Journal
FEBS JOURNAL
Volume 273, Issue 9, Pages 2000-2011Publisher
WILEY
DOI: 10.1111/j.1742-4658.2006.05216.x
Keywords
actin fiber; angiogenesis; angiostatin; migration; tight junction
Categories
Funding
- NCI NIH HHS [R01 CA60499, R01 CA089406, R01 CA089406-07A2] Funding Source: Medline
- NHLBI NIH HHS [R01 HL 64597] Funding Source: Medline
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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, Amot1-1 and Amot1-2, 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.
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