The TNFR2-TRAF signaling complex contains two novel proteins related to baculoviral inhibitor of apoptosis proteins
Identifieur interne : 001F83 ( Istex/Corpus ); précédent : 001F82; suivant : 001F84The TNFR2-TRAF signaling complex contains two novel proteins related to baculoviral inhibitor of apoptosis proteins
Auteurs : Mike Rothe ; Ming-Gui Pan ; William J. Henzel ; T. Merrill Ayres ; David V. GoeddelSource :
- Cell [ 0092-8674 ] ; 1995.
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Traf domain, Traf2, Traf3, Trafl, Trafp, Trafs, Transfected, Tumor necrosis factor, Tumor necrosis factor receptor, Unpublished data, Yeast system.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:
DOI: 10.1016/0092-8674(95)90149-3
Links to Exploration step
ISTEX:EA5DDDFB1957ABF234D2BDA8D894BDDAEE97E52DLe document en format XML
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Goeddel</name><affiliation><mods:affiliation>Department of Molecular Biology Tularik, Incorporated 270 East Grand Avenue South San Francisco, California 94080, USA</mods:affiliation></affiliation></author></analytic><monogr></monogr><series><title level="j">Cell</title><title level="j" type="abbrev">CELL</title><idno type="ISSN">0092-8674</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1995">1995</date><biblScope unit="volume">83</biblScope><biblScope unit="issue">7</biblScope><biblScope unit="page" from="1243">1243</biblScope><biblScope unit="page" to="1252">1252</biblScope></imprint><idno type="ISSN">0092-8674</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0092-8674</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="Teeft" xml:lang="en"><term>Acid sequence</term><term>Aclap</term><term>Amino</term><term>Amino acid identity</term><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><term>Cell death</term><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><term>Goeddel</term><term>Histidine residues</term><term>Human homolog</term><term>Human tissues</term><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><term>Naip</term><term>Necrosis</term><term>Neuronal apoptosis</term><term>Northern blot analysis</term><term>Novel member</term><term>Novel proteins</term><term>Other members</term><term>Polyhedrosis virus</term><term>Protein</term><term>Protein bands</term><term>Protein sequencing</term><term>Receptor</term><term>Ring finger</term><term>Ring finger domain</term><term>Ring finger domains</term><term>Ring finger proteins</term><term>Rothe</term><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><term>Yeast system</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><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></front></TEI><istex><corpusName>elsevier</corpusName><keywords><teeft><json:string>tnfr2</json:string><json:string>traf2</json:string><json:string>rothe</json:string><json:string>trafl</json:string><json:string>receptor</json:string><json:string>murine</json:string><json:string>apoptosis</json:string><json:string>cytoplasmic</json:string><json:string>cdna</json:string><json:string>trafs</json:string><json:string>traf</json:string><json:string>amino acids</json:string><json:string>goeddel</json:string><json:string>amino</json:string><json:string>tartaglia</json:string><json:string>mutant</json:string><json:string>iaps</json:string><json:string>lysates</json:string><json:string>fusion proteins</json:string><json:string>cytoplasmic domain</json:string><json:string>epitope</json:string><json:string>encoding</json:string><json:string>gal4</json:string><json:string>monoclonal</json:string><json:string>clem</json:string><json:string>clone</json:string><json:string>ring finger domains</json:string><json:string>cell death</json:string><json:string>cell lysates</json:string><json:string>transfected</json:string><json:string>traf3</json:string><json:string>aclap</json:string><json:string>naip</json:string><json:string>tnfr</json:string><json:string>trafp</json:string><json:string>mammalian cells</json:string><json:string>ring finger domain</json:string><json:string>yeast system</json:string><json:string>tumor necrosis factor receptor</json:string><json:string>monoclonal