VE-cadherin: Adhesion at arm's length

Peter A. Vincent, Kanyan Xiao, Kathleen M. Buckley, Andrew P. Kowalczyk

Research output: Contribution to journalReview articlepeer-review

141 Scopus citations


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 β-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.

Original languageEnglish (US)
Pages (from-to)C987-C997
JournalAmerican Journal of Physiology - Cell Physiology
Issue number5 55-5
StatePublished - May 2004

All Science Journal Classification (ASJC) codes

  • Physiology
  • Cell Biology


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