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Regulation of cell structure and function by actin‐binding proteins: Villin's perspective
Author(s) -
Khurana Seema,
George Sudeep P.
Publication year - 2008
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2008.02.040
Subject(s) - villin , gelsolin , microbiology and biotechnology , actin binding protein , actin , actin remodeling of neurons , chemistry , actin remodeling , fascin , actin cytoskeleton , biology , cell , cytoskeleton , biochemistry
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‐γ 1 ) are mechanistically important for the crosstalk between signaling pathways and actin reorganization in epithelial cells.