| pubmed-article:20614026 | rdf:type | pubmed:Citation | lld:pubmed |
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| pubmed-article:20614026 | lifeskim:mentions | umls-concept:C1179435 | lld:lifeskim |
| pubmed-article:20614026 | lifeskim:mentions | umls-concept:C0037083 | lld:lifeskim |
| pubmed-article:20614026 | lifeskim:mentions | umls-concept:C0079904 | lld:lifeskim |
| pubmed-article:20614026 | lifeskim:mentions | umls-concept:C1539081 | lld:lifeskim |
| pubmed-article:20614026 | lifeskim:mentions | umls-concept:C1710082 | lld:lifeskim |
| pubmed-article:20614026 | lifeskim:mentions | umls-concept:C0439855 | lld:lifeskim |
| pubmed-article:20614026 | lifeskim:mentions | umls-concept:C1705248 | lld:lifeskim |
| pubmed-article:20614026 | lifeskim:mentions | umls-concept:C1548799 | lld:lifeskim |
| pubmed-article:20614026 | lifeskim:mentions | umls-concept:C1524073 | lld:lifeskim |
| pubmed-article:20614026 | lifeskim:mentions | umls-concept:C0449432 | lld:lifeskim |
| pubmed-article:20614026 | lifeskim:mentions | umls-concept:C1998811 | lld:lifeskim |
| pubmed-article:20614026 | pubmed:issue | 6 | lld:pubmed |
| pubmed-article:20614026 | pubmed:dateCreated | 2010-7-8 | lld:pubmed |
| pubmed-article:20614026 | pubmed:abstractText | The tumor necrosis factor receptor (TNFR) superfamily mediates signals critical for regulation of the immune system. One family member, CD40, is important for the efficient activation of antibody-producing B cells and other antigen-presenting cells. The molecules and mechanisms that mediate CD40 signaling are only partially characterized. Proteins known to interact with the cytoplasmic domain of CD40 include members of the TNF receptor-associated factor (TRAF) family, which regulate signaling and serve as links to other signaling molecules. To identify additional proteins important for CD40 signaling, we used a combined stimulation/immunoprecipitation procedure to isolate CD40 signaling complexes from B cells and characterized the associated proteins by mass spectrometry. In addition to known CD40-interacting proteins, we detected SMAC/DIABLO, HTRA2/Omi, and HOIP/RNF31/PAUL/ZIBRA. We found that these previously unknown CD40-interacting partners were recruited in a TRAF2-dependent manner. HOIP is a ubiquitin ligase capable of mediating NF-kappaB activation through the ubiquitin-dependent activation of IKKgamma. We found that a mutant HOIP molecule engineered to lack ubiquitin ligase activity inhibited the CD40-mediated activation of NF-kappaB. Together, our results demonstrate a powerful approach for the identification of signaling molecules associated with cell surface receptors and indicate an important role for the ubiquitin ligase activity of HOIP in proximal CD40 signaling. | lld:pubmed |
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| pubmed-article:20614026 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:20614026 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:20614026 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:20614026 | pubmed:issn | 1932-6203 | lld:pubmed |
| pubmed-article:20614026 | pubmed:author | pubmed-author:RothmanPaul... | lld:pubmed |
| pubmed-article:20614026 | pubmed:author | pubmed-author:EipperBetty... | lld:pubmed |
| pubmed-article:20614026 | pubmed:author | pubmed-author:HostagerBruce... | lld:pubmed |
| pubmed-article:20614026 | pubmed:author | pubmed-author:WilkersonCurt... | lld:pubmed |
| pubmed-article:20614026 | pubmed:author | pubmed-author:FranconeVicto... | lld:pubmed |
| pubmed-article:20614026 | pubmed:author | pubmed-author:WhittenDougla... | lld:pubmed |
| pubmed-article:20614026 | pubmed:author | pubmed-author:ColganJohn... | lld:pubmed |
| pubmed-article:20614026 | pubmed:author | pubmed-author:FoxDaniel KDK | lld:pubmed |
| pubmed-article:20614026 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:20614026 | pubmed:volume | 5 | lld:pubmed |
| pubmed-article:20614026 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:20614026 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:20614026 | pubmed:pagination | e11380 | lld:pubmed |
| pubmed-article:20614026 | pubmed:dateRevised | 2011-9-26 | lld:pubmed |
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| pubmed-article:20614026 | pubmed:year | 2010 | lld:pubmed |
| pubmed-article:20614026 | pubmed:articleTitle | HOIL-1L interacting protein (HOIP) as an NF-kappaB regulating component of the CD40 signaling complex. | lld:pubmed |
| pubmed-article:20614026 | pubmed:affiliation | Department of Internal Medicine, University of Iowa, Iowa City, Iowa, United States of America. bruce-hostager@uiowa.edu | lld:pubmed |
| pubmed-article:20614026 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:20614026 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| pubmed-article:20614026 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
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