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Originally published In Press as doi:10.1074/jbc.C000869200 on January 22, 2001

J. Biol. Chem., Vol. 276, Issue 11, 7709-7712, March 16, 2001
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ACCELERATED PUBLICATION
The Atypical Protein Kinase C-interacting Protein p62 Is a Scaffold for NF-kappa B Activation by Nerve Growth Factor*

Marie W. WootenDagger §, M. Lamar SeibenhenerDagger , Vidya MamidipudiDagger , Maria T. Diaz-Meco, Philip A. Barker||, and Jorge Moscat

From the Dagger  Department of Biological Sciences, Program in Cell and Molecular Biosciences, Auburn University, Auburn, Alabama 36849,  Centro Biologia Molecular "Severo Ochoa" (CSIC), Universidad Autonoma, Canto Blanco, 28049 Madrid, Spain, and the || Centre for Neuronal Survival, Montreal Neurological Institute, McGill University, Montreal H3A 2B4, Canada

Nerve growth factor (NGF) binding to both p75 and TrkA neurotrophin receptors activates the transcription factor nuclear factor kappa B (NF-kappa B). Here we show that the atypical protein kinase C-interacting protein, p62, which binds TRAF6, selectively interacts with TrkA but not p75. In contrast, TRAF6 interacts with p75 but not TrkA. We demonstrate the formation of a TRAF6-p62 complex that serves as a bridge linking both p75 and TrkA signaling. Of functional relevance, transfection of antisense p62-enhanced p75-mediated cell death and diminished NGF-induced differentiation occur through a mechanism involving inhibition of IKK activity. These findings reveal a new function for p62 as a common platform for communication of both p75-TRAF6 and TrkA signals. Moreover, we demonstrated that p62 serves as a scaffold for activation of the NF-kappa B pathway, which mediates NGF survival and differentiation responses.

* This study was funded by grants from the National Institutes of Health (to M. W. W.), the Ministry of Science and Education Spain (to M. W. W. and J. M.), and the European Union and Glaxo Wellcome Spain (to J. M.).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 © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.


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