pubmed-article:10903733 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:10903733 | lifeskim:mentions | umls-concept:C0086282 | lld:lifeskim |
pubmed-article:10903733 | lifeskim:mentions | umls-concept:C1705455 | lld:lifeskim |
pubmed-article:10903733 | lifeskim:mentions | umls-concept:C0004561 | lld:lifeskim |
pubmed-article:10903733 | lifeskim:mentions | umls-concept:C1516349 | lld:lifeskim |
pubmed-article:10903733 | lifeskim:mentions | umls-concept:C0077503 | lld:lifeskim |
pubmed-article:10903733 | lifeskim:mentions | umls-concept:C0079904 | lld:lifeskim |
pubmed-article:10903733 | lifeskim:mentions | umls-concept:C0248813 | lld:lifeskim |
pubmed-article:10903733 | lifeskim:mentions | umls-concept:C0258441 | lld:lifeskim |
pubmed-article:10903733 | lifeskim:mentions | umls-concept:C0295022 | lld:lifeskim |
pubmed-article:10903733 | lifeskim:mentions | umls-concept:C1120843 | lld:lifeskim |
pubmed-article:10903733 | lifeskim:mentions | umls-concept:C0332281 | lld:lifeskim |
pubmed-article:10903733 | lifeskim:mentions | umls-concept:C1420888 | lld:lifeskim |
pubmed-article:10903733 | lifeskim:mentions | umls-concept:C1366777 | lld:lifeskim |
pubmed-article:10903733 | lifeskim:mentions | umls-concept:C1420809 | lld:lifeskim |
pubmed-article:10903733 | lifeskim:mentions | umls-concept:C1515877 | lld:lifeskim |
pubmed-article:10903733 | lifeskim:mentions | umls-concept:C1879547 | lld:lifeskim |
pubmed-article:10903733 | lifeskim:mentions | umls-concept:C1449799 | lld:lifeskim |
pubmed-article:10903733 | lifeskim:mentions | umls-concept:C0626649 | lld:lifeskim |
pubmed-article:10903733 | pubmed:issue | 3 | lld:pubmed |
pubmed-article:10903733 | pubmed:dateCreated | 2000-8-22 | lld:pubmed |
pubmed-article:10903733 | pubmed:abstractText | BCMA (B cell maturation) is a nonglycosylated integral membrane type I protein that is preferentially expressed in mature B lymphocytes. Previously, we reported in a human malignant myeloma cell line that BCMA is not primarily present on the cell surface but lies in a perinuclear structure that partially overlaps the Golgi apparatus. We now show that in transiently or stably transfected cells, BCMA is located on the cell surface, as well as in a perinulear Golgi-like structure. We also show that overexpression of BCMA in 293 cells activates NF-kappa B, Elk-1, the c-Jun N-terminal kinase, and the p38 mitogen-activated protein kinase. Coimmunoprecipitation experiments performed in transfected cells showed that BCMA associates with TNFR-associated factor (TRAF) 1, TRAF2, and TRAF3 adaptor proteins. Analysis of deletion mutants of the intracytoplasmic tail of BCMA showed that the 25-aa protein segment, from position 119 to 143, conserved between mouse and human BCMA, is essential for its association with the TRAFs and the activation of NF-kappa B, Elk-1, and c-Jun N-terminal kinase. BCMA belongs structurally to the TNFR family. Its unique TNFR motif corresponds to a variant motif present in the fourth repeat of the TNFRI molecule. This study confirms that BCMA is a functional member of the TNFR superfamily. Furthermore, as BCMA is lacking a "death domain" and its overexpression activates NF-kappa B and c-Jun N-terminal kinase, we can reasonably hypothesize that upon binding of its corresponding ligand BCMA transduces signals for cell survival and proliferation. | lld:pubmed |
pubmed-article:10903733 | pubmed:language | eng | lld:pubmed |
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pubmed-article:10903733 | pubmed:citationSubset | AIM | lld:pubmed |
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pubmed-article:10903733 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:10903733 | pubmed:month | Aug | lld:pubmed |
pubmed-article:10903733 | pubmed:issn | 0022-1767 | lld:pubmed |
pubmed-article:10903733 | pubmed:author | pubmed-author:RousselJJ | lld:pubmed |
pubmed-article:10903733 | pubmed:author | pubmed-author:RogierEE | lld:pubmed |
pubmed-article:10903733 | pubmed:author | pubmed-author:InoueJJ | lld:pubmed |
pubmed-article:10903733 | pubmed:author | pubmed-author:TsapisAA | lld:pubmed |
pubmed-article:10903733 | pubmed:author | pubmed-author:BourgeadeM... | lld:pubmed |
pubmed-article:10903733 | pubmed:author | pubmed-author:DevergneOO | lld:pubmed |
pubmed-article:10903733 | pubmed:author | pubmed-author:HatzoglouAA | lld:pubmed |
pubmed-article:10903733 | pubmed:author | pubmed-author:MadryCC | lld:pubmed |
pubmed-article:10903733 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:10903733 | pubmed:day | 1 | lld:pubmed |
pubmed-article:10903733 | pubmed:volume | 165 | lld:pubmed |
pubmed-article:10903733 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:10903733 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:10903733 | pubmed:pagination | 1322-30 | lld:pubmed |
pubmed-article:10903733 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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pubmed-article:10903733 | pubmed:year | 2000 | lld:pubmed |
pubmed-article:10903733 | pubmed:articleTitle | TNF receptor family member BCMA (B cell maturation) associates with TNF receptor-associated factor (TRAF) 1, TRAF2, and TRAF3 and activates NF-kappa B, elk-1, c-Jun N-terminal kinase, and p38 mitogen-activated protein kinase. | lld:pubmed |
pubmed-article:10903733 | pubmed:affiliation | Laboratory of Experimental Endocrinology, Faculty of Medicine, University of Crete, Heraklion, Greece. | lld:pubmed |
pubmed-article:10903733 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:10903733 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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