VIL1
Description
The VIL1 (villin 1) is a protein-coding gene located on chromosome 2.
Villin-1, also known as villin, is a calcium-regulated actin-binding protein that plays a crucial role in the organization and dynamics of microvillus actin filaments. It participates in actin nucleation, filament bundle assembly, capping, and severing, contributing to the dynamic remodeling of the actin cytoskeleton. Villin interacts with lipids like phosphatidylinositol 4,5-bisphosphate (PIP2) and lysophosphatidic acid (LPA), with a higher affinity for LPA. Binding to LPA promotes phosphorylation by SRC, leading to the inhibition of all actin-modifying activities. Conversely, PIP2 binding inhibits actin-capping and -severing but enhances actin-bundling activity. These interactions regulate a variety of cellular processes, including intestinal epithelial cell morphology, invasion, migration, and apoptosis. Villin protects against dextran sodium sulfate (DSS)-induced apoptosis in the gastrointestinal epithelium by preserving mitochondrial integrity. It also enhances hepatocyte growth factor (HGF)-induced epithelial cell motility, chemotaxis, and wound repair. Notably, during S.flexneri infection, villin's actin-severing activity promotes the actin-based motility of the bacteria, aiding in their dissemination.
VIL1 is also known as D2S1471, VIL.
