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J. Biol. Chem., Vol. 280, Issue 6, 4753-4760, February 11, 2005

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Separation Force Measurements Reveal Different Types of Modulation of E-cadherin-based Adhesion by Nectin-1 and -3^*

Clara Martinez-Rico, Frederic Pincet¶, Eric Perez¶, Jean Paul Thiery, Kazuya Shimizu||, Yoshimi Takai||, and Sylvie Dufour**

From the UMR 144 CNRS-Institut Curie, 26 rue d'Ulm, 75248 Paris Cedex 05, France, the ^¶UMR8550 CNRS-ENS, 24 rue Lhomond, 75248 Paris Cedex 05, France, and the ^||Department of Molecular Biology and Biochemistry, Osaka University Graduate School of Medicine/Faculty of Medicine, Suita, 565-0871, Japan

Nectins are Ca²⁺-independent cell adhesion molecules found at cadherin-based adherens junctions. We used a dual pipette assay that measures the forces required to separate cell doublets to determine how nectins affect the formation and strength of cell-cell adhesion. Less force was required to separate doublets of L cells expressing nectin-1 or nectin-3 than to separate doublets of E-cadherin-expressing cells. Heterodimers formed between cells expressing nectin-1 or nectin-3 adhered more strongly than homodimers. Nectin-3 that does not trans-interact with nectin-1 inhibited E-cadherin-mediated adhesion. However, the extracellular fragment of nectin-1 did not have an agonistic effect on E-cadherin-dependent cell adhesion when it trans-interacted with nectin-3, expressed at high levels in cells. In contrast, the extracellular fragment of nectin-3 had a significant agonistic effect on cadherin-based adhesion when it interacted with endogenous nectin-1, expressed at low levels in cells. Our results indicate that E-cadherin is the key molecule involved in cell adhesion and that the regulation of E-cadherin-based adhesion involving cellular nectin-1 trans-interacting with nectin-3 is qualitatively different from that involving cellular nectin-3 trans-interacting with nectin-1 and depends on the nectin levels expressed by cells.

Received for publication, November 5, 2004 , and in revised form, November 16, 2004.

^* This work was supported in part by the CNRS, the Institut Curie (Programme Incitatif et Coopératif, Physicochimie des Structures Biologiques Complexes), and European Community Contract QLGI-CT-2001-00869. 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 fellowships from an European Community contract.

^** To whom correspondence should be addressed. Tel: 33-1-42-34-63-35; Fax: 33-1-42-34-63-49; E-mail: Sylvie.Dufour{at}curie.fr.

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