antibody</json:string><json:string>cheng</json:string><json:string>cytoplasmic domains</json:string><json:string>family members</json:string><json:string>cdna clone</json:string><json:string>domain</json:string><json:string>birnbaum</json:string><json:string>tnfr superfamily</json:string><json:string>amino acid identity</json:string><json:string>death domarn</json:string><json:string>traf domain</json:string><json:string>cytoplasmic proteins</json:string><json:string>coprecipitation experiments</json:string><json:string>polyhedrosis virus</json:string><json:string>insect cells</json:string><json:string>unpublished data</json:string><json:string>consensus sequence</json:string><json:string>mammalian members</json:string><json:string>mutant protein</json:string><json:string>protein</json:string><json:string>necrosis</json:string><json:string>mutant traf2 protein</json:string><json:string>ring finger proteins</json:string><json:string>protein sequencing</json:string><json:string>degenerate oligonucleotides</json:string><json:string>degradation product</json:string><json:string>autographa californica</json:string><json:string>novel proteins</json:string><json:string>fusion protein</json:string><json:string>neuronal apoptosis</json:string><json:string>histidine residues</json:string><json:string>human homolog</json:string><json:string>human tissues</json:string><json:string>identical results</json:string><json:string>functional properties</json:string><json:string>acid sequence</json:string><json:string>amino acid region</json:string><json:string>fusion protein affinity column</json:string><json:string>protein bands</json:string><json:string>silver staining</json:string><json:string>experimental procedures</json:string><json:string>direct association</json:string><json:string>northern blot analysis</json:string><json:string>novel member</json:string><json:string>cellular members</json:string><json:string>expression vector encoding</json:string><json:string>immunoblot analysrs</json:string><json:string>sequence analysis</json:string><json:string>signal transduction</json:string><json:string>functional analysis</json:string><json:string>gal4 dnabinding domain</json:string><json:string>gal4 activation</json:string><json:string>mutational analysis</json:string><json:string>other members</json:string><json:string>flag epitope</json:string><json:string>ring finger</json:string><json:string>apoptosis protein</json:string><json:string>sequence motif</json:string><json:string>signal transducers</json:string><json:string>tnfrbassociated protein</json:string><json:string>amino acid sequencing</json:string><json:string>expression vectors</json:string><json:string>lysis buffer</json:string><json:string>baculoviral inhibitor</json:string><json:string>cold spring harbor laboratory press</json:string><json:string>tumor necrosis factor</json:string></teeft></keywords><author><json:item><name>Mike Rothe</name><affiliations><json:string>Department of Molecular Biology Tularik, Incorporated 270 East Grand Avenue South San Francisco, California 94080, USA</json:string></affiliations></json:item><json:item><name>Ming-Gui Pan</name><affiliations><json:string>Department of Molecular Biology Tularik, Incorporated 270 East Grand Avenue South San Francisco, California 94080, USA</json:string></affiliations></json:item><json:item><name>William J. Henzel</name><affiliations><json:string>Department of Protein Chemistry Genentech, Incorporated 460 Point San Bruno Boulevard South San Francisco, California 94080, USA</json:string></affiliations></json:item><json:item><name>T.Merrill Ayres</name><affiliations><json:string>Department of Molecular Biology Tularik, Incorporated 270 East Grand Avenue South San Francisco, California 94080, USA</json:string></affiliations></json:item><json:item><name>David V. Goeddel</name><affiliations><json:string>Department of Molecular Biology Tularik, Incorporated 270 East Grand Avenue South San Francisco, California 94080, USA</json:string></affiliations></json:item></author><arkIstex>ark:/67375/6H6-4R850QTC-G</arkIstex><language><json:string>eng</json:string></language><originalGenre><json:string>Full-length article</json:string></originalGenre><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.