Phospho-SXXE/D motif mediated TNF receptor 1-TRADD death domain complex formation for T cell activation and migration.
Phospho-SXXE/D motif mediated TNF receptor 1-TRADD death domain complex formation for T cell activation and migration.
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DOI：
10.4049/jimmunol.1003399
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发表时间：
2011-08-01
期刊：
影响因子：
--
通讯作者：
Chin YE
中科院分区：
文献类型：
--
作者：
Guan YJ;Zhang Z;Yu C;Ma L;Hu W;Xu L;Gao JS;Chung CS;Wang L;Yang ZF;Fast LD;Chung AS;Kim M;Ayala A;Zhuang S;Zheng S;Chin YE
In TNF treated cells, TNFR1, TRADD, FADD, and RIP proteins form the signaling complex via modular interaction within their C-terminal death domains. Here we report that the death domain SXXE/D motifs, i.e., S381DHE motif of TNFR1-death domain, S215LKD and S296LAE motifs of TRADD-death domain are phosphorylated and this is required for stable TNFR1-TRADD complex formation and subsequent activation of NF-κB. Phospho-S215LKD and phospho-S296LAE motifs are also critical to TRADD for recruiting FADD and RIP. IKKβ plays a critical role in TNFR1 phosphorylation of S381, which leads to subsequent T cell migration and accumulation. Consistently, we observed in IBD specimens that TNFR1 was constitutively phosphorylated on S381 in those inflammatory T cells, which had accumulated in high numbers in the inflamed mucosa. Therefore, SXXE/D motifs found in the cytoplasmic domains of many TNFR family members and their adaptor proteins may serve to function as a specific interaction module for the α-helical death domain signal transduction.
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