 phosphorylates 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.