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Phosphorylation of filamin A regulates chemokine receptor CCR2 recycling

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dc.contributor.author Pons, Mónica
dc.contributor.author Izquierdo, Ismael
dc.contributor.author Andreu-Carbó, Mireia
dc.contributor.author Garrido, Georgina
dc.contributor.author Planagumà, Jesús
dc.contributor.author Muriel, Olivia
dc.contributor.author Pozo, Miguel Ángel del
dc.contributor.author Isabel Geli, M.
dc.contributor.author Aragay, Anna M.
dc.date.accessioned 2018-06-15T07:49:54Z
dc.date.available 2018-06-15T07:49:54Z
dc.date.issued 2017
dc.identifier.citation Pons M, Izquierdo I, Andreu-Carbo M, Garrido G, Planaguma J, Muriel O et al. Phosphorylation of filamin A regulates chemokine receptor CCR2 recycling. J Cell Sci. 2017 Jan 15;130(2):490-501. DOI: 10.1242/jcs.193821. Epub 2016 Dec 1
dc.identifier.issn 0021-9533
dc.identifier.uri http://hdl.handle.net/10230/34914
dc.description.abstract Proper endosomal trafficking of ligand-activated G-protein-coupled receptors (GPCRs) is essential to spatiotemporally tune their physiological responses. For the monocyte chemoattractant receptor 2 (CCR2B; one of two isoforms encoded by CCR2), endocytic recycling is important to sustain monocyte migration, whereas filamin A (FLNa) is essential for CCL2-induced monocyte migration. Here, we analyze the role of FLNa in the trafficking of CCR2B along the endocytic pathway. In FLNa-knockdown cells, activated CCR2B accumulated in enlarged EEA-1-positive endosomes, which exhibited slow movement and fast fluorescence recovery, suggesting an imbalance between receptor entry and exit rates. Utilizing super-resolution microscopy, we observed that FLNa-GFP, CCR2B and β2-adrenergic receptor (β2AR) were present in actin-enriched endosomal microdomains. Depletion of FLNa decreased CCR2B association with these microdomains and concomitantly delayed CCR2B endosomal traffic, without apparently affecting the number of microdomains. Interestingly, CCR2B and β2AR signaling induced phosphorylation of FLNa at residue S2152, and this phosphorylation event was contributes to sustain receptor recycling. Thus, our data strongly suggest that CCR2B and β2AR signals to FLNa to stimulate its endocytosis and recycling to the plasma membrane.
dc.description.sponsorship This work was supported by grants from Ministerio de Economía y Competitividad (BFU2011-30080 and BFU2014-53978-R); and Agència de Gestió d'Ajuts Universitaris i de Recerca (SGR41635). G.G. and I.I. were supported by Investigator Research Fellowships (Agéncia de Gestió d'Ajuts Universitaris i de Recerca).
dc.format.mimetype application/pdf
dc.language.iso eng
dc.publisher Company of Biologists
dc.relation.ispartof J Cell Sci. 2017 Jan 15;130(2):490-501
dc.rights Published originally by Cold Spring Harbor Laboratory Press at 10.1242/jcs.193821. Beginning six months from the full-issue publication date, articles are distributed under the Creative Commons Attribution-Non-Commercial 4.0 International License (CC-BY-NC), as described at http://creativecommons.org/licenses/by-nc/4.0/. This license permits non-commercial use, including reproduction, adaptation, and distribution of the article provided the original author and source are credited.
dc.rights.uri http://creativecommons.org/licenses/by-nc/4.0/
dc.title Phosphorylation of filamin A regulates chemokine receptor CCR2 recycling
dc.type info:eu-repo/semantics/article
dc.identifier.doi http://dx.doi.org/10.1242/jcs.193821
dc.subject.keyword G-protein-coupled receptors
dc.subject.keyword Ccr2
dc.subject.keyword Filamin A
dc.subject.keyword Recycling
dc.relation.projectID info:eu-repo/grantAgreement/ES/3PN/BFU2011-30080
dc.relation.projectID info:eu-repo/grantAgreement/ES/1PE/BFU2014-53978-R
dc.rights.accessRights info:eu-repo/semantics/openAccess
dc.type.version info:eu-repo/semantics/publishedVersion


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