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Keywords :
Actins/metabolism; Animals; Calcium-Binding Proteins/physiology; Carrier Proteins/biosynthesis/genetics/physiology; Cell Line; Cell Membrane/metabolism/ultrastructure; DNA/genetics; Fibroblasts/metabolism/ultrastructure; Fluorescent Antibody Technique; Gene Expression; Immunoblotting; Microfilament Proteins/biosynthesis/genetics/physiology; Microscopy, Electron; Microscopy, Electron, Scanning; Microvilli/ultrastructure; Mutation; Transfection
Abstract :
[en] The function of villin, an actin-binding protein, has been investigated by transfecting fibroblasts with cloned human cDNAs encoding wild-type villin or functional villin domains. Synthesis of large amounts of villin induced the growth of numerous long microvilli on cell surfaces together with the redistribution of F-actin. These microvilli contained a cytoskeleton of F-actin, and their appearance was frequently accompanied by the disappearance of stress fibers. The complete villin gene sequence was required to exert its morphogenic effect. Villin lacking one actin-binding domain (113 amino acids), located at its carboxyterminal end, did not induce growth if microvilli or stress fiber disruption. Our results indicate that villin plays a key role in vivo in the morphogenesis of microvilli.
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