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J. Biol. Chem., Vol. 279, Issue 30, 31365-31373, July 23, 2004

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Involvement of LMO7 in the Association of Two Cell-Cell Adhesion Molecules, Nectin and E-cadherin, through Afadin and -Actinin in Epithelial Cells^*

Takako Ooshio, Kenji Irie, Koji Morimoto, Atsunori Fukuhara, Toshio Imai, and Yoshimi Takai¶

From the Department of Molecular Biology and Biochemistry, