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The isolated intestinal microvillus cytoskeleton (core) consists of four major proteins: actin, villin, fimbrin, and brush border myosin-I. These proteins can assemble in vitro into structures resembling native microvillus cores. Of these components, villin, and brush border myosin-I show tissue-specific expression, so they may be involved in the morphogenesis of intestinal microvilli. Found in association with the microvillar actin bundles of the intestinal brush border, villin is a 95kDa protein composed of two very similar domains of approximately 44kDa each, the core, and a C-terminal domain of 8kDa, the headpiece. The core has been shown to contain villin's Ca2 regulated capping, nucleating, and severing activities, but it cannot induce the formation of microfilament bundles without the headpiece. Villin is a useful differentiation marker of early embryogenesis and may be useful in diagnosis and follow-up of colorectal cancers. It has been demonstrated that villin is necessary for both the cytoskeletal and membrane protein organization of a functional brush border.Immunofluorescence, Immunohistochemistry, Immunoprecipitation, Western Blotting
