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Article
Ena/VASP is required for endothelial barrier function in vivo
Science
  • Craig Furman, Massachusetts Institute of Technology
  • Alisha L. Sieminski, Franklin W. Olin College of Engineering
  • Adam V. Kwiatkowski, Massachusetts Institute of Technology
  • Douglas A. Rubinson, Massachusetts Institute of Technology
  • Eliza Vasile, Massachusetts Institute of Technology
  • Roderick T. Bronson, Harvard Medical School
  • Reinhard Fassler, Max Planck Institute for Biochemistry, Germany
Document Type
Article
Publication Date
11-1-2007
Abstract

Enabled/vasodilator-stimulated phosphoprotein (Ena/VASP) proteins are key actin regulators that localize at regions of dynamic actin remodeling, including cellular protrusions and cell-cell and cell-matrix junctions. Several studies have suggested that Ena/VASP proteins are involved in the formation and function of cellular junctions. Here, we establish the importance of Ena/VASP in endothelial junctions in vivo by analysis of Ena/VASP-deficient animals. In the absence of Ena/VASP, the vasculature exhibits patterning defects and lacks structural integrity, leading to edema, hemorrhaging, and late stage embryonic lethality. In endothelial cells, we find that Ena/VASP activity is required for normal F-actin content, actomyosin contractility, and proper response to shear stress. These findings demonstrate that Ena/VASP is critical for actin cytoskeleton remodeling events involved in the maintenance of functional endothelia.

Comments

© Alisha Sieminski, 2007. The article appeared in the Journal of Cell Biology, vol. 179, iss. 4, p. 761-775.

Citation Information
Craig Furman, Alisha L. Sieminski, Adam V. Kwiatkowski, Douglas A. Rubinson, et al.. "Ena/VASP is required for endothelial barrier function in vivo" (2007)
Available at: http://works.bepress.com/alisha_sarang-sieminski/1/