A comprehensive view of the ß-arrestinome

G protein-coupled receptors (GPCRs) are membrane receptors critically involved in sensing the environment and orchestrating physiological processes. As such, they transduce extracellular signals such as hormone, neurotransmitters, ions, and light into an integrated cell response. The intracellular t...

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Authors: Crépieux, Pascale, Poupon, Anne, Langonné Gallay, Nathalie, Reiter, Éric R., Delgado Blanco, Javier, Schaefer, Martin H., Bourquard, Thomas, Serrano Pubull, Luis, 1982-, Kiel, Christina
Format: article
Status:Published version
Publication Date:2017
Country:España
Institution:Universitat Pompeu Fabra
Repository:Repositorio Digital de la UPF
OAI Identifier:oai:repositori.upf.edu:10230/34748
Online Access:http://hdl.handle.net/10230/34748
http://dx.doi.org/10.3389/fendo.2017.00032
Access Level:Open access
Keyword:G protein-coupled receptors
Hub proteins
Protein/protein interaction network
Systems biology
β-arrestins
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spelling A comprehensive view of the ß-arrestinomeCrépieux, PascalePoupon, AnneLangonné Gallay, NathalieReiter, Éric R.Delgado Blanco, JavierSchaefer, Martin H.Bourquard, ThomasSerrano Pubull, Luis, 1982-Kiel, ChristinaG protein-coupled receptorsHub proteinsProtein/protein interaction networkSystems biologyβ-arrestinsG protein-coupled receptors (GPCRs) are membrane receptors critically involved in sensing the environment and orchestrating physiological processes. As such, they transduce extracellular signals such as hormone, neurotransmitters, ions, and light into an integrated cell response. The intracellular trafficking, internalization, and signaling ability of ligand-activated GPCRs are controlled by arrestins, adaptor proteins that they interact with upon ligand binding. β-arrestins 1 and 2 in particular are now considered as hub proteins assembling multiprotein complexes to regulate receptor fate and transduce diversified cell responses. While more than 400 β-arrestin interaction partners have been identified so far, much remains to be learnt on how discrimination between so many binding partners is accomplished. Here, we gathered the interacting partners of β-arrestins through database mining and manual curation of the literature to map the β-arrestin interactome (β-arrestinome). We discussed several parameters that determine compatible (AND) or mutually exclusive (XOR) binding of β-arrestin interactors, such as structural constraints, intracellular abundance, or binding affinity.This work was funded by the Agence Nationale de la Recherche GPCRnet project, by the Centre National de la Recherche Scientifique, by the Institut de la Recherche Agronomique PHASE Department, by the Région Centre, and by the European Commission (EC) Framework programme (FP) 7 project SynSignal (contract nr. 613879). LS is supported by the Spanish Ministerio de Economía y Competitividad, Plan Nacional BIO2012-39754, and the European Fund for Economic and Regional Development. LS and CK are particularly grateful for the support of the Spanish Ministry of Economy and Competitiveness, “Centro de Excelencia Severo Ochoa 2013-2017” (SEV-2012-0208).Frontiers201820182017info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionapplication/pdfapplication/pdfhttp://hdl.handle.net/10230/34748http://dx.doi.org/10.3389/fendo.2017.00032reponame:Repositorio Digital de la UPFinstname:Universitat Pompeu FabraInglésFront Endocrinol (Lausanne). 2017 Mar 6;8:32info:eu-repo/grantAgreement/EC/FP7/613879info:eu-repo/grantAgreement/ES/3PN/BIO2012-39754© 2017 Crépieux, Poupon, Langonné-Gallay, Reiter, Delgado, Schaefer, Bourquard, Serrano and Kiel. This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY) (http://creativecommons.org/licenses/by/4.0/). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.http://creativecommons.org/licenses/by/4.0/info:eu-repo/semantics/openAccessoai:repositori.upf.edu:10230/347482026-06-12T07:21:37Z
dc.title.none.fl_str_mv A comprehensive view of the ß-arrestinome
title A comprehensive view of the ß-arrestinome
spellingShingle A comprehensive view of the ß-arrestinome
Crépieux, Pascale
G protein-coupled receptors
Hub proteins
Protein/protein interaction network
Systems biology
β-arrestins
title_short A comprehensive view of the ß-arrestinome
title_full A comprehensive view of the ß-arrestinome
title_fullStr A comprehensive view of the ß-arrestinome
title_full_unstemmed A comprehensive view of the ß-arrestinome
title_sort A comprehensive view of the ß-arrestinome
dc.creator.none.fl_str_mv Crépieux, Pascale
Poupon, Anne
Langonné Gallay, Nathalie
Reiter, Éric R.
