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. 2015 Jan 1;26(1):151–160. doi: 10.1091/mbc.E14-08-1277

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© 2015 Wi, Park, et al. This article is distributed by The American Society for Cell Biology under license from the author(s). Two months after publication it is available to the public under an Attribution–Noncommercial–Share Alike 3.0 Unported Creative Commons License (http://creativecommons.org/licenses/by-nc-sa/3.0).

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FIGURE 8: — Model detailing the roles of ECSIT in TLR4-mediated signaling. On TLR4 stimulation, ECSIT forms the TAK1/TRAF6 complex, in which TAK1 is activated and ECSIT is simultaneously ubiquitinated on K372 by TRAF6. Activated TAK1 activates the IKKs complex through phosphorylation, leading to IκB-α degradation through phosphorylation and polyubiquitination. The dissociated p65/p50 NF-κB proteins from IκB-α interact with K372-ubiquitinated ECSIT and translocates to the nucleus, leading to the induction of p65/p50-dependent gene expression.