p130-Angiomotin associates to actin and controls endothelial cell shape

Academic Article


  • 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. p130-Angiomotin consists of a cytoplasmic N-terminal extension that mediates its association with F-actin. Transfection of p130-angiomotin into endothelial cells induces actin fiber formation and changes cell shape. The p130-angiomotin protein remained associated with actin after destabilization of actin fibers with cytochalasin B. In contrast to p80-angiomotin, p130-angiomotin does not promote cell migration and did not respond to angiostatin. We propose that p80- and p130-angiomotin play coordinating roles in tube formation by affecting cell migration and cell shape, respectively. ¬© 2006 The Authors.
  • Authors

    Digital Object Identifier (doi)

    Author List

  • Ernkvist M; Aase K; Ukomadu C; Wohlschlegel J; Blackman R; Veitonm√§ki N; Bratt A; Dutta A; Holmgren L
  • Start Page

  • 2000
  • End Page

  • 2011
  • Volume

  • 273
  • Issue

  • 9