InterPro domain: IPR044155

Villin is an actin-binding protein that is found in a variety of tissues. It is able to bind to the barbed end of actin filaments with high affinity and can sever filaments [ 1 ]. In addition, villin's activity is important for actin bundling in certain cell types [ 2 ]. It was first isolated as a major component of the core of intestinal microvilli [ 3 ].

Five villin proteins (Villin1-5) coexist in Arabidopsis. This entry represents the Villin-3 family. It has been shown that Villin-1 and Villin-3 have distinct and overlapping functions in formation and turnover of actin filament bundles [ 4 ]. While Villin-2 and Villin3 act redundantly to regulate cell elongation and directional organ growth [ 5 ] through bundling of actin filament [ 6 ].

1. Different calcium dependence of the capping and cutting activities of villin. J. Biol. Chem. 261, 9274-81
2. From the structure to the function of villin, an actin-binding protein of the brush border. Bioessays 12, 403-8
3. Villin: the major microfilament-associated protein of the intestinal microvillus. Proc. Natl. Acad. Sci. U.S.A. 76, 2321-5
4. Arabidopsis VILLIN1 and VILLIN3 have overlapping and distinct activities in actin bundle formation and turnover. Plant Cell 22, 2727-48
5. Arabidopsis VILLIN2 and VILLIN3 are required for the generation of thick actin filament bundles and for directional organ growth. Plant Physiol. 158, 1426-38
6. Arabidopsis VILLIN2 and VILLIN3 act redundantly in sclerenchyma development via bundling of actin filaments. Plant J. 71, 962-75