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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

Wong, C. W.
Ballestrem, Christoph
Etteldorf, S.
Bruckner, M.
Engelhardt, Britta
Gisler, R. H.
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Published in Molecular Biology of the Cell. 2000, vol. 11, no. 9, p. 3109-3121
Abstract 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 alphavbeta3 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 alphavbeta3 associates with PECAM-1 on the same cell surface as in a cis manner.
Keywords Alternative SplicingAnimalsAntigens, CD31/chemistry/ genetics/ metabolismCHO CellsCapillaries/cytology/physiologyCell LineCells, CulturedCerebrovascular CirculationCricetinaeCytoplasm/physiologyEndothelium, Vascular/ physiology/ultrastructureExonsGreen Fluorescent ProteinsIntercellular Junctions/ physiologyLuminescent Proteins/analysisMiceMice, KnockoutModels, MolecularProtein ConformationReceptors, Vitronectin/chemistry/ metabolismRecombinant Fusion Proteins/analysis/metabolismSignal TransductionTransfection
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PMID: 10982404
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