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J Biol Chem, Vol. 274, Issue 38, 26751-26760, September 17, 1999

Villin Function in the Organization of the Actin Cytoskeleton
CORRELATION OF IN VIVO EFFECTS TO ITS BIOCHEMICAL ACTIVITIES IN VITRO

Evelyne Friederich, Katia Vancompernolle^¶, Daniel Louvard, and Joël Vandekerckhove^¶

From the  Laboratoire de Morphogenèse et Signalisation Cellulaire, Centre National de la Recherche Scientifique, UMR 144, Institut Curie, 26, rue d'Ulm, Paris 75248 Cedex 05 France and the ^¶ V.I.B., Flanders Interuniversity Institute of Biotechnology (ViBO9), Department of Biochemistry, University of Ghent, B-9000 Ghent, Belgium

Villin is an actin-binding protein of the intestinal brush border that bundles, nucleates, caps, and severs actin in a Ca²⁺-dependent manner in vitro. Villin induces the growth of microvilli in transfected cells, an activity that requires a carboxyl-terminally located KKEK motif. By combining cell transfection and biochemical assays, we show that the capacity of villin to induce growth of microvilli in cells correlates with its ability to bundle F-actin in vitro but not with its nucleating activity. In agreement with its importance for microfilament bundling in cells, the KKEK motif of the carboxyl-terminal F-actin-binding site is crucial for bundling in vitro. In addition, substitutions of basic residues in a second site, located in the amino-terminal portion of villin, impaired its activity in cells and reduced its binding to F-actin in the absence of Ca²⁺ as well as its bundling and severing activities in vitro. Altogether, these findings suggest that villin participates in the organization and stabilization of the brush border core bundle but does not initiate its assembly by nucleation of actin filaments.

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Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.

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