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rdf:type |
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lifeskim:mentions |
umls-concept:C0033684,
umls-concept:C0037083,
umls-concept:C0079005,
umls-concept:C0205314,
umls-concept:C0439849,
umls-concept:C0439855,
umls-concept:C0445223,
umls-concept:C0679622,
umls-concept:C0893445,
umls-concept:C1549781,
umls-concept:C1552599,
umls-concept:C1704787,
umls-concept:C1710082
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pubmed:issue |
7
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pubmed:dateCreated |
1996-2-21
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pubmed:databankReference |
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pubmed:abstractText |
The 75 kDa tumor necrosis factor receptor (TNFR2) transduces extracellular signals via receptor-associated cytoplasmic proteins. Two of these signal transducers, TRAF1 and TRAF2, were isolated and characterized previously. We report here the biochemical purification and subsequent molecular cloning of two novel TNFR2-associated proteins, designated c-IAP1 and c-IAP2, that are closely related mammalian members of the inhibitor of apoptosis protein (IAP) family originally identified in baculoviruses. The viral and cellular IAPs contain N-terminal baculovirus IAP repeat (BIR) motifs and a C-terminal RING finger. The c-IAPs do not directly contact TNFR2, but rather associate with TRAF1 and TRAF2 through their N-terminal BIR motif-comprising domain. The recruitment of c-IAP1 or c-IAP2 to the TNFR2 signaling complex requires a TRAF2-TRAF1 heterocomplex.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Cell Cycle Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Inhibitor of Apoptosis Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Tumor Necrosis Factor,
http://linkedlifedata.com/resource/pubmed/chemical/TNF Receptor-Associated Factor 1,
http://linkedlifedata.com/resource/pubmed/chemical/TNF Receptor-Associated Factor 2,
http://linkedlifedata.com/resource/pubmed/chemical/Viral Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/inhibitor of apoptosis...
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0092-8674
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
29
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pubmed:volume |
83
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1243-52
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pubmed:dateRevised |
2005-11-17
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pubmed:meshHeading |
pubmed-meshheading:8548810-Animals,
pubmed-meshheading:8548810-Apoptosis,
pubmed-meshheading:8548810-Cell Cycle Proteins,
pubmed-meshheading:8548810-Cell Line,
pubmed-meshheading:8548810-Cloning, Molecular,
pubmed-meshheading:8548810-Humans,
pubmed-meshheading:8548810-Inhibitor of Apoptosis Proteins,
pubmed-meshheading:8548810-Kidney,
pubmed-meshheading:8548810-Mice,
pubmed-meshheading:8548810-Molecular Sequence Data,
pubmed-meshheading:8548810-Molecular Weight,
pubmed-meshheading:8548810-Proteins,
pubmed-meshheading:8548810-RNA, Messenger,
pubmed-meshheading:8548810-Receptors, Tumor Necrosis Factor,
pubmed-meshheading:8548810-Sequence Homology, Amino Acid,
pubmed-meshheading:8548810-Signal Transduction,
pubmed-meshheading:8548810-T-Lymphocytes, Cytotoxic,
pubmed-meshheading:8548810-TNF Receptor-Associated Factor 1,
pubmed-meshheading:8548810-TNF Receptor-Associated Factor 2,
pubmed-meshheading:8548810-Viral Proteins
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pubmed:year |
1995
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pubmed:articleTitle |
The TNFR2-TRAF signaling complex contains two novel proteins related to baculoviral inhibitor of apoptosis proteins.
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pubmed:affiliation |
Department of Molecular Biology Tularik, Incorporated, South San Francisco, California 94080, USA.
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pubmed:publicationType |
Journal Article
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