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INVITED REVIEW
1The Center for Cardiovascular Sciences, Albany Medical College, Albany, New York 12208; and 2Departments of Dermatology and Cell Biology, Emory University School of Medicine, and 3Graduate Program in Biochemistry, Cell and Developmental Biology, Emory University, Atlanta, Georgia 30322
VE-cadherin was first identified in the early 1990s and quickly emerged as an important endothelial cell adhesion molecule. The past decade of research has revealed key roles for VE-cadherin in vascular permeability and in the morphogenic events associated with vascular remodeling. The details of how VE-cadherin functions in adhesion became apparent with structure-function analysis of the cadherin extracellular domain and with the identification of the catenins, a series of cytoplasmic proteins that bind to the cadherin tail and mediate interactions between cadherins and the cytoskeleton. Whereas early work focused on the armadillo family proteins 
-catenin and plakoglobin, more recent investigations have identified p120-catenin (p120ctn) and a related group of armadillo family members as key binding partners for the cadherin tail. Furthermore, a series of new studies indicate a key role for p120ctn in regulating cadherin membrane trafficking in mammalian cells. These recent studies place p120ctn at the hub of a cadherin-catenin regulatory mechanism that controls cadherin plasma membrane levels in cells of both epithelial and endothelial origin.
endothelial cell; cytoskeleton; -catenin; p120ctn; cell adhesion; vascular endothelial cadherin
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