MersV1, Main, Exploration, bibRecord, 004061

The TNFR2-TRAF signaling complex contains two novel proteins related to baculoviral inhibitor of apoptosis proteins

Identifieur interne : 004061 ( Main/Exploration ); précédent : 004060; suivant : 004062

The TNFR2-TRAF signaling complex contains two novel proteins related to baculoviral inhibitor of apoptosis proteins

Auteurs : Mike Rothe [États-Unis] ; Ming-Gui Pan [États-Unis] ; William J. Henzel [États-Unis] ; T. Merrill Ayres [États-Unis] ; David V. Goeddel [États-Unis]

Source :

Cell [ 0092-8674 ] ; 1995.

RBID : ISTEX:EA5DDDFB1957ABF234D2BDA8D894BDDAEE97E52D

English descriptors

Teeft :
- Acid sequence, Aclap, Amino, Amino acid identity, Amino acid region, Amino acid sequencing, Amino acids, Apoptosis, Apoptosis protein, Autographa californica, Baculoviral inhibitor, Birnbaum, Cdna, Cdna clone, Cell death, Cell lysates, Cellular members, Cheng, Clem, Clone, Cold spring harbor laboratory press, Consensus sequence, Coprecipitation experiments, Cytoplasmic, Cytoplasmic domain, Cytoplasmic domains, Cytoplasmic proteins, Death domarn, Degenerate oligonucleotides, Degradation product, Direct association, Domain, Encoding, Epitope, Experimental procedures, Expression vector encoding, Expression vectors, Family members, Flag epitope, Functional analysis, Functional properties, Fusion protein, Fusion protein affinity column, Fusion proteins, Gal4, Gal4 activation, Gal4 dnabinding domain, Goeddel, Histidine residues, Human homolog, Human tissues, Iaps, Identical results, Immunoblot analysrs, Insect cells, Lysates, Lysis buffer, Mammalian cells, Mammalian members, Monoclonal, Monoclonal antibody, Murine, Mutant, Mutant protein, Mutant traf2 protein, Mutational analysis, Naip, Necrosis, Neuronal apoptosis, Northern blot analysis, Novel member, Novel proteins, Other members, Polyhedrosis virus, Protein, Protein bands, Protein sequencing, Receptor, Ring finger, Ring finger domain, Ring finger domains, Ring finger proteins, Rothe, Sequence analysis, Sequence motif, Signal transducers, Signal transduction, Silver staining, Tartaglia, Tnfr, Tnfr superfamily, Tnfr2, Tnfrbassociated protein, Traf, Traf domain, Traf2, Traf3, Trafl, Trafp, Trafs, Transfected, Tumor necrosis factor, Tumor necrosis factor receptor, Unpublished data, Yeast system.

Abstract

Abstract: 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 orginally 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.

Url:

https://api.istex.fr/ark:/67375/6H6-4R850QTC-G/fulltext.pdf

DOI: 10.1016/0092-8674(95)90149-3

Affiliations:

États-Unis

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Le document en format XML

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<term>Amino acid region</term>
<term>Amino acid sequencing</term>
<term>Amino acids</term>
<term>Apoptosis</term>
<term>Apoptosis protein</term>
<term>Autographa californica</term>
<term>Baculoviral inhibitor</term>
<term>Birnbaum</term>
<term>Cdna</term>
<term>Cdna clone</term>
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<term>Cell lysates</term>
<term>Cellular members</term>
<term>Cheng</term>
<term>Clem</term>
<term>Clone</term>
<term>Cold spring harbor laboratory press</term>
<term>Consensus sequence</term>
<term>Coprecipitation experiments</term>
<term>Cytoplasmic</term>
<term>Cytoplasmic domain</term>
<term>Cytoplasmic domains</term>
<term>Cytoplasmic proteins</term>
<term>Death domarn</term>
<term>Degenerate oligonucleotides</term>
<term>Degradation product</term>
<term>Direct association</term>
<term>Domain</term>
<term>Encoding</term>
<term>Epitope</term>
<term>Experimental procedures</term>
<term>Expression vector encoding</term>
<term>Expression vectors</term>
<term>Family members</term>
<term>Flag epitope</term>
<term>Functional analysis</term>
<term>Functional properties</term>
<term>Fusion protein</term>
<term>Fusion protein affinity column</term>
<term>Fusion proteins</term>
<term>Gal4</term>
<term>Gal4 activation</term>
<term>Gal4 dnabinding domain</term>
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<term>Human homolog</term>
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<term>Iaps</term>
<term>Identical results</term>
<term>Immunoblot analysrs</term>
<term>Insect cells</term>
<term>Lysates</term>
<term>Lysis buffer</term>
<term>Mammalian cells</term>
<term>Mammalian members</term>
<term>Monoclonal</term>
<term>Monoclonal antibody</term>
<term>Murine</term>
<term>Mutant</term>
<term>Mutant protein</term>
<term>Mutant traf2 protein</term>
<term>Mutational analysis</term>
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<term>Necrosis</term>
<term>Neuronal apoptosis</term>
<term>Northern blot analysis</term>
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<term>Protein bands</term>
<term>Protein sequencing</term>
<term>Receptor</term>
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<term>Ring finger domain</term>
<term>Ring finger domains</term>
<term>Ring finger proteins</term>
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<term>Sequence analysis</term>
<term>Sequence motif</term>
<term>Signal transducers</term>
<term>Signal transduction</term>
<term>Silver staining</term>
<term>Tartaglia</term>
<term>Tnfr</term>
<term>Tnfr superfamily</term>
<term>Tnfr2</term>
<term>Tnfrbassociated protein</term>
<term>Traf</term>
<term>Traf domain</term>
<term>Traf2</term>
<term>Traf3</term>
<term>Trafl</term>
<term>Trafp</term>
<term>Trafs</term>
<term>Transfected</term>
<term>Tumor necrosis factor</term>
<term>Tumor necrosis factor receptor</term>
<term>Unpublished data</term>
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<front><div type="abstract" xml:lang="en">Abstract: 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 orginally 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.</div>
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The TNFR2-TRAF signaling complex contains two novel proteins related to baculoviral inhibitor of apoptosis proteins

The TNFR2-TRAF signaling complex contains two novel proteins related to baculoviral inhibitor of apoptosis proteins

Source :

English descriptors

Abstract

Links toward previous steps (curation, corpus...)

Le document en format XML

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Pour mettre un lien sur cette page dans le réseau Wicri