VE-cadherin: adhesion at arm's length.
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.
Vincent
Peter A
PA
Dept. of Dermatology, Emory Univ. School of Medicine, Woodruff Memorial Bldg., 1639 Pierce Drive, Atlanta, GA 30322, USA. akowalc@emory.edu
Xiao
Kanyan
K
Buckley
Kathleen M
KM
Kowalczyk
Andrew P
AP
D000818:Animals; D015703:Antigens, CD; D015820:Cadherins / Q000378:metabolism / Q000502:physiology*; D002448:Cell Adhesion; D003598:Cytoskeletal Proteins / Q000378:metabolism; D004730:Endothelium, Vascular / Q000166:cytology / Q000502:physiology*; D006801:Humans; D008954:Models, Biological; D015398:Signal Transduction / Q000502:physiology; D000099152:Cadherin 5
D015703:Antigens, CD; D015820:Cadherins; D003598:Cytoskeletal Proteins; D000099152:Cadherin 5