Filamin a binds to CCR2B and regulates its internalization

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dc.contributor.authorMinsaas, Lauraen_ZA
dc.contributor.authorPlanagumà, Jesúsen_ZA
dc.contributor.authorMadziva, Michaelen_ZA
dc.contributor.authorKrakstad, Beate Fen_ZA
dc.contributor.authorMasià-Balagué, Míriamen_ZA
dc.contributor.authorKatz, Arieh Aen_ZA
dc.contributor.authorAragay, Anna Men_ZA
dc.date.accessioned2016-01-02T05:07:38Z
dc.date.available2016-01-02T05:07:38Z
dc.date.issued2010en_ZA
dc.description.abstractThe 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.en_ZA
dc.identifier.apacitationMinsaas, L., Planagumà, J., Madziva, M., Krakstad, B. F., Masià-Balagué, M., Katz, A. A., & Aragay, A. M. (2010). Filamin a binds to CCR2B and regulates its internalization. <i>PLoS One</i>, http://hdl.handle.net/11427/16175en_ZA
dc.identifier.chicagocitationMinsaas, Laura, Jesús Planagumà, Michael Madziva, Beate F Krakstad, Míriam Masià-Balagué, Arieh A Katz, and Anna M Aragay "Filamin a binds to CCR2B and regulates its internalization." <i>PLoS One</i> (2010) http://hdl.handle.net/11427/16175en_ZA
dc.identifier.citationMinsaas, L., Planagumà, J., Madziva, M., Krakstad, B. F., Masià-Balagué, M., Katz, A. A., & Aragay, A. M. (2010). Filamin a binds to CCR2B and regulates its internalization. PLoS One, 5(8), e12212. doi:10.1371/journal.pone.0012212en_ZA
dc.identifier.ris TY - Journal Article AU - Minsaas, Laura AU - Planagumà, Jesús AU - Madziva, Michael AU - Krakstad, Beate F AU - Masià-Balagué, Míriam AU - Katz, Arieh A AU - Aragay, Anna M AB - 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. DA - 2010 DB - OpenUCT DO - 10.1371/journal.pone.0012212 DP - University of Cape Town J1 - PLoS One LK - https://open.uct.ac.za PB - University of Cape Town PY - 2010 T1 - Filamin a binds to CCR2B and regulates its internalization TI - Filamin a binds to CCR2B and regulates its internalization UR - http://hdl.handle.net/11427/16175 ER - en_ZA
dc.identifier.urihttp://hdl.handle.net/11427/16175
dc.identifier.urihttp://dx.doi.org/10.1371/journal.pone.0012212
dc.identifier.vancouvercitationMinsaas L, Planagumà J, Madziva M, Krakstad BF, Masià-Balagué M, Katz AA, et al. Filamin a binds to CCR2B and regulates its internalization. PLoS One. 2010; http://hdl.handle.net/11427/16175.en_ZA
dc.language.isoengen_ZA
dc.publisherPublic Library of Scienceen_ZA
dc.publisher.departmentDivision of Medical Biochemistryen_ZA
dc.publisher.facultyFaculty of Health Sciencesen_ZA
dc.publisher.institutionUniversity of Cape Town
dc.rightsThis is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.en_ZA
dc.rights.holder© 2010 Minsaas et alen_ZA
dc.rights.urihttp://creativecommons.org/licenses/by/4.0en_ZA
dc.sourcePLoS Oneen_ZA
dc.source.urihttp://journals.plos.org/plosoneen_ZA
dc.subject.otherCell membranesen_ZA
dc.subject.otherSmall interfering RNAsen_ZA
dc.subject.otherVesiclesen_ZA
dc.subject.otherActinsen_ZA
dc.subject.otherMembrane proteinsen_ZA
dc.subject.otherMembrane receptor signalingen_ZA
dc.subject.otherActin filamentsen_ZA
dc.subject.otherChemokinesen_ZA
dc.titleFilamin a binds to CCR2B and regulates its internalizationen_ZA
dc.typeJournal Articleen_ZA
uct.type.filetypeText
uct.type.filetypeImage
uct.type.publicationResearchen_ZA
uct.type.resourceArticleen_ZA
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