Unraveling the molecular architecture of a G protein-coupled receptor/β-arrestin/Erk module complex
Identifieur interne : 000515 ( Main/Exploration ); précédent : 000514; suivant : 000516Unraveling the molecular architecture of a G protein-coupled receptor/β-arrestin/Erk module complex
Auteurs : Thomas Bourquard [France] ; Flavie Landomiel [France] ; Eric Reiter [France] ; Pascale Crépieux [France] ; David W. Ritchie [France] ; Jérôme Azé [France] ; Anne Poupon [France]Source :
- Scientific Reports [ 2045-2322 ] ; 2015-06.
English descriptors
Abstract
β-arrestins serve as signaling scaffolds downstream of G protein-coupled receptors, and thus play a crucial role in a plethora of cellular processes. Although it is largely accepted that the ability of β-arrestins to interact simultaneously with many protein partners is key in G protein-independent signaling of GPCRs, only the precise knowledge of these multimeric arrangements will allow a full understanding of the dynamics of these interactions and their functional consequences. However, current experimental procedures for the determination of the three-dimensional structures of protein-protein complexes are not well adapted to analyze these short-lived, multi-component assemblies. We propose a model of the receptor/β-arrestin/Erk1 signaling module, which is consistent with most of the available experimental data. Moreover, for the β-arrestin/Raf1 and the β-arrestin/ERK interactions, we have used the model to design interfering peptides and shown that they compete with both partners, hereby demonstrating the validity of the predicted interaction regions.
Url:
DOI: 10.1038/srep10760
Affiliations:
- France
- Centre-Val de Loire, Grand Est, Lorraine (région), Région Centre
- Metz, Nancy, Tours
- Centre Val de Loire Université, Université de Lorraine, Université de Tours
Links toward previous steps (curation, corpus...)
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- to stream Hal, to step Curation: 005080
- to stream Hal, to step Checkpoint: 000495
- to stream Main, to step Merge: 000515
- to stream Main, to step Curation: 000515
Le document en format XML
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Tours</orgName><desc><address><addrLine>60 rue du Plat d'Étain, 37020 Tours cedex 1 </addrLine><country key="FR"></country></address><ref type="url">http://www.univ-tours.fr</ref></desc></org></tutelle><tutelle name="UR0085" active="#struct-92114" type="direct"><org type="institution" xml:id="struct-92114" status="VALID"><orgName>Institut National de la Recherche Agronomique</orgName><orgName type="acronym">INRA</orgName><desc><address><country key="FR"></country></address><ref type="url">http://www.inra.fr</ref></desc></org></tutelle><tutelle name="UMR7247" active="#struct-441569" type="direct"><org type="institution" xml:id="struct-441569" status="VALID"><idno type="ISNI">0000000122597504</idno><idno type="IdRef">02636817X</idno><orgName>Centre National de la Recherche Scientifique</orgName><orgName type="acronym">CNRS</orgName><date type="start">1939-10-19</date><desc><address><country key="FR"></country></address><ref type="url">http://www.cnrs.fr/</ref></desc></org></tutelle><tutelle active="#struct-200225" type="direct"><org type="institution" xml:id="struct-200225" status="VALID"><orgName>Institut Français du Cheval et de l'Equitation [Saumur]</orgName><desc><address><addrLine>Terrefort, BP 207, F-49411 Saumur</addrLine><country key="FR"></country></address><ref type="url">http://www.ifce.fr/</ref></desc></org></tutelle></tutelles></hal:affiliation><country>France</country><placeName><settlement type="city">Tours</settlement><region type="old region" nuts="2">Région Centre</region><region type="region" nuts="2">Centre-Val de Loire</region></placeName><orgName type="university">Université de Tours</orgName><orgName type="institution" wicri:auto="newGroup">Centre Val de Loire Université</orgName></affiliation></author></analytic><idno type="DOI">10.1038/srep10760</idno><series><title level="j">Scientific Reports</title><idno type="ISSN">2045-2322</idno><imprint><date type="datePub">2015-06</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="mix" xml:lang="en"><term>Biochemical networks</term><term>Molecular modelling</term><term>Protein structure predictions</term><term>Signal processing</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">β-arrestins serve as signaling scaffolds downstream of G protein-coupled receptors, and thus play a crucial role in a plethora of cellular processes. Although it is largely accepted that the ability of β-arrestins to interact simultaneously with many protein partners is key in G protein-independent signaling of GPCRs, only the precise knowledge of these multimeric arrangements will allow a full understanding of the dynamics of these interactions and their functional consequences. However, current experimental procedures for the determination of the three-dimensional structures of protein-protein complexes are not well adapted to analyze these short-lived, multi-component assemblies. We propose a model of the receptor/β-arrestin/Erk1 signaling module, which is consistent with most of the available experimental data. Moreover, for the β-arrestin/Raf1 and the β-arrestin/ERK interactions, we have used the model to design interfering peptides and shown that they compete with both partners, hereby demonstrating the validity of the predicted interaction regions.</div></front></TEI><affiliations><list><country><li>France</li></country><region><li>Centre-Val de Loire</li><li>Grand Est</li><li>Lorraine (région)</li><li>Région Centre</li></region><settlement><li>Metz</li><li>Nancy</li><li>Tours</li></settlement><orgName><li>Centre Val de Loire Université</li><li>Université de Lorraine</li><li>Université de Tours</li></orgName></list><tree><country name="France"><region name="Région Centre"><name sortKey="Bourquard, Thomas" sort="Bourquard, Thomas" uniqKey="Bourquard T" first="Thomas" last="Bourquard">Thomas Bourquard</name></region><name sortKey="Aze, Jerome" sort="Aze, Jerome" uniqKey="Aze J" first="Jérôme" last="Azé">Jérôme Azé</name><name sortKey="Crepieux, Pascale" sort="Crepieux, Pascale" uniqKey="Crepieux P" first="Pascale" last="Crépieux">Pascale Crépieux</name><name sortKey="Landomiel, Flavie" sort="Landomiel, Flavie" uniqKey="Landomiel F" first="Flavie" last="Landomiel">Flavie Landomiel</name><name sortKey="Poupon, Anne" sort="Poupon, Anne" uniqKey="Poupon A" first="Anne" last="Poupon">Anne Poupon</name><name sortKey="Reiter, Eric" sort="Reiter, Eric" uniqKey="Reiter E" first="Eric" last="Reiter">Eric Reiter</name><name sortKey="Ritchie, David W" sort="Ritchie, David W" uniqKey="Ritchie D" first="David W." last="Ritchie">David W. Ritchie</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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