Source:http://linkedlifedata.com/resource/pubmed/id/15214041
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
7
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pubmed:dateCreated |
2004-6-23
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pubmed:abstractText |
We investigated the membrane localization of CD95 in type I and type II cells, which differ in their ability to recruit and activate caspase-8. We found that CD95 was preferentially located in lipid rafts of type I cells, while it was present both in raft and non-raft plasma membrane sub-domains of type II cells. After stimulation, CD95 located in phospholipid-rich plasma membrane was recruited to lipid rafts in both types of cells. Similarly, CD95 cross-linking resulted in caspase-independent translocation of FADD/MORT1 and caspase-8 to the lipid rafts, which was prevented by a death domain-defective receptor. CD95 internalization was then rapid in type I and delayed in type II cells and showed a substantial correlation with the kinetics of Fas-associated death domain (FADD)and caspase-8 recruitment to lipid rafts. Finally, electron microscopy analysis showed that after CD95 stimulation lipid rafts aggregated in large clusters that were internalized in endosomal vesicles, where caspase-8 underwent massive processing. Taken together, our data demonstrate that CD95 death-inducing signaling complex formation and internalization in type I and type II cells occur in lipid rafts, which are a major site of caspase-8 activation.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD95,
http://linkedlifedata.com/resource/pubmed/chemical/Caspases,
http://linkedlifedata.com/resource/pubmed/chemical/Cholesterol,
http://linkedlifedata.com/resource/pubmed/chemical/Death Domain Receptor Signaling...,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Tumor Necrosis Factor
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
0014-2980
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pubmed:author |
pubmed-author:De MariaRuggeroR,
pubmed-author:EramoAdrianaA,
pubmed-author:LottiFiorenzaF,
pubmed-author:MessinaCarlo G MCG,
pubmed-author:ParoliniIsabellaI,
pubmed-author:PeschleCesareC,
pubmed-author:Ricci-VitianiLuciaL,
pubmed-author:SargiacomoMassimoM,
pubmed-author:SetteGiovanniG,
pubmed-author:StassiGiorgioG,
pubmed-author:TodaroMatildeM
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pubmed:issnType |
Print
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pubmed:volume |
34
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1930-40
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:15214041-Antigens, CD95,
pubmed-meshheading:15214041-Apoptosis,
pubmed-meshheading:15214041-Caspases,
pubmed-meshheading:15214041-Cell Line, Tumor,
pubmed-meshheading:15214041-Cholesterol,
pubmed-meshheading:15214041-Death Domain Receptor Signaling Adaptor Proteins,
pubmed-meshheading:15214041-Endocytosis,
pubmed-meshheading:15214041-Humans,
pubmed-meshheading:15214041-Membrane Microdomains,
pubmed-meshheading:15214041-Protein Binding,
pubmed-meshheading:15214041-Protein Transport,
pubmed-meshheading:15214041-Receptors, Tumor Necrosis Factor,
pubmed-meshheading:15214041-Signal Transduction,
pubmed-meshheading:15214041-T-Lymphocytes
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pubmed:year |
2004
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pubmed:articleTitle |
CD95 death-inducing signaling complex formation and internalization occur in lipid rafts of type I and type II cells.
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pubmed:affiliation |
Department of Hematology, Oncology and Molecular Medicine, Istituto Superiore di Sanità, Rome, Italy.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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