VIL1
VIL1 (villin 1, also known as villin, VIL or D2S1471) is an epithelial cell-specific, calcium-regulated actin-modifying protein. It reorganises microvillar actin filaments and is a dominant component of the brush border cytoskeleton. Browse Assay Genie's current range of VIL1 research reagents below, or read on for the biology behind the target.
VIL1 modulates the reorganisation of actin filaments in microvilli. It contributes to actin nucleation, actin filament bundle assembly, filament capping and severing. These activities are regulated by calcium and by lipid binding: VIL1 binds phosphatidylinositol 4,5-bisphosphate (PIP2) and lysophosphatidic acid (LPA), with higher affinity for LPA. PIP2 binding inhibits capping and severing but enhances bundling, whereas LPA binding inhibits all actin-modifying activities and increases phosphorylation of the protein by SRC.
Beyond cytoskeletal organisation, VIL1 regulates intestinal epithelial cell morphology, invasion, migration and apoptosis. It protects the gastrointestinal epithelium against apoptosis induced by dextran sodium sulfate (DSS) and appears to regulate cell death by maintaining mitochondrial integrity. It also enhances hepatocyte growth factor (HGF)-induced epithelial cell motility, chemotaxis and wound repair. During S. flexneri infection, its actin-severing activity enhances actin-based motility of the bacteria and contributes to their dissemination.
The VIL1 gene belongs to the villin/gelsolin family of calcium-regulated actin-binding proteins, and HGNC places it in the gelsolin/villins group. Two mRNAs of 2.7 kb and 3.5 kb have been observed, arising from alternate polyadenylation signals in the terminal exon. In UniProt the protein localises to the cytoskeleton and to cell projections including microvilli, lamellipodia, ruffles and filopodia. The mouse ortholog is Vil1.
VIL1 is a dominant part of the brush border cytoskeleton, making it a core target for studying microvillar actin organisation.
Its capping, severing, bundling and nucleation activities, controlled by calcium, PIP2 and LPA, make VIL1 a model for regulated actin remodelling.
VIL1 influences intestinal epithelial morphology, migration, invasion and apoptosis, including protection against DSS-induced injury.
VIL1 enhances HGF-induced motility and wound repair, and its severing activity promotes S. flexneri actin-based motility and dissemination.
VIL1 is a calcium-regulated actin-modifying protein specific to epithelial cells. It takes part in actin nucleation, filament bundling, capping and severing, and so reorganises microvillar actin. It also regulates epithelial cell morphology, migration, invasion and apoptosis, and appears to maintain mitochondrial integrity.
The HGNC-approved name is villin 1, and the UniProt protein name is Villin-1. The gene is also known as VIL and D2S1471. Two mRNAs of 2.7 kb and 3.5 kb result from alternate polyadenylation signals in the terminal exon.
VIL1 has a mouse ortholog, Vil1. In the UniProt annotation, villin protects the gastrointestinal epithelium against DSS-induced apoptosis and promotes S. flexneri dissemination through its actin-severing activity. Check the datasheet of any product for its validated reactivity.
Other villin/gelsolin family proteins, actin-regulating factors and epithelial signalling targets with products at Assay Genie.
Gene and protein annotations from HGNC, NCBI Gene and UniProt P09327; product specifications from Assay Genie datasheets.