VE-cadherin: adhesion at arm's length |
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Authors: | Vincent Peter A Xiao Kanyan Buckley Kathleen M Kowalczyk Andrew P |
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Institution: | Dept. of Dermatology, Emory Univ. School of Medicine, Woodruff Memorial Bldg., 1639 Pierce Drive, Atlanta, GA 30322, USA. akowalc@emory.edu |
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Abstract: | 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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