VIL1

This gene encodes a member of a family of calcium-regulated actin-binding proteins. This protein represents a dominant part of the brush border cytoskeleton which functions in the capping, severing, and bundling of actin filaments. Two mRNAs of 2.7 kb and 3.5 kb have been observed; they result from utilization of alternate poly-adenylation signals present in the terminal exon. [provided by RefSeq, Jul 2008]

Villin 1

Epithelial cell-specific Ca2+-regulated actin-modifying protein that modulates the reorganization of microvillar actin filaments. Plays a role in the actin nucleation, actin filament bundle assembly, actin filament capping and severing. Binds phosphatidylinositol 4,5-bisphosphate (PIP2) and lysophosphatidic acid (LPA); binds LPA with higher affinity than PIP2. Binding to LPA increases its phosphorylation by SRC and inhibits all actin-modifying activities. Binding to PIP2 inhibits actin-capping and -severing activities but enhances actin-bundling activity. Regulates the intestinal epithelial cell morphology, cell invasion, cell migration and apoptosis. Protects against apoptosis induced by dextran sodium sulfate (DSS) in the gastrointestinal epithelium. Appears to regulate cell death by maintaining mitochondrial integrity. Enhances hepatocyte growth factor (HGF)-induced epithelial cell motility, chemotaxis and wound repair. Upon S.flexneri cell infection, its actin-severing activity enhances actin-based motility of the bacteria and plays a role during the dissemination.

Biological Process actin filament capping Source:UniProtKB3 Publications
Biological Process actin filament depolymerization Source:UniProtKB1 Publication
Biological Process actin filament polymerization Source:UniProtKB1 Publication
Biological Process actin filament severing Source:UniProtKB3 Publications
Biological Process actin nucleation Source:InterPro
Biological Process actin polymerization or depolymerization Source:GO_Central1 Publication
Biological Process barbed-end actin filament capping Source:UniProtKB1 Publication
Biological Process cellular response to epidermal growth factor stimulus Source:UniProtKB1 Publication
Biological Process cellular response to hepatocyte growth factor stimulus Source:Ensembl
Biological Process cytoplasmic actin-based contraction involved in cell motility Source:UniProtKB1 Publication
Biological Process epidermal growth factor receptor signaling pathway Source:UniProtKB1 Publication
Biological Process epithelial cell differentiation Source:UniProtKB1 Publication
Biological Process intestinal D-glucose absorption Source:Ensembl
Biological Process positive regulation of actin filament bundle assembly Source:UniProtKB1 Publication
Biological Process positive regulation of actin filament depolymerization Source:UniProtKB1 Publication
Biological Process positive regulation of cell migration Source:UniProtKB1 Publication
Biological Process positive regulation of epithelial cell migration Source:UniProtKB1 Publication
Biological Process positive regulation of lamellipodium morphogenesis Source:UniProtKB1 Publication
Biological Process positive regulation of multicellular organism growth Source:Ensembl
Biological Process positive regulation of protein localization to plasma membrane Source:Ensembl
Biological Process protein-containing complex assembly Source:ProtInc1 Publication
Biological Process regulation of actin nucleation Source:UniProtKB3 Publications
Biological Process regulation of cell shape Source:UniProtKB1 Publication
Biological Process regulation of lamellipodium morphogenesis Source:UniProtKB
Biological Process regulation of microvillus length Source:Ensembl
Biological Process regulation of wound healing Source:UniProtKB
Biological Process response to bacterium Source:UniProtKB1 Publication
Biological Process terminal web assembly Source:Ensembl

Cytoplasm, cytoskeleton
Cell projection, lamellipodium
Cell projection, ruffle
Cell projection, microvillus
Cell projection, filopodium tip
Cell projection, filopodium
Relocalized in the tip of cellular protrusions and filipodial extensions upon infection with S.flexneri in primary intestinal epithelial cells (IEC) and in the tail-like structures forming the actin comets of S.flexneri. Redistributed to the leading edge of hepatocyte growth factor (HGF)-induced lamellipodia (By similarity).
Rapidly redistributed to ruffles and lamellipodia structures in response to autotaxin, lysophosphatidic acid (LPA) and epidermal growth factor (EGF) treatment

Biliary atresia is a chronic and progressive cholestatic liver disease of chilhood characterized by an abnormal villin gene expression and severe malformation of canalicular microvillus structure.

Tyrosine phosphorylation is induced by epidermal growth factor (EGF) and stimulates cell migration (By similarity).
Phosphorylated on tyrosine residues by SRC. The unphosphorylated form increases the initial rate of actin-nucleating activity, whereas the tyrosine-phosphorylated form inhibits actin-nucleating activity, enhances actin-bundling activity and enhances actin-severing activity by reducing high Ca2+ requirements. The tyrosine-phosphorylated form does not regulate actin-capping activity. Tyrosine phosphorylation is essential for cell migration: tyrosine phosphorylation sites in the N-terminus half regulate actin reorganization and cell morphology, whereas tyrosine phosphorylation sites in the C-terminus half regulate cell migration via interaction with PLCG1.