Delgado Blanco, Javier
Schaefer, Martin H.
Bourquard, Thomas
Serrano Pubull, Luis, 1982-
Kiel, Christina
author Crépieux, Pascale
author_facet Crépieux, Pascale
Poupon, Anne
Langonné Gallay, Nathalie
Reiter, Éric R.
Delgado Blanco, Javier
Schaefer, Martin H.
Bourquard, Thomas
Serrano Pubull, Luis, 1982-
Kiel, Christina
author_role author
author2 Poupon, Anne
Langonné Gallay, Nathalie
Reiter, Éric R.
Delgado Blanco, Javier
Schaefer, Martin H.
Bourquard, Thomas
Serrano Pubull, Luis, 1982-
Kiel, Christina
author2_role author
author
author
author
author
author
author
author
dc.subject.none.fl_str_mv G protein-coupled receptors
Hub proteins
Protein/protein interaction network
Systems biology
β-arrestins
topic G protein-coupled receptors
Hub proteins
Protein/protein interaction network
Systems biology
β-arrestins
description G protein-coupled receptors (GPCRs) are membrane receptors critically involved in sensing the environment and orchestrating physiological processes. As such, they transduce extracellular signals such as hormone, neurotransmitters, ions, and light into an integrated cell response. The intracellular trafficking, internalization, and signaling ability of ligand-activated GPCRs are controlled by arrestins, adaptor proteins that they interact with upon ligand binding. β-arrestins 1 and 2 in particular are now considered as hub proteins assembling multiprotein complexes to regulate receptor fate and transduce diversified cell responses. While more than 400 β-arrestin interaction partners have been identified so far, much remains to be learnt on how discrimination between so many binding partners is accomplished. Here, we gathered the interacting partners of β-arrestins through database mining and manual curation of the literature to map the β-arrestin interactome (β-arrestinome). We discussed several parameters that determine compatible (AND) or mutually exclusive (XOR) binding of β-arrestin interactors, such as structural constraints, intracellular abundance, or binding affinity.
publishDate 2017
dc.date.none.fl_str_mv 2017
2018
2018
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/10230/34748
http://dx.doi.org/10.3389/fendo.2017.00032
url http://hdl.handle.net/10230/34748
http://dx.doi.org/10.3389/fendo.2017.00032
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv Front Endocrinol (Lausanne). 2017 Mar 6;8:32
info:eu-repo/grantAgreement/EC/FP7/613879
info:eu-repo/grantAgreement/ES/3PN/BIO2012-39754
dc.rights.none.fl_str_mv http://creativecommons.org/licenses/by/4.0/
info:eu-repo/semantics/openAccess
rights_invalid_str_mv http://creativecommons.org/licenses/by/4.0/
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv Frontiers
publisher.none.fl_str_mv Frontiers
dc.source.none.fl_str_mv reponame:Repositorio Digital de la UPF
instname:Universitat Pompeu Fabra
instname_str Universitat Pompeu Fabra
reponame_str Repositorio Digital de la UPF
collection Repositorio Digital de la UPF
repository.name.fl_str_mv
repository.mail.fl_str_mv
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