</abstract><qualityIndicators><score>8.416</score><pdfWordCount>6012</pdfWordCount><pdfCharCount>41997</pdfCharCount><pdfVersion>1.3</pdfVersion><pdfPageCount>10</pdfPageCount><pdfPageSize>612 x 792 pts (letter)</pdfPageSize><refBibsNative>true</refBibsNative><abstractWordCount>118</abstractWordCount><abstractCharCount>868</abstractCharCount><keywordCount>0</keywordCount></qualityIndicators><title>The TNFR2-TRAF signaling complex contains two novel proteins related to baculoviral inhibitor of apoptosis proteins</title><pmid><json:string>8548810</json:string></pmid><pii><json:string>0092-8674(95)90149-3</json:string></pii><genre><json:string>research-article</json:string></genre><serie><title>Proc. Natl. Acad. Sci. USA</title><language><json:string>unknown</json:string></language><volume>89</volume><pages><first>5789</first><last>5793</last></pages></serie><host><title>Cell</title><language><json:string>unknown</json:string></language><publicationDate>1995</publicationDate><issn><json:string>0092-8674</json:string></issn><pii><json:string>S0092-8674(00)X0438-2</json:string></pii><volume>83</volume><issue>7</issue><pages><first>1243</first><last>1252</last></pages><genre><json:string>journal</json:string></genre></host><namedEntities><unitex><date><json:string>1995</json:string></date><geogName></geogName><orgName><json:string>United States Siochemical</json:string><json:string>Pharmacia</json:string><json:string>Genentech</json:string><json:string>Clontech</json:string></orgName><orgName_funder></orgName_funder><orgName_provider></orgName_provider><persName><json:string>H. Hsu</json:string><json:string>J. Biol</json:string><json:string>M. Ft</json:string><json:string>J. Cell</json:string><json:string>B. Sadoul</json:string><json:string>Keith Williamson</json:string><json:string>Gerald</json:string><json:string>The</json:string><json:string>Suzy Wong</json:string><json:string>Steve McKnight</json:string><json:string>David V. Goeddel</json:string><json:string>Ming-Gui Pan</json:string><json:string>Bruce Hay</json:string><json:string>Elmer Thermocycler</json:string><json:string>William J. Henzel</json:string></persName><placeName><json:string>San Bruno</json:string><json:string>Nonstad</json:string><json:string>San Francisco</json:string></placeName><ref_url></ref_url><ref_bibl><json:string>Vandenabeele et al., 1995</json:string><json:string>Hsu et al., 1995</json:string><json:string>Crook et al., 1993</json:string><json:string>Rothe et al., 1994, 1995</json:string><json:string>Sato et al., 1995a, 1995b</json:string><json:string>Sarma et al., 1995</json:string><json:string>Boldin et al., 1995</json:string><json:string>Ausubel et al., 1967</json:string><json:string>Birnbaum et al., 1994</json:string><json:string>Rothe et al., 1992</json:string><json:string>Chevray and Nathans, 1992</json:string><json:string>see Freemont, 1993</json:string><json:string>Cheng et al., 1995</json:string><json:string>Chinnaiyan et al., 1995</json:string><json:string>Clem and Miller, 1994</json:string><json:string>Martinou et al., 1995</json:string><json:string>Vaux et al., 1994</json:string><json:string>Schall et al., 1990</json:string><json:string>reviewed by Raff, 1992</json:string><json:string>Roy et al., 1995</json:string><json:string>reviewed by Tartaglia and Goeddel, 1992</json:string><json:string>Beidler et al., 1995</json:string><json:string>Schwabeand Ktug, 1994</json:string><json:string>Mosialos et al., 1995</json:string><json:string>Rothe et al., 1995</json:string><json:string>Oltvai and Korsmeyer, 1994</json:string><json:string>Berberich et al., 1994</json:string><json:string>Tartaglia et al., 1993b</json:string><json:string>Hay et al., 1995</json:string><json:string>Stanger et al., 1995</json:string><json:string>Song and Donner, 1995</json:string><json:string>Sato et al., 1995a</json:string><json:string>Tartaglia et al., 1991, 1993a</json:string><json:string>Rothe et al., 1994</json:string><json:string>Sugimoto et al., 1994</json:string><json:string>reviewed by Schwabe and Klug, 1994</json:string><json:string>Hu et al., 1994</json:string><json:string>Sambrook et