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. 2016 Mar 1;2:15048. doi: 10.1038/celldisc.2015.48

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Copyright © 2016 SIBS, CAS

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A model for the cooperative regulation between TRIP6 and TRAF6 in the LPA2 receptor signaling. Upon LPA stimulation, TRIP6 is targeted to the plasma membrane, where it forms a complex with the LPA2 receptor and NHERF2, and serves as a scaffold to recruit TRAF6, c-Src and AKT. Together, they coordinate to activate ERK, JNK, p38, AKT and induce c-Src-dependent tyrosine phosphorylation of TRIP6. Through direct binding to TRAF6, TRIP6 antagonizes the recruitment of A20 and CYLD to TRAF6, thus sustaining the E3 ligase activity of TRAF6 upon LPA stimulation. This promotes the IKK-dependent phosphorylation and degradation of IκB, and allows TRIP6 to bind NF-κB p65. Once translocated to the nucleus, TRIP6 can further serve as a coactivator of NF-κB p65 and AP-1 to activate their target genes involved in apoptotic resistance, chronic inflammation, proliferation and invasion.