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Gene Review

VIL1  -  villin 1

Gallus gallus

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High impact information on VIL1


Biological context of VIL1

  • The protein sequence of villin deduced from a single cDNA clone contains a conserved sequence that is repeated six times and is found in each domain of the villin core [4].
  • In addition, chemical shift changes for residues Lys70-Phe76 in the C-terminal subdomain suggest that the HP67 actin binding site is disrupted upon unfolding of the N-terminal subdomain, providing a potential mechanism for regulating the villin-dependent bundling of actin filaments [5].
  • Calcium-binding proteins of this system include intestinal calcium binding protein (CaBP), calmodulin (CaM), villin, and a 36,000-mol-wt protein substrate of tyrosine kinases [6].
  • Gel-sol transformation of actin filaments, a process essential for cell motility, can be reconstituted in vitro and regulated in a predictable fashion by the combined action of villin and filamin [7].
  • We have investigated the structure, equilibria, and folding kinetics of an engineered 35-residue subdomain of the chicken villin headpiece, an ultrafast-folding protein [8].

Anatomical context of VIL1

  • Six are contained in the amino-terminal Mr 87,000 villin core, a Ca2+-regulated actin-severing fragment, whereas the carboxyl-terminal domain includes the villin "headpiece," a fragment involved in bundling of actin filaments [4].
  • Villin, a Ca2+-modulated F-actin-binding protein (95,000 daltons) present in microvillus core filament bundles, has been shown to contain multiple Ca2+-binding sites [9].
  • The headpiece domain of villin, a protein found in the actin bundles of the brush border epithelium, is of interest both as a compact F-actin binding domain and as a model folded protein [10].
  • Villin is a member of a family of actin-severing proteins that regulate the organization of actin in the eukaryotic cytoskeleton [11].
  • This study would suggest that as the Ca++ rises in the intestinal epithelial cell an ordered sequence of Ca++ saturation of intracellular receptors occurs with the order from the lowest to highest Ca++ requirements being CaBP less than CaM less than villin less than P-36 [6].

Associations of VIL1 with chemical compounds

  • Protein sequence analysis documents that the core comprises the NH2-terminal portion of intact villin, whereas the headpiece covers the COOH-terminal 76 amino acids [12].
  • The contribution of interactions involving the imidazole ring of His41 to the pH-dependent stability of the villin headpiece (HP67) N-terminal subdomain has been investigated by nuclear magnetic resonance (NMR) spin relaxation [5].
  • In reconstitution experiments, actin filaments incubated in EGTA with purified fimbrin and villin form smooth-sided bundles containing an apparently random number of filaments [13].
  • Maps constructed from the cleavage pattern suggest that villin contains six cysteine residues, two located in its amino-terminal peptide of Mr 44,000, and four located in the carboxyl-terminal peptide of Mr 51,000 [14].
  • Peptide antisera specific for either the amino- or carboxyl-terminal regions of villin were used to locate the position of cysteine residues in immunoblots of villin cleaved with 2-nitro-5-thiocyanobenzoic acid [14].

Regulatory relationships of VIL1

  • Villin inhibits filamin-induced F-actin gelation, but the effect can be overcome by increasing the amount of filamin [7].

Other interactions of VIL1

  • Moreover a significant within-sire effect of VIL1, a marker gene for NRAMP1, was observed in 117 progeny resulting from 25 informative matings [15].
  • Actin, villin, myosin, tropomyosin and spectrin, but not myosin I (previously called 110 kD; see Mooseker and Coleman, J. Cell Biol. 108, 2395-2400, 1989) are already concentrated in the luminal cytoplasm of crypt cells, as seen by immunofluorescence [16].
  • Sedimentation assays show that villin does not inhibit gelation of actin by preventing filamin from binding to F-actin [7].

Analytical, diagnostic and therapeutic context of VIL1

  • Using quantitative densitometry of cDNA-hybridized RNA blots from cells isolated from crypts, villus middle (mid), or villus tip (tip), we found a 2- to 3-fold increase in villin, calmodulin and tropomyosin steady-state mRNA levels; an increase parallel to morphological brush border development [16].
  • The physical structure of villin, a Ca2+-modulated regulator protein of actin filament organization, has been studied in the absence and presence of Ca2+ using analytical ultracentrifugation, gel chromatography, ultraviolet difference spectroscopy, and circular dichroism [17].
  • A procedure is described for the immobilization of monomeric actin so that about 30% of the immobilized protein is competent to bind the monomeric-actin-binding proteins bovine pancreatic deoxyribonuclease I and chicken villin [18].
  • Villin, a 95,000 dalton polypeptide of intestinal brush border which is known to bundle or sever actin filaments in a Ca++-dependent manner, was localized in rat and chicken intestinal epithelium by means of immunocytochemistry at the light- and electron-microscopic levels [19].
  • PvuII PCR polymorphism at the chicken VIL locus [20].


