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VE-cadherin: adhesion at arm s length Vincent PA; Xiao K; Buckley KM; Kowalczyk APAm J Physiol Cell Physiol 2004[May]; 286 (5): C987-97VE-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 beta-catenin and plakoglobin, more recent investigations have identified p120-catenin (p120(ctn)) 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 p120(ctn) in regulating cadherin membrane trafficking in mammalian cells. These recent studies place p120(ctn) at the hub of a cadherin-catenin regulatory mechanism that controls cadherin plasma membrane levels in cells of both epithelial and endothelial origin.|Animals[MESH]|Antigens, CD[MESH]|Cadherins/metabolism/*physiology[MESH]|Cell Adhesion[MESH]|Cytoskeletal Proteins/metabolism[MESH]|Endothelium, Vascular/cytology/*physiology[MESH]|Humans[MESH]|Models, Biological[MESH]|Signal Transduction/physiology[MESH] |
