High impact information on VIL1

• Supervillin (p205): A novel membrane-associated, F-actin-binding protein in the villin/gelsolin superfamily [1].
• Calcium control of microfilaments: uncoupling of the F-actin-severing and -bundling activity of villin by limited proteolysis in vitro [2].
• The other two fragments' NH2-terminal sequencing showed a similar homology to the amino acid sequences of gelsolin and villin [3].
• Twelve amino acids of the Mr 39,000 fragment were sequenced from the NH2 terminus; the sequence of this part had a homology to the hinge region between segments 3 and 4 of gelsolin and villin [4].
• The intestinal epithelial nature of the cells was affirmed by the presence of villin on their luminal surface [5].

Biological context of VIL1

• The sequence homology and similar functional domain structure suggest a common structural basis for the calcium- and phospholipid-regulated actin-severing properties shared by adseverin, gelsolin, and villin [4].
• These chromosomes and chromosome bands are believed to be homologous and the VIL locus is the same as that previously found on cattle chromosome 2q43 [6].

Anatomical context of VIL1

• The presence of villin, which has so far been demonstrated only in intestinal and kidney brush border, was further confirmed by antibody staining of blotted electrophoresis gels of whole acinar cell extracts [7].
• To extend our recent observation that villin mRNA, encoding an apical microvillous protein, is dichotomously localized in the basal region of human enterocytes, we examined the localization of mRNAs for brush border myosin I (BBMI) and intestinal fimbrin (I-fim) [8].

Associations of VIL1 with chemical compounds

• Nucleotide and amino acid sequence analysis indicate that scinderin has six domains each containing three internal sequence motifs, two actin and two PIP2 binding sites and has 63 and 53% homology with gelsolin and villin [9].

Other interactions of VIL1

• The COOH terminus exhibits a striking similarity to villin and gelsolin, particularly in regions known to bind F-actin [1].

Analytical, diagnostic and therapeutic context of VIL1

• Two genomic clones of the villin (VIL) gene were independently hybridized on river buffalo (Bubalus bubalis, BBU), sheep (Ovis aries, OAR) and goat (Capra hircus, CHI) chromosomes by using sequential fluorescence in situ hybridization (FISH) and R-banding (RBP- and RBA-banding) [6].

References