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
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Le document en format XML
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<desc><address><addrLine>60 rue du Plat d'Étain, 37020 Tours cedex 1 </addrLine>
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</address>
<ref type="url">http://www.univ-tours.fr</ref>
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<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>
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</address>
<ref type="url">http://www.inra.fr</ref>
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<orgName>Centre National de la Recherche Scientifique</orgName>
<orgName type="acronym">CNRS</orgName>
<date type="start">1939-10-19</date>
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<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>
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</address>
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<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>
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<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>
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<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>
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<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>
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