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MBC in Press, published online ahead of print August 22, 2003
Mol. Biol. Cell 10.1091/mbc.E03-02-0091

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Submitted on February 19, 2003
Revised on June 23, 2003
Accepted on June 25, 2003

Villin enhances HGF-induced actin cytoskeleton remodeling in epithelial cells

Rafika Athman1, Daniel Louvard1, and Sylvie Robine1*

1 Laboratoire de morphogenèse et signalisation cellulaires, Institut Curie UMR 144, 26 rue d'Ulm 75248 Paris cedex 05, France

* Corresponding author. E-mail address: sylvie.robine{at}curie.fr.

Villin is an actin binding protein localized to intestinal and kidney brush borders. In vitro, villin has been demonstrated to bundle and sever F-actin in a calcium dependent manner. While villin is not necessary for the bundling of F-actin in vivo, it is important for the reorganization of the actin cytoskeleton elicited by stress during both physiological and pathological conditions (Ferrary et al., 1999). These data suggest that villin may be involved in actin cytoskeleton remodeling necessary for many processes requiring cellular plasticity. Here we study the role of villin in Hepatocyte Growth Factor (HGF)-induced epithelial cell motility and morphogenesis. For this purpose, we used primary cultures of enterocytes derived from vil+/+ and vil-/- mice and MDCK cells, expressing villin in an inducible manner. In vitro, we show that epithelial cell lysates from villin-expressing cells induced dramatic, calcium-dependent severing of actin filaments. In cell culture, we found that villin-expressing cells exhibit enhanced cell motility and morphogenesis upon HGF stimulation. In addition, we show that the ability of villin to potentiate HGF-induced actin reorganization occurs through the HGF-activated Phospholipase C{gamma} (PLC{gamma}) signaling pathway. Collectively, these data demonstrate that villin acts as a regulator of HGF-induced actin dynamics.




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