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FEBS Lett. 2008 Jun 18;582(14):2128-39. doi: 10.1016/j.febslet.2008.02.040. Epub 2008 Feb 26.

Regulation of cell structure and function by actin-binding proteins: villin's perspective.

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Department of Physiology, University of Tennessee Health Science Center, 894 Union Avenue, Nash 402, Memphis, TN 38163, United States.


Villin is a tissue-specific actin modifying protein that is associated with actin filaments in the microvilli and terminal web of epithelial cells. It belongs to a large family of actin-binding proteins which includes actin-capping, -nucleating and/or -severing proteins such as gelsolin, severin, fragmin, adseverin/scinderin and actin crosslinking proteins such as dematin and supervillin. Studies done in epithelial cell lines and villin knock-out mice have demonstrated the function of villin in regulating actin dynamics, cell morphology, epithelial-to-mesenchymal transition, cell migration and cell survival. In addition, the ligand-binding properties of villin (F-actin, G-actin, calcium, phospholipids and phospholipase C-gamma1) are mechanistically important for the crosstalk between signaling pathways and actin reorganization in epithelial cells.

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