Formation of the death domain complex between FADD and RIP1 proteins in vitro
Fas-associated death domain (FADD) protein is an adapter molecule that bridges the interactions between membrane death receptors and initiator caspases. The death receptors contain an intracellular death domain (DD) which is essential to the transduction of the apoptotic signal. The kinase receptor-...
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description | Fas-associated death domain (FADD) protein is an adapter molecule that bridges the interactions between membrane death receptors and initiator caspases. The death receptors contain an intracellular death domain (DD) which is essential to the transduction of the apoptotic signal. The kinase receptor-interacting protein 1 (RIP1) is crucial to programmed necrosis. The cell type interplay between FADD and RIP1, which mediates both necrosis and NF-κB activation, has been evaluated in other studies, but the mechanism of the interaction of the FADD and RIP1 proteins remain poorly understood. Here, we provided evidence indicating that the DD of human FADD binds to the DD of RIP1 in vitro. We developed a molecular docking model using homology modeling based on the structures of FADD and RIP1. In addition, we found that two structure-based mutants (G109A and R114A) of the FADD DD were able to bind to the RIP1 DD, and two mutations (Q169A and N171A) of FADD DD and four mutations (G595, K596, E620, and D622) of RIP1 DD disrupted the FADD–RIP1 interaction. Six mutations (Q169A, N171A, G595, K596, E620, and D622) lowered the stability of the FADD–RIP1 complex and induced aggregation that structurally destabilized the complex, thus disrupting the interaction.
► DD of human FADD binds to the DD of RIP1 in vitro. ► Structural models of FADD DD and RIP1 DD interactions were predicted. ► Six mutations of FADD or RIP1 disrupted FADD and RIP1 interaction. |
doi_str_mv | 10.1016/j.bbapap.2012.08.013 |
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► DD of human FADD binds to the DD of RIP1 in vitro. ► Structural models of FADD DD and RIP1 DD interactions were predicted. ► Six mutations of FADD or RIP1 disrupted FADD and RIP1 interaction.</description><identifier>ISSN: 1570-9639</identifier><identifier>ISSN: 0006-3002</identifier><identifier>EISSN: 1878-1454</identifier><identifier>DOI: 10.1016/j.bbapap.2012.08.013</identifier><identifier>PMID: 22922561</identifier><language>eng</language><publisher>Netherlands: Elsevier B.V</publisher><subject>Amino Acid Substitution ; apoptosis ; caspases ; FADD ; Fas-Associated Death Domain Protein - chemistry ; Fas-Associated Death Domain Protein - genetics ; Fas-Associated Death Domain Protein - metabolism ; Humans ; Interaction ; Modeling ; Molecular Docking Simulation ; molecular models ; Multiprotein Complexes - chemistry ; Multiprotein Complexes - genetics ; Multiprotein Complexes - metabolism ; mutants ; mutation ; Mutation, Missense ; necrosis ; Nuclear Pore Complex Proteins - chemistry ; Nuclear Pore Complex Proteins - genetics ; Nuclear Pore Complex Proteins - metabolism ; Protein Binding ; Protein Structure, Quaternary ; Protein Structure, Tertiary ; receptors ; RIP1 ; RNA-Binding Proteins - chemistry ; RNA-Binding Proteins - genetics ; RNA-Binding Proteins - metabolism ; transcription factor NF-kappa B</subject><ispartof>Biochimica et biophysica acta, 2013-01, Vol.1834 (1), p.292-300</ispartof><rights>2012 Elsevier B.V.</rights><rights>Copyright © 2012 Elsevier B.V. All rights reserved.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c485t-26d5c12a02e120dfd3b12b238ef77b5adc3fa55c2a90ccaa3d2f09a77d624f33</citedby><cites>FETCH-LOGICAL-c485t-26d5c12a02e120dfd3b12b238ef77b5adc3fa55c2a90ccaa3d2f09a77d624f33</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.bbapap.2012.08.013$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3550,4024,27923,27924,27925,45995</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/22922561$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Park, Young-Hoon</creatorcontrib><creatorcontrib>Jeong, Mi Suk</creatorcontrib><creatorcontrib>Park, Hyun Ho</creatorcontrib><creatorcontrib>Jang, Se Bok</creatorcontrib><title>Formation of the death domain complex between FADD and RIP1 proteins in vitro</title><title>Biochimica et biophysica acta</title><addtitle>Biochim Biophys Acta</addtitle><description>Fas-associated death domain (FADD) protein is an adapter molecule that bridges the interactions between membrane death receptors and initiator caspases. The death receptors contain an intracellular death domain (DD) which is essential to the transduction of the apoptotic signal. The kinase receptor-interacting protein 1 (RIP1) is crucial to programmed necrosis. The cell type interplay between FADD and RIP1, which mediates both necrosis and NF-κB activation, has been evaluated in other studies, but the mechanism of the interaction of the FADD and RIP1 proteins remain poorly understood. Here, we provided evidence indicating that the DD of human FADD binds to the DD of RIP1 in vitro. We developed a molecular docking model using homology modeling based on the structures of FADD and RIP1. In addition, we found that two structure-based mutants (G109A and R114A) of the FADD DD were able to bind to the RIP1 DD, and two mutations (Q169A and N171A) of FADD DD and four mutations (G595, K596, E620, and D622) of RIP1 DD disrupted the FADD–RIP1 interaction. Six mutations (Q169A, N171A, G595, K596, E620, and D622) lowered the stability of the FADD–RIP1 complex and induced aggregation that structurally destabilized the complex, thus disrupting the interaction.
