title: p130-angiomotin associates to actin and controls endothelial cell shape.
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.
authors.affiliation: Department of Oncology-Pathology, Cancer Centre Karolinska Institute, Stockholm, Sweden.
authors.forename: Mira
authors.initials: M
authors.lastname: Ernkvist
authors.forename: Karin
authors.initials: K
authors.lastname: Aase
authors.forename: Chinwe
authors.initials: C
authors.lastname: Ukomadu
authors.forename: James
authors.initials: J
authors.lastname: Wohlschlegel
authors.forename: Ryan
authors.initials: R
authors.lastname: Blackman
authors.forename: Niina
authors.initials: N
authors.lastname: Veitonmäki
authors.forename: Anders
authors.initials: A
authors.lastname: Bratt
authors.forename: Anindya
authors.initials: A
authors.lastname: Dutta
authors.forename: Lars
authors.initials: L
authors.lastname: Holmgren
mesh_terms: D000199:Actins / Q000378:metabolism*; D017398:Alternative Splicing; D000595:Amino Acid Sequence; D000091082:Angiomotins; D043168:Angiostatins / Q000502:physiology; D000818:Animals; D002460:Cell Line; D002461:Cell Line, Transformed; D002465:Cell Movement / Q000502:physiology; D048430:Cell Shape / Q000502:physiology*; D042783:Endothelial Cells / Q000166:cytology* / Q000378:metabolism*; D004730:Endothelium, Vascular / Q000166:cytology / Q000378:metabolism; D006367:HeLa Cells; D006801:Humans; D036341:Intercellular Signaling Peptides and Proteins / Q000096:biosynthesis / Q000235:genetics / Q000378:metabolism* / Q000502:physiology; D008565:Membrane Proteins / Q000096:biosynthesis / Q000235:genetics / Q000378:metabolism* / Q000502:physiology; D051379:Mice; D018345:Mice, Knockout; D008840:Microfilament Proteins / Q000096:biosynthesis / Q000235:genetics / Q000378:metabolism / Q000502:physiology; D008969:Molecular Sequence Data; D020033:Protein Isoforms / Q000096:biosynthesis / Q000235:genetics / Q000378:metabolism / Q000502:physiology
chemical_list: C423985:AMOT protein, human; D000199:Actins; C511047:Amot protein, mouse; D000091082:Angiomotins; D036341:Intercellular Signaling Peptides and Proteins; D008565:Membrane Proteins; D008840:Microfilament Proteins; D020033:Protein Isoforms; D043168:Angiostatins