Reference : Villin induces microvilli growth and actin redistribution in transfected fibroblasts. |
Scientific journals : Article | |||
Life sciences : Biochemistry, biophysics & molecular biology | |||
http://hdl.handle.net/10993/6295 | |||
Villin induces microvilli growth and actin redistribution in transfected fibroblasts. | |
English | |
Friederich, Evelyne ![]() | |
Huet, C. [> >] | |
Arpin, M. [> >] | |
Louvard, D. [> >] | |
1989 | |
Cell | |
59 | |
3 | |
461-75 | |
Yes (verified by ORBilu) | |
International | |
0092-8674 | |
UNITED STATES | |
[en] 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 | |
[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. | |
http://hdl.handle.net/10993/6295 |
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