p130-angiomotin associates to actin and controls endothelial cell shape.

Angiomotin, an 80 kDa protein expressed in endothelial cells, promotes cell migration and invasion, and stabilizes tube formation in vitro. Angiomotin belongs to a new protein family with two additional members, Amotl-1 and Amotl-2, which are characterized by conserved coiled-coil domains and C-terminal PDZ binding motifs. Here, we report the identification of a 130 kDa splice isoform of angiomotin that is expressed in different cell types including vascular endothelial cells, as well as cytotrophoblasts of the placenta.

Angiomotin expression promotes hemangioendothelioma invasion.

Angiomotin was identified by its ability to bind angiostatin and has been shown to mediate its activity in vitro. The family of angiomotin-like protein consists of three members that have coiled-coil domains and conserved c-terminal PDZ-binding motifs. We show here that expression of angiomotin in mouse aortic endothelial (MAE) cells results in stabilization of tubes in the Matrigel assay.