► DD of human FADD binds to the DD of RIP1 in vitro. ► Structural models of FADD DD and RIP1 DD interactions were predicted. ► Six mutations of FADD or RIP1 disrupted FADD and RIP1 interaction.</description><subject>Amino Acid Substitution</subject><subject>apoptosis</subject><subject>caspases</subject><subject>FADD</subject><subject>Fas-Associated Death Domain Protein - chemistry</subject><subject>Fas-Associated Death Domain Protein - genetics</subject><subject>Fas-Associated Death Domain Protein - metabolism</subject><subject>Humans</subject><subject>Interaction</subject><subject>Modeling</subject><subject>Molecular Docking Simulation</subject><subject>molecular models</subject><subject>Multiprotein Complexes - chemistry</subject><subject>Multiprotein Complexes - genetics</subject><subject>Multiprotein Complexes - metabolism</subject><subject>mutants</subject><subject>mutation</subject><subject>Mutation, Missense</subject><subject>necrosis</subject><subject>Nuclear Pore Complex Proteins - chemistry</subject><subject>Nuclear Pore Complex Proteins - genetics</subject><subject>Nuclear Pore Complex Proteins - metabolism</subject><subject>Protein Binding</subject><subject>Protein Structure, Quaternary</subject><subject>Protein Structure, Tertiary</subject><subject>receptors</subject><subject>RIP1</subject><subject>RNA-Binding Proteins - chemistry</subject><subject>RNA-Binding Proteins - genetics</subject><subject>RNA-Binding Proteins - metabolism</subject><subject>transcription factor NF-kappa B</subject><issn>1570-9639</issn><issn>0006-3002</issn><issn>1878-1454</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2013</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkU1v1DAQhi1ERUvhHyDwkUuCP-LYuSBVLQuVWhVBOVuOPaZebeJgewv8-3qVwhFOM4fnnRk9g9ArSlpKaP9u246jWczSMkJZS1RLKH-CTqiSqqGd6J7WXkjSDD0fjtHznLeEMCKleIaOGRsYEz09QdebmCZTQpxx9LjcAXZgyh12cTJhxjZOyw5-4RHKT4AZb84uLrCZHf5y-ZniJcUCYc64kvehpPgCHXmzy_DysZ6i282H2_NPzdXNx8vzs6vGdkqUhvVOWMoMYUAZcd7xkbKRcQVeylEYZ7k3QlhmBmKtMdwxTwYjpetZ5zk_RW_XsfWAH3vIRU8hW9jtzAxxnzVVjA-d6FX3f5RJLoa-7q5ot6I2xZwTeL2kMJn0W1OiD8r1Vq_K9UG5JkpX5TX2-nHDfpzA_Q39cVyBNyvgTdTmewpZf_taJ4j6D9r16kC8Xwmozu4DJJ1tgNmCCwls0S6Gf9_wANdRm6E</recordid><startdate>201301</startdate><enddate>201301</enddate><creator>Park, Young-Hoon</creator><creator>Jeong, Mi Suk</creator><creator>Park, Hyun Ho</creator><creator>Jang, Se Bok</creator><general>Elsevier B.V</general><scope>FBQ</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>7X8</scope><scope>7QO</scope><scope>8FD</scope><scope>FR3</scope><scope>P64</scope></search><sort><creationdate>201301</creationdate><title>Formation of the death domain complex between FADD and RIP1 proteins in vitro</title><author>Park, Young-Hoon ; Jeong, Mi Suk ; Park, Hyun Ho ; Jang, Se Bok</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c485t-26d5c12a02e120dfd3b12b238ef77b5adc3fa55c2a90ccaa3d2f09a77d624f33</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2013</creationdate><topic>Amino Acid Substitution</topic><topic>apoptosis</topic><topic>caspases</topic><topic>FADD</topic><topic>Fas-Associated Death Domain Protein - chemistry</topic><topic>Fas-Associated Death Domain Protein - genetics</topic><topic>Fas-Associated Death Domain Protein - metabolism</topic><topic>Humans</topic><topic>Interaction</topic><topic>Modeling</topic><topic>Molecular Docking Simulation</topic><topic>molecular models</topic><topic>Multiprotein Complexes - chemistry</topic><topic>Multiprotein Complexes - genetics</topic><topic>Multiprotein Complexes - metabolism</topic><topic>mutants</topic><topic>mutation</topic><topic>Mutation, Missense</topic><topic>necrosis</topic><topic>Nuclear Pore Complex Proteins - chemistry</topic><topic>Nuclear Pore Complex Proteins - genetics</topic><topic>Nuclear Pore Complex Proteins - metabolism</topic><topic>Protein Binding</topic><topic>Protein