al., 1989</json:string><json:string>Grell et al., 1993</json:string><json:string>Tartaglia et al., 1991</json:string><json:string>reviewed by Clem and Miller, 1994</json:string><json:string>Braunagel et al., 1992</json:string><json:string>Pennica et al., 1992</json:string><json:string>Smith et al., 1994</json:string><json:string>reviewed by Oltvai and Korsmeyer, 1994</json:string></ref_bibl><bibl></bibl></unitex></namedEntities><ark><json:string>ark:/67375/6H6-4R850QTC-G</json:string></ark><categories><wos><json:string>1 - 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Goeddel</surname></persName><affiliation>Department of Molecular Biology Tularik, Incorporated 270 East Grand Avenue South San Francisco, California 94080, USA</affiliation></author><idno type="istex">EA5DDDFB1957ABF234D2BDA8D894BDDAEE97E52D</idno><idno type="ark">ark:/67375/6H6-4R850QTC-G</idno><idno type="DOI">10.1016/0092-8674(95)90149-3</idno><idno type="PII">0092-8674(95)90149-3</idno></analytic><monogr><title level="j">Cell</title><title level="j" type="abbrev">CELL</title><idno type="pISSN">0092-8674</idno><idno type="PII">S0092-8674(00)X0438-2</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1995"></date><biblScope unit="volume">83</biblScope><biblScope unit="issue">7</biblScope><biblScope unit="page" from="1243">1243</biblScope><biblScope unit="page" to="1252">1252</biblScope></imprint></monogr></biblStruct></sourceDesc></fileDesc><profileDesc><creation><date>1995</date></creation><langUsage><language ident="en">en</language></langUsage><abstract xml:lang="en"><p>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.</p></abstract></profileDesc><revisionDesc><change when="1995-11-27">Modified</change><change when="1995">Published</change></revisionDesc></teiHeader></istex:fulltextTEI><json:item><extension>txt</extension><original>false</original><mimetype>text/plain</mimetype><uri>https://api.istex.fr/ark:/67375/6H6-4R850QTC-G/fulltext.txt</uri></json:item></fulltext><metadata><istex:metadataXml wicri:clean="Elsevier, elements deleted: tail"><istex:xmlDeclaration>version="1.0" encoding="utf-8"</istex:xmlDeclaration><istex:docType PUBLIC="-//ES//DTD journal article DTD version 4.5.2//EN//XML" URI="art452.dtd" name="istex:docType"></istex:docType><istex:document><converted-article version="4.5.2" docsubtype="fla"><item-info><jid>CELL</jid><aid>95901493</aid><ce:pii>0092-8674(95)90149-3</ce:pii><ce:doi>10.1016/0092-8674(95)90149-3</ce:doi><ce:copyright type="unknown" year="1995"></ce:copyright></item-info><head><ce:dochead><ce:textfn>Article</ce:textfn></ce:dochead><ce:title>The TNFR2-TRAF signaling complex contains two novel proteins related to baculoviral inhibitor of apoptosis proteins</ce:title><ce:author-group><ce:author><ce:given-name>Mike</ce:given-name><ce:surname>Rothe</ce:surname><ce:cross-ref refid="AFF1"><ce:sup>∗</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>Ming-Gui</ce:given-name><ce:surname>Pan</ce:surname><ce:cross-ref refid="AFF1"><ce:sup>∗</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>William J.</ce:given-name><ce:surname>Henzel</ce:surname><ce:cross-ref refid="AFF2"><ce:sup>†</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>T.Merrill</ce:given-name><ce:surname>Ayres</ce:surname><ce:cross-ref refid="AFF1"><ce:sup>∗</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>David</ce:given-name><ce:surname>V. Goeddel</ce:surname><ce:cross-ref refid="AFF1"><ce:sup>∗</ce:sup></ce:cross-ref></ce:author><ce:affiliation id="AFF1"><ce:label>a</ce:label><ce:textfn>Department of Molecular Biology Tularik, Incorporated 270 East Grand Avenue South San Francisco, California 94080, USA</ce:textfn></ce:affiliation><ce:affiliation id="AFF2"><ce:label>b</ce:label><ce:textfn>Department of Protein Chemistry Genentech, Incorporated 460 Point San Bruno Boulevard South San Francisco, California 94080, USA</ce:textfn></ce:affiliation></ce:author-group><ce:date-received day="16" month="10" year="1995"></ce:date-received><ce:date-revised day="27" month="11" year="1995"></ce:date-revised><ce:abstract><ce:section-title>Abstract</ce:section-title><ce:abstract-sec><ce:simple-para>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.