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Sanz-Rodriguez, F. et al.

Sanz-Rodriguez, Guerrero-Esteo, Botella, Banville, Vary, Bernabéu,

Endoglin regulates cytoskeletal organization through binding to ZRP-1, a member of the Lim family of proteins.

Endoglin is a component of the transforming growth factor-beta 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.[1]

References

Endoglin regulates cytoskeletal organization through binding to ZRP-1, a member of the Lim family of proteins. Sanz-Rodriguez, F., Guerrero-Esteo, M., Botella, L.M., Banville, D., Vary, C.P., Bernabéu, C. J. Biol. Chem. (2004) [Pubmed]

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