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From the structure to the function of villin, an actin‐binding protein of the brush border
Author(s) -
Friederich Evelync,
Pringault Eric,
Arpin Monique,
Louvard Daniel
Publication year - 1990
Publication title -
bioessays
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.175
H-Index - 184
eISSN - 1521-1878
pISSN - 0265-9247
DOI - 10.1002/bies.950120902
Subject(s) - villin , microbiology and biotechnology , brush border , actin , biology , chaperonin , morphogenesis , mutant , actin binding protein , actin cytoskeleton , cytoskeleton , biochemistry , cell , protein folding , gene , vesicle , membrane
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.