PECAM-1/CD31 trans-homophilic binding at the intercellular junctions is independent of its cytoplasmic domain;: Evidence for heterophilic interaction with integrin αvβ3 in cis

被引:84
作者
Wong, CWY
Wiedle, G
Ballestrem, C
Wehrle-Haller, B
Etteldorf, S
Bruckner, M
Engelhardt, B
Gisler, RH
Imhof, BA [1 ]
机构
[1] Ctr Med Univ Geneva, Dept Pathol, CH-1211 Geneva 4, Switzerland
[2] Basel Inst Immunol, CH-4005 Basel, Switzerland
[3] Max Planck Inst Physiol & Klin Forsch, WG Kerckhoff Inst, Bad Nauheim, Germany
关键词
D O I
10.1091/mbc.11.9.3109
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
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 alpha v beta 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 alpha v beta 3 associates with PECAM-1 on the same cell surface as in a cis manner.
引用
收藏
页码:3109 / 3121
页数:13
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