Source:http://linkedlifedata.com/resource/pubmed/id/11395500
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
34
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pubmed:dateCreated |
2001-8-20
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pubmed:abstractText |
Homophilic interactions of death effector domains (DEDs) are crucial for the signaling pathways of death receptor-mediated apoptosis. The machinery that regulates proper oligomerization and autoactivation of procaspase-8 and/or procaspase-10 during T lymphocyte activation determines whether the cells will undergo caspase-mediated apoptosis or proliferation. We screened a yeast two-hybrid library by using the DEDs contained in the prodomains of procaspase-8 and procaspase-10 and isolated a DED-associated factor (DEDAF) that interacts with several DED-containing proteins but does not itself contain a DED. DEDAF is highly conserved between human and mouse (98% amino acid identity) and is homologous to a nuclear regulatory protein YAF-2. DEDAF is expressed at the highest levels in lymphoid tissues and placenta. DEDAF interacts with FADD, procaspase-8, and procaspase-10 in the cytosol as well as with the DED-containing DNA-binding protein (DEDD) in the nucleus. At the cell membrane, DEDAF augmented the formation of CD95-FADD-caspase-8 complexes and enhanced death receptor- as well as DED-mediated apoptosis. In the nucleus, DEDAF caused the DEDD protein to relocalize from subnuclear structures to a diffuse distribution in the nucleoplasm. Our data therefore suggest that DEDAF may be involved in the regulation of both cytoplasmic and nuclear events of apoptosis.
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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/CASP10 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Caspase 10,
http://linkedlifedata.com/resource/pubmed/chemical/Caspases,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Complementary,
http://linkedlifedata.com/resource/pubmed/chemical/Intracellular Signaling Peptides...
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
24
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pubmed:volume |
276
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
31945-52
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:11395500-Amino Acid Sequence,
pubmed-meshheading:11395500-Apoptosis,
pubmed-meshheading:11395500-Carrier Proteins,
pubmed-meshheading:11395500-Caspase 10,
pubmed-meshheading:11395500-Caspases,
pubmed-meshheading:11395500-Cell Line,
pubmed-meshheading:11395500-Cell Nucleus,
pubmed-meshheading:11395500-Cloning, Molecular,
pubmed-meshheading:11395500-Cytoplasm,
pubmed-meshheading:11395500-DNA, Complementary,
pubmed-meshheading:11395500-Humans,
pubmed-meshheading:11395500-Intracellular Signaling Peptides and Proteins,
pubmed-meshheading:11395500-Molecular Sequence Data,
pubmed-meshheading:11395500-Protein Binding,
pubmed-meshheading:11395500-Sequence Homology, Amino Acid
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pubmed:year |
2001
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pubmed:articleTitle |
The death effector domain-associated factor plays distinct regulatory roles in the nucleus and cytoplasm.
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pubmed:affiliation |
Laboratory of Immunology, NIAID, National Institutes of Health, Bethesda, Maryland 20892, USA.
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pubmed:publicationType |
Journal Article
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