Structure, Quaternary</topic><topic>Protein Structure, Tertiary</topic><topic>receptors</topic><topic>RIP1</topic><topic>RNA-Binding Proteins - chemistry</topic><topic>RNA-Binding Proteins - genetics</topic><topic>RNA-Binding Proteins - metabolism</topic><topic>transcription factor NF-kappa B</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Park, Young-Hoon</creatorcontrib><creatorcontrib>Jeong, Mi Suk</creatorcontrib><creatorcontrib>Park, Hyun Ho</creatorcontrib><creatorcontrib>Jang, Se Bok</creatorcontrib><collection>AGRIS</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><collection>Biotechnology Research Abstracts</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><jtitle>Biochimica et biophysica acta</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Park, Young-Hoon</au><au>Jeong, Mi Suk</au><au>Park, Hyun Ho</au><au>Jang, Se Bok</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Formation of the death domain complex between FADD and RIP1 proteins in vitro</atitle><jtitle>Biochimica et biophysica acta</jtitle><addtitle>Biochim Biophys Acta</addtitle><date>2013-01</date><risdate>2013</risdate><volume>1834</volume><issue>1</issue><spage>292</spage><epage>300</epage><pages>292-300</pages><issn>1570-9639</issn><issn>0006-3002</issn><eissn>1878-1454</eissn><abstract>Fas-associated death domain (FADD) protein is an adapter molecule that bridges the interactions between membrane death receptors and initiator caspases. The death receptors contain an intracellular death domain (DD) which is essential to the transduction of the apoptotic signal. The kinase receptor-interacting protein 1 (RIP1) is crucial to programmed necrosis. The cell type interplay between FADD and RIP1, which mediates both necrosis and NF-κB activation, has been evaluated in other studies, but the mechanism of the interaction of the FADD and RIP1 proteins remain poorly understood. Here, we provided evidence indicating that the DD of human FADD binds to the DD of RIP1 in vitro. We developed a molecular docking model using homology modeling based on the structures of FADD and RIP1. In addition, we found that two structure-based mutants (G109A and R114A) of the FADD DD were able to bind to the RIP1 DD, and two mutations (Q169A and N171A) of FADD DD and four mutations (G595, K596, E620, and D622) of RIP1 DD disrupted the FADD–RIP1 interaction. Six mutations (Q169A, N171A, G595, K596, E620, and D622) lowered the stability of the FADD–RIP1 complex and induced aggregation that structurally destabilized the complex, thus disrupting the interaction.
► DD of human FADD binds to the DD of RIP1 in vitro. ► Structural models of FADD DD and RIP1 DD interactions were predicted. ► Six mutations of FADD or RIP1 disrupted FADD and RIP1 interaction.</abstract><cop>Netherlands</cop><pub>Elsevier B.V</pub><pmid>22922561</pmid><doi>10.1016/j.bbapap.2012.08.013</doi><tpages>9</tpages></addata></record> |
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subjects | Amino Acid Substitution apoptosis caspases FADD Fas-Associated Death Domain Protein - chemistry Fas-Associated Death Domain Protein - genetics Fas-Associated Death Domain Protein - metabolism Humans Interaction Modeling Molecular Docking Simulation molecular models Multiprotein Complexes - chemistry Multiprotein Complexes - genetics Multiprotein Complexes - metabolism mutants mutation Mutation, Missense necrosis Nuclear Pore Complex Proteins - chemistry Nuclear Pore Complex Proteins - genetics Nuclear Pore Complex Proteins - metabolism Protein Binding Protein Structure, Quaternary Protein Structure, Tertiary receptors RIP1 RNA-Binding Proteins - chemistry RNA-Binding Proteins - genetics RNA-Binding Proteins - metabolism transcription factor NF-kappa B |
title | Formation of the death domain complex between FADD and RIP1 proteins in vitro |
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