p130-angiomotin associates to actin and controls endothelial cell shape

FEBS J. 2006 May;273(9):2000-11. doi: 10.1111/j.1742-4658.2006.05216.x.

Abstract

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.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Actins / metabolism*
  • Alternative Splicing
  • Amino Acid Sequence
  • Angiomotins
  • Angiostatins / physiology
  • Animals
  • Cell Line
  • Cell Line, Transformed
  • Cell Movement / physiology
  • Cell Shape / physiology*
  • Endothelial Cells / cytology*
  • Endothelial Cells / metabolism*
  • Endothelium, Vascular / cytology
  • Endothelium, Vascular / metabolism
  • HeLa Cells
  • Humans
  • Intercellular Signaling Peptides and Proteins / biosynthesis
  • Intercellular Signaling Peptides and Proteins / genetics
  • Intercellular Signaling Peptides and Proteins / metabolism*
  • Intercellular Signaling Peptides and Proteins / physiology
  • Membrane Proteins / biosynthesis
  • Membrane Proteins / genetics
  • Membrane Proteins / metabolism*
  • Membrane Proteins / physiology
  • Mice
  • Mice, Knockout
  • Microfilament Proteins / biosynthesis
  • Microfilament Proteins / genetics
  • Microfilament Proteins / metabolism
  • Microfilament Proteins / physiology
  • Molecular Sequence Data
  • Protein Isoforms / biosynthesis
  • Protein Isoforms / genetics
  • Protein Isoforms / metabolism
  • Protein Isoforms / physiology

Substances

  • AMOT protein, human
  • Actins
  • Amot protein, mouse
  • Angiomotins
  • Intercellular Signaling Peptides and Proteins
  • Membrane Proteins
  • Microfilament Proteins
  • Protein Isoforms
  • Angiostatins

Associated data

  • GENBANK/AY987378