From the structure to the function of villin, an actin-binding protein of the brush border

Bioessays. 1990 Sep;12(9):403-8. doi: 10.1002/bies.950120902.


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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Actins / metabolism*
  • Animals
  • Carrier Proteins / chemistry
  • Carrier Proteins / genetics
  • Carrier Proteins / physiology*
  • Cells, Cultured
  • Chick Embryo
  • DNA / genetics
  • Gene Expression Regulation
  • Humans
  • Intestinal Mucosa / growth & development
  • Intestinal Mucosa / metabolism
  • Intestinal Mucosa / ultrastructure
  • Mice
  • Microfilament Proteins / chemistry
  • Microfilament Proteins / genetics
  • Microfilament Proteins / physiology*
  • Microvilli / metabolism*
  • Microvilli / ultrastructure
  • Molecular Structure
  • Organ Specificity
  • Recombinant Proteins / metabolism


  • Actins
  • Carrier Proteins
  • Microfilament Proteins
  • Recombinant Proteins
  • villin
  • DNA