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Originally published In Press as doi:10.1074/jbc.M109730200 on May 28, 2002

J. Biol. Chem., Vol. 277, Issue 31, 28010-28018, August 2, 2002
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Identification of Interleukin 1 Receptor-associated Kinase as a Conserved Component in the p75-Neurotrophin Receptor Activation of Nuclear Factor-kappa B*

Vidya MamidipudiDagger , Xiaoxia Li§, and Marie W. WootenDagger

From the Dagger  Department of Biological Sciences, Program in Cell and Molecular Biosciences, Auburn University, Auburn, Alabama 36849 and the § Department of Molecular Biology, Lerner Research Institute, Cleveland Clinic Foundation, Cleveland, Ohio 44195

The neurotrophin nerve growth factor (NGF) supports neuronal survival by activating the transcription factor nuclear factor-kappa B (NF-kappa B). We report here, for the first time, the identification of p75-associated kinase that mediates NGF-driven NF-kappa B activation. Using co-immunoprecipitation, we demonstrate an NGF-dependent association of interleukin 1 receptor-associated kinase (IRAK) with the p75 neurotrophin receptor in PC12 cells. Our results reveal that IRAK is recruited to the p75-NGF receptor leading to formation of a complex between IRAK, atypical protein kinase C interacting protein, p62, and TRAF6. Activation of NF-kappa B occurs predominantly through the p75 receptor, and TrkA activity suppresses NF-kappa B activation and retards Ikappa Bbeta degradation. In addition, we observe a requirement for the kinase activity of IRAK in mediating NGF-induced NF-kappa B activation, recruitment of the adapter protein p62 to the p75 receptor, and cell survival. Moreover, p75-IRAK-mediated kappa B activation and the recruitment of IKKbeta , but not IKKalpha , to the receptor require p62. Altogether, our data provide novel information regarding the proximal components involved in p75 receptor signaling and underscore the importance of the atypical PKC interacting protein p62 in this process.

* This work was supported by NINDS, National Institutes of Health Grant 33661 (to M. W. W.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

To whom correspondence should be addressed: Dept. of Biological Sciences, 331 Funchess Hall, Auburn University, AL 36849. Tel.: 334-844-9226; Fax: 334-844-9234; E-mail: Wootemw@auburn.edu.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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