Regulation of cell structure and function by actin-binding proteins: villin's perspective |
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Authors: | Khurana Seema George Sudeep P |
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Affiliation: | Department of Physiology, University of Tennessee Health Science Center, 894 Union Avenue, Nash 402, Memphis, TN 38163, United States. skhurana@utmem.edu |
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Abstract: | 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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Keywords: | DSS, dextran sodium sulfate EMT, epithelial-to-mesenchymal transition FRET, fluorescence resonance energy transfer LPA, lysophosphatidic acid PH, pleckstrin homology PIP2, phosphatidylinositol 4,5-bisphosphate PLC-γ1, phospholipase C-gamma 1 SEYFP, super-enhanced yellowed fluorescent protein SH2, Src homology 2 VDAC, voltage-dependent anion channel |
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