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J. Biol. Chem., Vol. 278, Issue 33, 31251-31260, August 15, 2003

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Recruitment of Nectin-3 to Cell-Cell Junctions through trans-Heterophilic Interaction with CD155, a Vitronectin and Poliovirus Receptor That Localizes to _v3 Integrin-containing Membrane Microdomains^*

Steffen Mueller  and Eckard Wimmer 

From the Department of Molecular Genetics and Microbiology, Stony Brook University, Stony Brook, New York 11794

Nectins present a novel class of Ig superfamily adhesion molecules that, cooperatively with cadherins, establish and maintain cell-cell adherens junctions. CD155, the cognate receptor for poliovirus, undergoes cell-matrix contacts by binding to the extracellular matrix protein vitronectin. The significant homology of nectins with CD155 prompted us to investigate the possibility of their interaction. We determined that nectin-3 binds CD155 and its putative mouse homologue Tage4 in cell-based ligand binding assays. Coculture of nectin-3- and CD155-expressing HeLa cells led to CD155-dependent recruitment of nectin-3 to cell-cell contacts. In a heterologous coculture system with CD155 expressing mouse neuroblastoma cells, HeLa cell-expressed nectin-3 was recruited to contact sites with CD155 bearing neurites. CD155 and nectin-3 colocalized to epithelial cell-cell junctions in renal proximal tubules and in the amniotic membrane. Efficient interaction depended on CD155 dimerization, which appears to be aided by cell type-specific cofactors. We furthermore found CD155 to codistribute with _v integrin microdomains on the surface of transfected mouse fibroblasts and at amniotic epithelial cell junctions. Our findings demonstrate the possible trans-interaction between the bona fide cell-cell adherens type adhesion system (cadherin/nectin) and the cell-matrix adhesion system (integrin/CD155) by virtue of their nectin-3 and CD155 components, respectively.

Received for publication, April 21, 2003

Note Added in Proof—Ikeda et al. (55) have shown heterophilic trans-interaction of necl-5/Tage4 with nectin-3, consistent with our result that CD155 heterophilically trans-interacts with nectin-3. Ikeda et al. (55) furthermore showed that the heterotrans-interaction of necl-5/Tage4 with nectin-3 enhances cell motility. Reymond et al. (56) have previously suggested an interaction between CD155 and nectin-3 without presenting data.

^* This work was supported in part by National Institutes of Health Grant AI39485 (to E. W.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Supported by a doctoral fellowship of the Boehringer Ingelheim Fonds, Heidesheim, Germany.

To whom correspondence should be addressed: Dept. of Molecular Genetics and Microbiology, Stony Brook University, Stony Brook, NY 11794. Tel.: 631-632-8787; Fax: 631-632-8891; E-mail: ewimmer{at}ms.cc.sunysb.edu.

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