InterPro domain: IPR030010

Villin belongs to the villin/gelsolin family, whose members are actin-modulating proteins that sever F-actin, cap the barbed ends of actin filaments preventing monomer exchange, and promote the nucleation step of actin polymerisation [ 1 ]. Villin is involved in actin remodelling necessary for many cellular processes requiring the actin cytoskeleton plasticity [ 2 , 3 ].

This entry represents villin-1 (VLN1) from plants, including AtVLN1 (At2g29890) from Arabidopsis [ 4 ]. Arabidopsis contains at least five villin-like genes (AtVLNs) encoding five different VLN isoforms. AtVLN1 bundles actin filaments [ 5 ]. However, unlike human plasma gelsolin, AtVLN1 does not nucleate actin filaments, does not block the polymerisation of profilin-actin onto barbed ends, and does not sever pre-existing filaments [ 6 ].

1. Villin severing activity enhances actin-based motility in vivo. Mol. Biol. Cell 18, 827-38
2. The epithelial cell cytoskeleton and intracellular trafficking. III. How is villin involved in the actin cytoskeleton dynamics in intestinal cells? Am. J. Physiol. Gastrointest. Liver Physiol. 283, G496-502
3. Regulation of cell structure and function by actin-binding proteins: villin's perspective. FEBS Lett. 582, 2128-39
4. Villin-like actin-binding proteins are expressed ubiquitously in Arabidopsis. Plant Physiol. 122, 35-48
5. Arabidopsis VILLIN1 generates actin filament cables that are resistant to depolymerization. Plant Cell 17, 486-501