  1. F actin assembly modulated by villin: Ca++-dependent nucleation and capping of the barbed end. Glenney, J.R., Kaulfus, P., Weber, K. Cell (1981) [Pubmed]
  2. Regulation of actin polymerization by villin, a 95,000 dalton cytoskeletal component of intestinal brush borders. Craig, S.W., Powell, L.D. Cell (1980) [Pubmed]
  3. Role of fimbrin and villin in determining the interfilament distances of actin bundles. Matsudaira, P., Mandelkow, E., Renner, W., Hesterberg, L.K., Weber, K. Nature (1983) [Pubmed]
  4. Villin sequence and peptide map identify six homologous domains. Bazari, W.L., Matsudaira, P., Wallek, M., Smeal, T., Jakes, R., Ahmed, Y. Proc. Natl. Acad. Sci. U.S.A. (1988) [Pubmed]
  5. Characterizing a partially folded intermediate of the villin headpiece domain under non-denaturing conditions: contribution of His41 to the pH-dependent stability of the N-terminal subdomain. Grey, M.J., Tang, Y., Alexov, E., McKnight, C.J., Raleigh, D.P., Palmer, A.G. J. Mol. Biol. (2006) [Pubmed]
  6. Comparison of Ca++-regulated events in the intestinal brush border. Glenney, J.R., Glenney, P. J. Cell Biol. (1985) [Pubmed]
  7. Reconstitution and regulation of actin gel-sol transformation with purified filamin and villin. Nunnally, M.H., Powell, L.D., Craig, S.W. J. Biol. Chem. (1981) [Pubmed]
  8. Sub-microsecond protein folding. Kubelka, J., Chiu, T.K., Davies, D.R., Eaton, W.A., Hofrichter, J. J. Mol. Biol. (2006) [Pubmed]
  9. Demonstration of three distinct calcium-binding sites in villin, a modulator of actin assembly. Hesterberg, L.K., Weber, K. J. Biol. Chem. (1983) [Pubmed]
  10. High-resolution crystal structures of villin headpiece and mutants with reduced F-actin binding activity. Meng, J., Vardar, D., Wang, Y., Guo, H.C., Head, J.F., McKnight, C.J. Biochemistry (2005) [Pubmed]
  11. Solution structure of villin 14T, a domain conserved among actin-severing proteins. Markus, M.A., Nakayama, T., Matsudaira, P., Wagner, G. Protein Sci. (1994) [Pubmed]
  12. Demonstration of at least two different actin-binding sites in villin, a calcium-regulated modulator of F-actin organization. Glenney, J.R., Geisler, N., Kaulfus, P., Weber, K. J. Biol. Chem. (1981) [Pubmed]
  13. Reassociation of microvillar core proteins: making a microvillar core in vitro. Coluccio, L.M., Bretscher, A. J. Cell Biol. (1989) [Pubmed]
  14. Mapping the cysteine residues and actin-binding regions of villin by using antisera to the amino and carboxyl termini of the molecule. Matsudaira, P., Jakes, R., Cameron, L., Atherton, E. Proc. Natl. Acad. Sci. U.S.A. (1985) [Pubmed]
  15. Heritability of susceptibility to Salmonella enteritidis infection in fowls and test of the role of the chromosome carrying the NRAMP1 gene. Girard-Santosuosso, O., Lantier, F., Lantier, I., Bumstead, N., Elsen, J.M., Beaumont, C. Genet. Sel. Evol. (2002) [Pubmed]
  16. Cytoskeletal protein and mRNA accumulation during brush border formation in adult chicken enterocytes. Fath, K.R., Obenauf, S.D., Burgess, D.R. Development (1990) [Pubmed]
  17. Ligand-induced conformational changes in villin, a calcium-controlled actin-modulating protein. Hesterberg, L.K., Weber, K. J. Biol. Chem. (1983) [Pubmed]
  18. Preparation of immobilized monomeric actin and its use in the isolation of protease-free and ribonuclease-free pancreatic deoxyribonuclease I. Nefsky, B., Bretscher, A. Eur. J. Biochem. (1989) [Pubmed]
  19. Evidence for the association of villin with core filaments and rootlets of intestinal epithelial microvilli. Drenckhahn, D., Hofmann, H.D., Mannherz, H.G. Cell Tissue Res. (1983) [Pubmed]
  20. PvuII PCR polymorphism at the chicken VIL locus. Girard-Santosuosso, O., Lantier, I., Millet, N., Mouline, C., Guillot, J.F., Protais, J., Colin, P., Beaumont, C., Lantier, F. Anim. Genet. (1996) [Pubmed]
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