FADD, a novel death domain-containing protein, interacts with the death domain of fas and initiates apoptosis
Using the cytoplasmic domain of Fas in the yeast two-hybrid system, we have identified a novel interacting protein, FADD, which binds Fas and Fas-FD5, a mutant of Fas possessing enhanced killing activity, but not the functionally inactive mutants Fas-LPR and Fas-FD8. FADD contains a death domain hom...
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| Veröffentlicht in: | Cell 1995-05, Vol.81 (4), p.505-512 |
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| creator | Chinnaiyan, Arul M. O'Rourke, Karen Tewari, Muneesh Dixit, Vishva M. |
| description | Using the cytoplasmic domain of Fas in the yeast two-hybrid system, we have identified a novel interacting protein, FADD, which binds Fas and Fas-FD5, a mutant of Fas possessing enhanced killing activity, but not the functionally inactive mutants Fas-LPR and Fas-FD8. FADD contains a death domain homologous to the death domains of Fas and TNFR-1. A point mutation in FADD, analogous to the
Ipr mutation of Fas, abolishes its ability to bind Fas, suggesting a death domain to death domain interaction. Overexpression of FADD in MCF7 and BJAB cells induces apoptosis, which, like Fas-induced apoptosis, is blocked by CrmA, a specific inhibitor of the interieukin-lβ-converting enzyme. These findings suggest that FADD may play an important role in the proximal signal transduction of Fas. |
| doi_str_mv | 10.1016/0092-8674(95)90071-3 |
| format | Article |
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Ipr mutation of Fas, abolishes its ability to bind Fas, suggesting a death domain to death domain interaction. Overexpression of FADD in MCF7 and BJAB cells induces apoptosis, which, like Fas-induced apoptosis, is blocked by CrmA, a specific inhibitor of the interieukin-lβ-converting enzyme. These findings suggest that FADD may play an important role in the proximal signal transduction of Fas.</description><identifier>ISSN: 0092-8674</identifier><identifier>EISSN: 1097-4172</identifier><identifier>DOI: 10.1016/0092-8674(95)90071-3</identifier><identifier>PMID: 7538907</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Adaptor Proteins, Signal Transducing ; Amino Acid Sequence ; Antigens, Surface - genetics ; Antigens, Surface - metabolism ; Apoptosis ; Base Sequence ; Binding Sites - genetics ; Carrier Proteins - genetics ; Carrier Proteins - isolation & purification ; Carrier Proteins - metabolism ; cDNA ; cell death ; Cell Line ; Cloning, Molecular ; death domain-containing protein ; FADD gene ; Fas antigen ; fas Receptor ; Fas-Associated Death Domain Protein ; Humans ; man ; Molecular Sequence Data ; nucleotide sequence ; Point Mutation ; prediction ; Saccharomyces cerevisiae ; Serpins - pharmacology ; Signal Transduction ; Viral Proteins</subject><ispartof>Cell, 1995-05, Vol.81 (4), p.505-512</ispartof><rights>1995</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c434t-133eff53579ffa9eb55b1b348852640bddccf6cfac08b4e3701cd8c12c85b4573</citedby><cites>FETCH-LOGICAL-c434t-133eff53579ffa9eb55b1b348852640bddccf6cfac08b4e3701cd8c12c85b4573</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/0092-8674(95)90071-3$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>314,776,780,3536,27903,27904,45974</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/7538907$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Chinnaiyan, Arul M.</creatorcontrib><creatorcontrib>O'Rourke, Karen</creatorcontrib><creatorcontrib>Tewari, Muneesh</creatorcontrib><creatorcontrib>Dixit, Vishva M.</creatorcontrib><title>FADD, a novel death domain-containing protein, interacts with the death domain of fas and initiates apoptosis</title><title>Cell</title><addtitle>Cell</addtitle><description>Using the cytoplasmic domain of Fas in the yeast two-hybrid system, we have identified a novel interacting protein, FADD, which binds Fas and Fas-FD5, a mutant of Fas possessing enhanced killing activity, but not the functionally inactive mutants Fas-LPR and Fas-FD8. FADD contains a death domain homologous to the death domains of Fas and TNFR-1. A point mutation in FADD, analogous to the
Ipr mutation of Fas, abolishes its ability to bind Fas, suggesting a death domain to death domain interaction. Overexpression of FADD in MCF7 and BJAB cells induces apoptosis, which, like Fas-induced apoptosis, is blocked by CrmA, a specific inhibitor of the interieukin-lβ-converting enzyme. These findings suggest that FADD may play an important role in the proximal signal transduction of Fas.</description><subject>Adaptor Proteins, Signal Transducing</subject><subject>Amino Acid Sequence</subject><subject>Antigens, Surface - genetics</subject><subject>Antigens, Surface - metabolism</subject><subject>Apoptosis</subject><subject>Base Sequence</subject><subject>Binding Sites - genetics</subject><subject>Carrier Proteins - genetics</subject><subject>Carrier Proteins - isolation & purification</subject><subject>Carrier Proteins - metabolism</subject><subject>cDNA</subject><subject>cell death</subject><subject>Cell Line</subject><subject>Cloning, Molecular</subject><subject>death domain-containing protein</subject><subject>FADD gene</subject><subject>Fas antigen</subject><subject>fas Receptor</subject><subject>Fas-Associated Death Domain Protein</subject><subject>Humans</subject><subject>man</subject><subject>Molecular