ArticleThe Journal of cell biology1988
Sequence of human villin: a large duplicated domain homologous with other actin-severing proteins and a unique small carboxy-terminal domain related to villin specificity.
Article in The Journal of cell biology, 1988. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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Who cites it
35 citing papers in PubMed, 129 citations in OpenAlex.
- Development and characterization of 2-dimensional culture for buffalo intestinal cells.Cytotechnology · 2018Article
- Villin severing activity enhances actin-based motility in vivo.Molecular biology of the cell · 2007Article
- Arabidopsis VILLIN1 generates actin filament cables that are resistant to depolymerization.The Plant cell · 2005Article
- Regulation of cell motility by tyrosine phosphorylated villin.Molecular biology of the cell · 2004Article
- Tissue-engineered small intestine improves recovery after massive small bowel resection.Annals of surgery · 2004Article
- Solution structures of the C-terminal headpiece subdomains of human villin and advillin, evaluation of headpiece F-actin-binding requirements.Protein science : a publication of the Protein Society · 2004Article
- Villin enhances hepatocyte growth factor-induced actin cytoskeleton remodeling in epithelial cells.Molecular biology of the cell · 2003Article
- Actin and pollen tube growth.Protoplasma · 2001Review
- Villin-like actin-binding proteins are expressed ubiquitously in Arabidopsis.Plant physiology · 2000Article
- In vivo, villin is required for Ca(2+)-dependent F-actin disruption in intestinal brush borders.The Journal of cell biology · 1999Article
- Phototactic migration of Dictyostelium cells is linked to a new type of gelsolin-related protein.Molecular biology of the cell · 1999Article
- Gelsolin and functionally similar actin-binding proteins are regulated by lysophosphatidic acid.The EMBO journal · 1998Article
- Refined structure of villin 14T and a detailed comparison with other actin-severing domains.Protein science : a publication of the Protein Society · 1997Article
- Comparative FISH-mapping of villin (VIL) gene in river buffalo, sheep and goat chromosomes.Chromosome research : an international journal on the molecular, supramolecular and evolutionary aspects of chromosome biology · 1997Article
- Human fetal enterocytes in vitro: modulation of the phenotype by extracellular matrix.Proceedings of the National Academy of Sciences of the United States of America · 1996Article
- The actin binding site of thymosin beta 4 mapped by mutational analysis.The EMBO journal · 1996Article
- Suppression of villin expression by antisense RNA impairs brush border assembly in polarized epithelial intestinal cells.The EMBO journal · 1995Article
- Autoantibodies specific for villin found in patients with colon cancer and other colitides.Digestive diseases and sciences · 1995Article
- A gelsolin-related protein from lobster muscle: cloning, sequence analysis and expression.The Biochemical journal · 1995Article
- Identification of secreted and cytosolic gelsolin in Drosophila.The Journal of cell biology · 1994Article
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Villin is a calcium-regulated actin-binding protein that caps, severs, and bundles actin filaments in vitro. This 92,500-D protein is a major constituent of the actin bundles within the microvilli of the brush border surface of intestinal and kidney proximal tubule cells. Villin is a very early marker of cells involved in absorption and its expression is highly increased during intestinal cell differentiation. The amino acid sequence deduced from the cDNA sequence revealed that human villin is composed of three domains. The first two domains appear as the result of a duplication: their structural organization is similar. We can then define a basic unit in which a slightly hydrophilic motif is followed by three hydrophobic motifs, similar between themselves and regularly spaced. The duplicated domain is highly homologous to three other actin-severing proteins and this basic structure represents the whole molecule in severin and fragmin, while two basic units compose gelsolin. The third domain which is carboxy terminal is villin specific: it is unique among actin modulating proteins so far known. It could account for its actin-binding properties (dual regulation by calcium of severing and bundling activities). We propose that it may also be related to the subcellular localization of villin in different epithelial cell types.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.