</ce:simple-para></ce:abstract-sec></ce:abstract></head></converted-article></istex:document></istex:metadataXml><mods version="3.6"><titleInfo><title>The TNFR2-TRAF signaling complex contains two novel proteins related to baculoviral inhibitor of apoptosis proteins</title></titleInfo><titleInfo type="alternative" contentType="CDATA"><title>The TNFR2-TRAF signaling complex contains two novel proteins related to baculoviral inhibitor of apoptosis proteins</title></titleInfo><name type="personal"><namePart type="given">Mike</namePart><namePart type="family">Rothe</namePart><affiliation>Department of Molecular Biology Tularik, Incorporated 270 East Grand Avenue South San Francisco, California 94080, USA</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Ming-Gui</namePart><namePart type="family">Pan</namePart><affiliation>Department of Molecular Biology Tularik, Incorporated 270 East Grand Avenue South San Francisco, California 94080, USA</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">William J.</namePart><namePart type="family">Henzel</namePart><affiliation>Department of Protein Chemistry Genentech, Incorporated 460 Point San Bruno Boulevard South San Francisco, California 94080, USA</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">T.Merrill</namePart><namePart type="family">Ayres</namePart><affiliation>Department of Molecular Biology Tularik, Incorporated 270 East Grand Avenue South San Francisco, California 94080, USA</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">David</namePart><namePart type="family">V. Goeddel</namePart><affiliation>Department of Molecular Biology Tularik, Incorporated 270 East Grand Avenue South San Francisco, California 94080, USA</affiliation><role><roleTerm type="text">author</roleTerm></role></name><typeOfResource>text</typeOfResource><genre type="research-article" displayLabel="Full-length article" authority="ISTEX" authorityURI="https://content-type.data.istex.fr" valueURI="https://content-type.data.istex.fr/ark:/67375/XTP-1JC4F85T-7">research-article</genre><originInfo><publisher>ELSEVIER</publisher><dateIssued encoding="w3cdtf">1995</dateIssued><dateModified encoding="w3cdtf">1995-11-27</dateModified><copyrightDate encoding="w3cdtf">1995</copyrightDate></originInfo><language><languageTerm type="code" authority="iso639-2b">eng</languageTerm><languageTerm type="code" authority="rfc3066">en</languageTerm></language><abstract 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.</abstract><note type="content">Section title: Article</note><relatedItem type="host"><titleInfo><title>Cell</title></titleInfo><titleInfo type="abbreviated"><title>CELL</title></titleInfo><genre type="journal" authority="ISTEX" authorityURI="https://publication-type.data.istex.fr" valueURI="https://publication-type.data.istex.fr/ark:/67375/JMC-0GLKJH51-B">journal</genre><originInfo><publisher>ELSEVIER</publisher><dateIssued encoding="w3cdtf">1995</dateIssued></originInfo><identifier type="ISSN">0092-8674</identifier><identifier type="PII">S0092-8674(00)X0438-2</identifier><part><date>1995</date><detail type="volume"><number>83</number><caption>vol.</caption></detail><detail type="issue"><number>7</number><caption>no.</caption></detail><extent unit="issue-pages"><start>1059</start><end>1271</end></extent><extent unit="pages"><start>1243</start><end>1252</end></extent></part></relatedItem><identifier type="istex">EA5DDDFB1957ABF234D2BDA8D894BDDAEE97E52D</identifier><identifier type="ark">ark:/67375/6H6-4R850QTC-G</identifier><identifier type="DOI">10.1016/0092-8674(95)90149-3</identifier><identifier type="PII">0092-8674(95)90149-3</identifier><recordInfo><recordContentSource authority="ISTEX" authorityURI="https://loaded-corpus.data.istex.fr" valueURI="https://loaded-corpus.data.istex.fr/ark:/67375/XBH-HKKZVM7B-M">elsevier</recordContentSource></recordInfo></mods><json:item><extension>json</extension><original>false</original><mimetype>application/json</mimetype><uri>https://api.istex.fr/ark:/67375/6H6-4R850QTC-G/record.json</uri></json:item></metadata></istex></record>Pour manipuler ce document sous Unix (Dilib)
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