| pubmed-article:15357952 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:15357952 | lifeskim:mentions | umls-concept:C0011065 | lld:lifeskim |
| pubmed-article:15357952 | lifeskim:mentions | umls-concept:C0812246 | lld:lifeskim |
| pubmed-article:15357952 | lifeskim:mentions | umls-concept:C1622418 | lld:lifeskim |
| pubmed-article:15357952 | lifeskim:mentions | umls-concept:C0077503 | lld:lifeskim |
| pubmed-article:15357952 | lifeskim:mentions | umls-concept:C0034850 | lld:lifeskim |
| pubmed-article:15357952 | lifeskim:mentions | umls-concept:C0037083 | lld:lifeskim |
| pubmed-article:15357952 | lifeskim:mentions | umls-concept:C1456820 | lld:lifeskim |
| pubmed-article:15357952 | lifeskim:mentions | umls-concept:C1710082 | lld:lifeskim |
| pubmed-article:15357952 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:15357952 | pubmed:dateCreated | 2004-9-10 | lld:pubmed |
| pubmed-article:15357952 | pubmed:abstractText | The molecular regulation of the recruitment of initial signaling complexes at the TNF-R1 is poorly defined. We demonstrate here that within minutes internalized TNF-R1 (TNF receptosomes) recruits TRADD, FADD, and caspase-8 to establish the "death-inducing signaling complex" (DISC). In addition, we identified the TNF-R1 internalization domain (TRID) required for receptor endocytosis and provide evidence that TNF-R1 internalization, DISC formation, and apoptosis are inseparable events. Analyzing cell lines expressing an internalization-deficient receptor (TNF-R1 DeltaTRID) revealed that recruitment of RIP-1 and TRAF-2 to TNF-R1 occurred at the level of the plasma membrane. In contrast, aggregation of TRADD, FADD, and caspase-8 to establish the TNF-R1-associated DISC is critically dependent on receptor endocytosis. Furthermore, fusion of TNF receptosomes with trans-Golgi vesicles results in activation of acid sphingomyelinase and cathepsin D. Thus, TNF receptosomes establish the different TNF signaling pathways by compartmentalization of plasma membrane-derived endocytic vesicles harboring the TNF-R1-associated DISC. | lld:pubmed |
| pubmed-article:15357952 | pubmed:language | eng | lld:pubmed |
| pubmed-article:15357952 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15357952 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:15357952 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15357952 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15357952 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15357952 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15357952 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15357952 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15357952 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15357952 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15357952 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15357952 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15357952 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15357952 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15357952 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15357952 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15357952 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15357952 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15357952 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15357952 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15357952 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15357952 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15357952 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15357952 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:15357952 | pubmed:month | Sep | lld:pubmed |
| pubmed-article:15357952 | pubmed:issn | 1074-7613 | lld:pubmed |
| pubmed-article:15357952 | pubmed:author | pubmed-author:HeinrichMicha... | lld:pubmed |
| pubmed-article:15357952 | pubmed:author | pubmed-author:AdamDieterD | lld:pubmed |
| pubmed-article:15357952 | pubmed:author | pubmed-author:KabelitzDiete... | lld:pubmed |
| pubmed-article:15357952 | pubmed:author | pubmed-author:SchützeStefan... | lld:pubmed |
| pubmed-article:15357952 | pubmed:author | pubmed-author:Held-FeindtJa... | lld:pubmed |
| pubmed-article:15357952 | pubmed:author | pubmed-author:MentleinRolfR | lld:pubmed |
| pubmed-article:15357952 | pubmed:author | pubmed-author:Schneider-Bra... | lld:pubmed |
| pubmed-article:15357952 | pubmed:author | pubmed-author:Winoto-Morbac... | lld:pubmed |
| pubmed-article:15357952 | pubmed:author | pubmed-author:TchikovVladim... | lld:pubmed |
| pubmed-article:15357952 | pubmed:author | pubmed-author:NeumeyerJensJ | lld:pubmed |
| pubmed-article:15357952 | pubmed:author | pubmed-author:JakobMartenM | lld:pubmed |
| pubmed-article:15357952 | pubmed:author | pubmed-author:MerkelOliverO | lld:pubmed |
| pubmed-article:15357952 | pubmed:author | pubmed-author:Ehrenschwende... | lld:pubmed |
| pubmed-article:15357952 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:15357952 | pubmed:volume | 21 | lld:pubmed |
| pubmed-article:15357952 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:15357952 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:15357952 | pubmed:pagination | 415-28 | lld:pubmed |
| pubmed-article:15357952 | pubmed:dateRevised | 2010-11-18 | lld:pubmed |
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| pubmed-article:15357952 | pubmed:meshHeading | pubmed-meshheading:15357952... | lld:pubmed |
| pubmed-article:15357952 | pubmed:year | 2004 | lld:pubmed |
| pubmed-article:15357952 | pubmed:articleTitle | Compartmentalization of TNF receptor 1 signaling: internalized TNF receptosomes as death signaling vesicles. | lld:pubmed |
| pubmed-article:15357952 | pubmed:affiliation | Institute of Medical Microbiology and Hygiene, University of Regensburg, D-93053, Germany. | lld:pubmed |
| pubmed-article:15357952 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:15357952 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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