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J. Biol. Chem., Vol. 279, Issue 31, 32858-32868, July 30, 2004

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Endoglin Regulates Cytoskeletal Organization through Binding to ZRP-1, a Member of the Lim Family of Proteins^*

Francisco Sanz-Rodriguez¶, Mercedes Guerrero-Esteo, Luisa-Maria Botella, Denis Banville||, Calvin P. H. Vary**, and Carmelo Bernabéu

From the Centro de Investigaciones Biológicas, CSIC, Ramiro de Maetzu 9, 28040 Madrid, Spain, ^||Biotechnology Research Institute, 6100 Royalmount, Montreal, Quebec H4P 2R2, Canada, and ^**Center for Molecular Medicine, Maine Medical Center Research Institute, Scarborough, Maine 04074

Endoglin is a component of the transforming growth factor- 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.

Received for publication, January 26, 2004 , and in revised form, May 14, 2004.

^* This work was supported by Ministerio de Ciencia y Tecnologia, Fondo de Investigación Sanitaria Grant PI020200, Comunidad Autonóma de Madrid (to C. B.), and National Center for Research Resources Grant P20 15555 from the National Institutes of Health. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Both authors contributed equally to this paper.

We regret the passing away of Dr. Banville on February 4th, 2004.

^¶ To whom correspondence should be addressed: Centro de Investigaciones Biológicas, CSIC, Ramiro de Maetzu 9, 28040 Madrid, Spain. Tel.: 34-91-8373112 (ext. 4246); Fax: 34-91-5360432; E-mail: francisco.sanz{at}uam.es.

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