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| Título: | Filamin a binds to CCR2B and regulates its internalization |
Autor: | Masià-Balagué, Miriam CSIC; Aragay, Anna M. CSIC ORCID | Fecha de publicación: | 17-ago-2010 | Editor: | Public Library of Science | Citación: | PLoS ONE 5(8): e12212 (2010) | Resumen: | The chemokine (C-C motif) receptor 2B (CCR2B) is one of the two isoforms of the receptor for monocyte chemoattractant protein-1 (CCL2), the major chemoattractant for monocytes, involved in an array of chronic inflammatory diseases. Employing the yeast two-hybrid system, we identified the actin-binding protein filamin A (FLNa) as a protein that associates with the carboxyl-terminal tail of CCR2B. Co-immunoprecipitation experiments and in vitro pull down assays demonstrated that FLNa binds constitutively to CCR2B. The colocalization of endogenous CCR2B and filamin A was detected at the surface and in internalized vesicles of THP-1 cells. In addition, CCR2B and FLNa were colocalized in lamellipodia structures of CCR2B-expressing A7 cells. Expression of the receptor in filamin-deficient M2 cells together with siRNA experiments knocking down FLNa in HEK293 cells, demonstrated that lack of FLNa delays the internalization of the receptor. Furthermore, depletion of FLNa in THP-1 monocytes by RNA interference reduced the migration of cells in response to MCP-1. Therefore, FLNa emerges as an important protein for controlling the internalization and spatial localization of the CCR2B receptor in different dynamic membrane structures. | Descripción: | et al. | Versión del editor: | http://dx.doi.org/10.1371/journal.pone.0012212 | URI: | http://hdl.handle.net/10261/44384 | DOI: | 10.1371/journal.pone.0012212 | ISSN: | 1932-6203 |
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| Filamin a binds.pdf | 3,86 MB | Adobe PDF |  Visualizar/Abrir |
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