pubmed-article:11244088 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:11244088 | lifeskim:mentions | umls-concept:C0027754 | lld:lifeskim |
pubmed-article:11244088 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
pubmed-article:11244088 | lifeskim:mentions | umls-concept:C0027752 | lld:lifeskim |
pubmed-article:11244088 | lifeskim:mentions | umls-concept:C0033640 | lld:lifeskim |
pubmed-article:11244088 | lifeskim:mentions | umls-concept:C0205182 | lld:lifeskim |
pubmed-article:11244088 | lifeskim:mentions | umls-concept:C1420393 | lld:lifeskim |
pubmed-article:11244088 | lifeskim:mentions | umls-concept:C1523116 | lld:lifeskim |
pubmed-article:11244088 | pubmed:issue | 11 | lld:pubmed |
pubmed-article:11244088 | pubmed:dateCreated | 2001-5-25 | lld:pubmed |
pubmed-article:11244088 | pubmed:abstractText | 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. | lld:pubmed |
pubmed-article:11244088 | pubmed:language | eng | lld:pubmed |
pubmed-article:11244088 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11244088 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:11244088 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11244088 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:11244088 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11244088 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11244088 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:11244088 | pubmed:month | Mar | lld:pubmed |
pubmed-article:11244088 | pubmed:issn | 0021-9258 | lld:pubmed |
pubmed-article:11244088 | pubmed:author | pubmed-author:BarkerP APA | lld:pubmed |
pubmed-article:11244088 | pubmed:author | pubmed-author:MoscatJJ | lld:pubmed |
pubmed-article:11244088 | pubmed:author | pubmed-author:Diaz-MecoM... | lld:pubmed |
pubmed-article:11244088 | pubmed:author | pubmed-author:WootenM WMW | lld:pubmed |
pubmed-article:11244088 | pubmed:author | pubmed-author:SeibenhenerM... | lld:pubmed |
pubmed-article:11244088 | pubmed:author | pubmed-author:MamidipudiVV | lld:pubmed |
pubmed-article:11244088 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:11244088 | pubmed:day | 16 | lld:pubmed |
pubmed-article:11244088 | pubmed:volume | 276 | lld:pubmed |
pubmed-article:11244088 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:11244088 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:11244088 | pubmed:pagination | 7709-12 | lld:pubmed |
pubmed-article:11244088 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
pubmed-article:11244088 | pubmed:meshHeading | pubmed-meshheading:11244088... | lld:pubmed |
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pubmed-article:11244088 | pubmed:meshHeading | pubmed-meshheading:11244088... | lld:pubmed |
pubmed-article:11244088 | pubmed:meshHeading | pubmed-meshheading:11244088... | lld:pubmed |
pubmed-article:11244088 | pubmed:year | 2001 | lld:pubmed |
pubmed-article:11244088 | pubmed:articleTitle | The atypical protein kinase C-interacting protein p62 is a scaffold for NF-kappaB activation by nerve growth factor. | lld:pubmed |
pubmed-article:11244088 | pubmed:affiliation | Department of Biological Sciences, Program in Cell and Molecular Biosciences, Auburn University, Auburn, Alabama 36849, USA. wootemw@auburn.edu | lld:pubmed |
pubmed-article:11244088 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:11244088 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
pubmed-article:11244088 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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