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-...

Ausführliche Beschreibung

Gespeichert in:
Bibliographische Detailangaben
Veröffentlicht in:Biochimica et biophysica acta 2013-01, Vol.1834 (1), p.292-300
Hauptverfasser: Park, Young-Hoon, Jeong, Mi Suk, Park, Hyun Ho, Jang, Se Bok
Format: Artikel
Sprache:eng
Schlagworte:
Online-Zugang:Volltext
Tags: Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
container_end_page 300
container_issue 1
container_start_page 292
container_title Biochimica et biophysica acta
container_volume 1834
creator Park, Young-Hoon
Jeong, Mi Suk
Park, Hyun Ho
Jang, Se Bok
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
format Article
fullrecord <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_1823945684</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>S1570963912001860</els_id><sourcerecordid>1823945684</sourcerecordid><originalsourceid>FETCH-LOGICAL-c485t-26d5c12a02e120dfd3b12b238ef77b5adc3fa55c2a90ccaa3d2f09a77d624f33</originalsourceid><addsrcrecordid>eNqFkU1v1DAQhi1ERUvhHyDwkUuCP-LYuSBVLQuVWhVBOVuOPaZebeJgewv8-3qVwhFOM4fnnRk9g9ArSlpKaP9u246jWczSMkJZS1RLKH-CTqiSqqGd6J7WXkjSDD0fjtHznLeEMCKleIaOGRsYEz09QdebmCZTQpxx9LjcAXZgyh12cTJhxjZOyw5-4RHKT4AZb84uLrCZHf5y-ZniJcUCYc64kvehpPgCHXmzy_DysZ6i282H2_NPzdXNx8vzs6vGdkqUhvVOWMoMYUAZcd7xkbKRcQVeylEYZ7k3QlhmBmKtMdwxTwYjpetZ5zk_RW_XsfWAH3vIRU8hW9jtzAxxnzVVjA-d6FX3f5RJLoa-7q5ot6I2xZwTeL2kMJn0W1OiD8r1Vq_K9UG5JkpX5TX2-nHDfpzA_Q39cVyBNyvgTdTmewpZf_taJ4j6D9r16kC8Xwmozu4DJJ1tgNmCCwls0S6Gf9_wANdRm6E</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>1273596238</pqid></control><display><type>article</type><title>Formation of the death domain complex between FADD and RIP1 proteins in vitro</title><source>MEDLINE</source><source>Elsevier ScienceDirect Journals Complete</source><creator>Park, Young-Hoon ; Jeong, Mi Suk ; Park, Hyun Ho ; Jang, Se Bok</creator><creatorcontrib>Park, Young-Hoon ; Jeong, Mi Suk ; Park, Hyun Ho ; Jang, Se Bok</creatorcontrib><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><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>
fulltext fulltext
identifier ISSN: 1570-9639
ispartof Biochimica et biophysica acta, 2013-01, Vol.1834 (1), p.292-300
issn 1570-9639
0006-3002
1878-1454
language eng
recordid cdi_proquest_miscellaneous_1823945684
source MEDLINE; Elsevier ScienceDirect Journals Complete
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
url https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-19T07%3A44%3A05IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Formation%20of%20the%20death%20domain%20complex%20between%20FADD%20and%20RIP1%20proteins%20in%20vitro&rft.jtitle=Biochimica%20et%20biophysica%20acta&rft.au=Park,%20Young-Hoon&rft.date=2013-01&rft.volume=1834&rft.issue=1&rft.spage=292&rft.epage=300&rft.pages=292-300&rft.issn=1570-9639&rft.eissn=1878-1454&rft_id=info:doi/10.1016/j.bbapap.2012.08.013&rft_dat=%3Cproquest_cross%3E1823945684%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=1273596238&rft_id=info:pmid/22922561&rft_els_id=S1570963912001860&rfr_iscdi=true