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Título: | Endoglin regulates cytoskeletal organization through binding to ZRP-1, a member of the LIM family of proteins |
Autor: | Sanz-Rodríguez, Francisco CSIC ORCID; Guerrero-Esteo, Mercedes CSIC; Botella, Luisa María CSIC ORCID ; Banville, Denis; Vary, Calvin P. H.; Bernabéu, Carmelo CSIC ORCID | Fecha de publicación: | 2004 | Editor: | American Society for Biochemistry and Molecular Biology | Citación: | Journal of Biological Chemistry 79:32858-32868(2004) | Resumen: | Endoglin is a component of the transforming growth factor-β receptor complex abundantly expressed at the surface of endothelial cells and plays an important role in cardiovascular development and vascular remodeling. By using the cytoplasmic domain of endoglin as a bait for screening protein interactors, we have identified ZRP-1 (zyxin-related protein 1), a 476-amino acid member that belongs to a family of LIM containing proteins that includes zyxin and lipoma-preferred partner. The endoglin interacting region was mapped within the three double zinc finger LIM domains of the ZRP-1 C terminus. Analysis of the subcellular distribution of ZRP-1 demonstrated that in the absence of endoglin, ZRP-1 mainly localizes to focal adhesion sites, whereas in the presence of endoglin ZRP-1 is found along actin stress fibers. Because the LIM family of proteins has been shown to associate with the actin cytoskeleton, we investigated the possibility of a regulatory role for endoglin with regard to this structure. Expression of endoglin resulted in a dramatic reorganization of the actin cytoskeleton. In the absence of endoglin, F-actin was localized to dense aggregates of bundles, whereas in the presence of endoglin, expressed in endothelial cells, F-actin was in stress fibers and colocalized with ZRP-1. Furthermore, small interfering RNA-mediated suppression of endoglin or ZRP-1, or clustering of endoglin in endothelial cells, led to mislocalization of F-actin fibers. These results suggest a regulatory role for endoglin, via its interaction with ZRP-1, in the actin cytoskeletal organization. | Descripción: | 11 p.-7 fig. | Versión del editor: | http://dx.doi.org/10.1074/jbc.M400843200 | URI: | http://hdl.handle.net/10261/73323 | DOI: | 10.1074/jbc.M400843200 | ISSN: | 0021-9258 | E-ISSN: | 1083-351X |
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J. Biol. Chem.-2004-Sanz-Rodriguez-32858-68.pdf | 1,11 MB | Adobe PDF | Visualizar/Abrir |
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