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Am J Physiol Cell Physiol. 2004 May;286(5):C987-97.

VE-cadherin: adhesion at arm's length.

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  • 1Dept. of Dermatology, Emory Univ. School of Medicine, Woodruff Memorial Bldg., 1639 Pierce Drive, Atlanta, GA 30322, USA. akowalc@emory.edu

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 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.

PMID:
15075197
[PubMed - indexed for MEDLINE]
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