Anti-Villin/VIL1 Antibody Picoband® Fluoro647 Conjugated

Villin is known as 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. In vertebrates, the villin proteins help to support the microfilaments of the microvilli of the brush border. It may play a role in cell plasticity through F-actin severing.

Specifically expressed in epithelial cells. Major component of microvilli of intestinal epithelial cells and kidney proximal tubule cells. Expressed in canalicular microvilli of hepatocytes (at protein level) . .

Epithelial cell-specific Ca (2+) -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. .

1. Friederich, E; Vancompernolle, K; Louvard, D; Vandekerckhove, J (1999) . Villin function in the organization of the actin cytoskeleton. Correlation of in vivo effects to its biochemical activities in vitro. The Journal of Biological Chemistry274 (38) : 26751–60. 2. Meng, J; Vardar, D; Wang, Y; Guo, HC; Head, JF; McKnight, CJ (2005) . High-resolution crystal structures of villin headpiece and mutants with reduced F-actin binding activity. Biochemistry 44 (36) : 11963–73.

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. .