Sequence Data</subject><subject>nucleotide sequence</subject><subject>Point Mutation</subject><subject>prediction</subject><subject>Saccharomyces cerevisiae</subject><subject>Serpins - pharmacology</subject><subject>Signal Transduction</subject><subject>Viral Proteins</subject><issn>0092-8674</issn><issn>1097-4172</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1995</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkUFrGzEQhUVJSR23_6ABnUIC2VRaSSvtJRDsOC0EcmnPQiuNagWv5K5kh_77rGNj6KU5DcN8b2Z4D6GvlNxQQptvhLR1pRrJL1tx1RIiacU-oAklraw4lfUJmhyRT-gs52dCiBJCnKJTKZhqiZygfnE3n19jg2Pawgo7MGWJXepNiJVNsYw1xN94PaQCIV7jEAsMxpaMX8JIliX8o8HJY28yNtGNaCjBFBi7dVqXlEP-jD56s8rw5VCn6Nfi_ufse_X49PBjdvdYWc54qShj4L1gQrbemxY6ITraMa6UqBtOOues9Y31xhLVcWCSUOuUpbVVouNCsim62O8d__6zgVx0H7KF1cpESJuspawVU1y9C9JGMSabHcj3oB1SzgN4vR5Cb4a_mhK9i0PvvNY7r3Ur9Fscmo2y88P-TdeDO4oO_o_z2_0cRje2AQadbYBowYUBbNEuhf8feAX3tpor</recordid><startdate>19950519</startdate><enddate>19950519</enddate><creator>Chinnaiyan, Arul M.</creator><creator>O'Rourke, Karen</creator><creator>Tewari, Muneesh</creator><creator>Dixit, Vishva M.</creator><general>Elsevier Inc</general><scope>6I.</scope><scope>AAFTH</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7T3</scope><scope>7T5</scope><scope>8FD</scope><scope>FR3</scope><scope>H94</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>19950519</creationdate><title>FADD, a novel death domain-containing protein, interacts with the death domain of fas and initiates apoptosis</title><author>Chinnaiyan, Arul M. ; O'Rourke, Karen ; Tewari, Muneesh ; Dixit, Vishva M.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c434t-133eff53579ffa9eb55b1b348852640bddccf6cfac08b4e3701cd8c12c85b4573</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1995</creationdate><topic>Adaptor Proteins, Signal Transducing</topic><topic>Amino Acid Sequence</topic><topic>Antigens, Surface - genetics</topic><topic>Antigens, Surface - metabolism</topic><topic>Apoptosis</topic><topic>Base Sequence</topic><topic>Binding Sites - genetics</topic><topic>Carrier Proteins - genetics</topic><topic>Carrier Proteins - isolation & purification</topic><topic>Carrier Proteins - metabolism</topic><topic>cDNA</topic><topic>cell death</topic><topic>Cell Line</topic><topic>Cloning, Molecular</topic><topic>death domain-containing protein</topic><topic>FADD gene</topic><topic>Fas antigen</topic><topic>fas Receptor</topic><topic>Fas-Associated Death Domain Protein</topic><topic>Humans</topic><topic>man</topic><topic>Molecular Sequence Data</topic><topic>nucleotide sequence</topic><topic>Point Mutation</topic><topic>prediction</topic><topic>Saccharomyces cerevisiae</topic><topic>Serpins - pharmacology</topic><topic>Signal Transduction</topic><topic>Viral Proteins</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Chinnaiyan, Arul M.</creatorcontrib><creatorcontrib>O'Rourke, Karen</creatorcontrib><creatorcontrib>Tewari, Muneesh</creatorcontrib><creatorcontrib>Dixit, Vishva M.</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Human Genome Abstracts</collection><collection>Immunology Abstracts</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Cell</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Chinnaiyan, Arul M.</au><au>O'Rourke, Karen</au><au>Tewari, Muneesh</au><au>Dixit, Vishva M.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>FADD, a novel death domain-containing protein, interacts with the death domain of fas and initiates apoptosis</atitle><jtitle>Cell</jtitle><addtitle>Cell</addtitle><date>1995-05-19</date><risdate>1995</risdate><volume>81</volume><issue>4</issue><spage>505</spage><epage>512</epage><pages>505-512</pages><issn>0092-8674</issn><eissn>1097-4172</eissn><abstract>Using the cytoplasmic domain of Fas in the yeast two-hybrid system, we have identified a novel interacting protein, FADD, which binds Fas and Fas-FD5, a mutant of Fas possessing enhanced killing activity, but not the functionally inactive mutants Fas-LPR and Fas-FD8. FADD contains a death domain homologous to the death domains of Fas and TNFR-1. A point mutation in FADD, analogous to the
Ipr mutation of Fas, abolishes its ability to bind Fas, suggesting a death domain to death domain interaction. Overexpression of FADD in MCF7 and BJAB cells induces apoptosis, which, like Fas-induced apoptosis, is blocked by CrmA, a specific inhibitor of the interieukin-lβ-converting enzyme. These findings suggest that FADD may play an important role in the proximal signal transduction of Fas.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>7538907</pmid><doi>10.1016/0092-8674(95)90071-3</doi><tpages>8</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Adaptor Proteins, Signal Transducing Amino Acid Sequence Antigens, Surface - genetics Antigens, Surface - metabolism Apoptosis Base Sequence Binding Sites - genetics Carrier Proteins - genetics Carrier Proteins - isolation & purification Carrier Proteins - metabolism cDNA cell death Cell Line Cloning, Molecular death domain-containing protein FADD gene Fas antigen fas Receptor Fas-Associated Death Domain Protein Humans man Molecular Sequence Data nucleotide sequence Point Mutation prediction Saccharomyces cerevisiae Serpins - pharmacology Signal Transduction Viral Proteins |
| title | FADD, a novel death domain-containing protein, interacts with the death domain of fas and initiates apoptosis |
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