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Vol. 11, Issue 9, 3109-3121, September 2000
v
3 in Cis*
¶¶
** and
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 examined the distribution of CD31-EGFPs
(PECAM-1 isoforms tagged with the enhanced green fluorescent protein)
in living Chinese hamster ovary cells and in PECAM-1-deficient
endothelial cells. Our results indicate that the extracellular, rather
than the cytoplasmic domain, directs PECAM-1 to the cell-cell borders.
Furthermore, coculturing PECAM-1 expressing and deficient cells along
with transfection of CD31-EGFP cDNAs into PECAM-1 deficient cells
reveal that this PECAM-1 localization is mediated by homophilic
interactions. Although the integrin Department of Pathology, Centre Médical
Universitaire, 1211 Geneva 4, Switzerland; Basel
Institute for Immunology, 4005 Basel, Switzerland; §Max
Planck Institut für physiologische und klinische Forschung, W.G.
Kerckhoff-Institut, Bad Nauheim, Germany
v
3 has been shown to
interact with PECAM-1, this trans-heterophilic interaction was not
detected at the borders of endothelial cells. However, based on
cocapping experiments performed on proT cells, we provide evidence that
the integrin v3 associates with PECAM-1 on the same cell
surface as in a cis manner.
Corresponding author. E-mail address:
Beat.Imhof{at}medecine.unige.ch.
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