PECAM-1/CD31 trans-homophilic binding at the intercellular junctions is independent of its cytoplasmic domain; evidence for heterophilic interaction with integrin alphavbeta3 in Cis.

@article{Wong2000PECAM1CD31TB,
  title={PECAM-1/CD31 trans-homophilic binding at the intercellular junctions is independent of its cytoplasmic domain; evidence for heterophilic interaction with integrin alphavbeta3 in Cis.},
  author={Cindy W Wong and Guido Wiedle and Christoph Ballestrem and Bernhard Wehrle-Haller and Susanne Etteldorf and Markus Bruckner and Britta Engelhardt and Roland H. Gisler and Beat Albert Imhof},
  journal={Molecular biology of the cell},
  year={2000},
  volume={11 9},
  pages={
          3109-21
        }
}
PECAM-1/CD31 is a cell adhesion and signaling molecule that is enriched at the endothelial cell junctions. Alternative splicing generates multiple PECAM-1 splice variants, which differ in their cytoplasmic domains. It has been suggested that the extracellular ligand-binding property, homophilic versus heterophilic, of these isoforms is controlled by their cytoplasmic tails. To determine whether the cytoplasmic domains also regulate the cell surface distribution of PECAM-1 splice variants, we… CONTINUE READING
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