| pmid | 11244088 | ||||||
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| title | The atypical protein kinase C-interacting protein p62 is a scaffold for NF-kappaB activation by nerve growth factor. | ||||||
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| journal | J Biol Chem | ||||||
| year | 2001 | ||||||
| full_text_available | false | ||||||
| doi | 10.1074/jbc.C000869200 |
The atypical protein kinase C-interacting protein p62 is a scaffold for NF-kappaB activation by nerve growth factor.
Authors: Wooten MW, Seibenhener ML, Mamidipudi V, Diaz-Meco MT, Barker PA, Moscat J Journal: J Biol Chem (2001) DOI: 10.1074/jbc.C000869200
- J Biol Chem. 2001 Mar 16;276(11):7709-12. doi: 10.1074/jbc.C000869200. Epub 2001 Jan 22.
The atypical protein kinase C-interacting protein p62 is a scaffold for NF-kappaB activation by nerve growth factor.
Wooten MW(1), Seibenhener ML, Mamidipudi V, Diaz-Meco MT, Barker PA, Moscat J.
Author information: (1)Department of Biological Sciences, Program in Cell and Molecular Biosciences, Auburn University, Auburn, Alabama 36849, USA. wootemw@auburn.edu
Nerve growth factor (NGF) binding to both p75 and TrkA neurotrophin receptors activates the transcription factor nuclear factor kappaB (NF-kappaB). 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-kappaB pathway, which mediates NGF survival and differentiation responses.
DOI: 10.1074/jbc.C000869200 PMID: 11244088 [Indexed for MEDLINE]