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1 Department of Molecular Biology, Graduate School of Science, Nagoya University, Nagoya, 464-8602 Japan
2 Department of Environmental and Molecular Toxicology, North Carolina State University, Raleigh, NC 27695-7633, USA
3 RIKEN Research Center for Allergy and Immunology, Yokohama, Japan
4 Department of Host Defense, Research Institute for Microbial Diseases, Osaka University, Osaka, Japan
5 CREST, Japan Science and Technology Corporation, Japan
TAK1 mitogen-activated protein kinase kinase kinase participates in the Interleukin-1 (IL-1) signaling pathway by mediating activation of JNK, p38, and NF-
B. TAK1-binding protein 2 (TAB2) was previously identified as an adaptor that links TAK1 to an upstream signaling intermediate, tumor necrosis factor receptor-associated factor 6 (TRAF6). Recently, ubiquitination of TRAF6 was shown to play an essential role in the activation of TAK1. However, the mechanism by which IL-1 induces TRAF6 ubiquitination remains to be elucidated. Here we report that TAB2 functions to facilitate TRAF6 ubiquitination and thereby mediates IL-1-induced cellular events. A conserved ubiquitin binding domain in TAB2, the CUE domain, is important for this function. We also found that TAB2 promotes the assembly of TRAF6 with a downstream kinase, IB kinase (IKK). These results show that TAB2 acts as a multifunctional signaling molecule, facilitating both IL-1-dependent TRAF6 ubiquitination and assembly of the IL-1 signaling complex.
* Correspondence: E-mail: Jun_Tsuji{at}ncsu.edu
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