Reference : From the structure to the function of villin, an actin-binding protein of the brush b...
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
From the structure to the function of villin, an actin-binding protein of the brush border.
Friederich, Evelyne mailto [University of Luxembourg > Faculty of Science, Technology and Communication (FSTC) > Life Science Research Unit >]
Pringault, E. [> >]
Arpin, M. [> >]
Louvard, D. [> >]
Yes (verified by ORBilu)
[en] Actins/metabolism ; Animals ; Carrier Proteins/chemistry/genetics/physiology ; Cells, Cultured ; Chick Embryo ; DNA/genetics ; Gene Expression Regulation ; Humans ; Intestinal Mucosa/growth & development/metabolism/ultrastructure ; Mice ; Microfilament Proteins/chemistry/genetics/physiology ; Microvilli/metabolism/ultrastructure ; Molecular Structure ; Organ Specificity ; Recombinant Proteins/metabolism
[en] Villin, a calcium-regulated actin-binding protein, modulates the structure and assembly of actin filaments in vitro. It is organized into three domains, the first two of which are homologous. Villin is mainly produced in epithelial cells that develop a brush border and which are responsible for nutrient uptake. Expression of the villin structural gene is precisely regulated during mouse embryogenesis and is restricted in adults, to certain epithelia of the gastrointestinal and urogenital tracts. The function of villin has been assessed by transfecting CV1 cells with a human cDNA encoding wild-type villin or mutant villin. Synthesis of large amounts of villin in cells which do not normally produce this protein induces the growth of microvilli on the cell surface and the redistribution of F-actin, concomitant with the disappearance of stress fibers. The complete villin sequence is required for the morphogenic effect. These results suggest that villin plays a key role in the morphogenesis of microvilli.

There is no file associated with this reference.

Bookmark and Share SFX Query

All documents in ORBilu are protected by a user license.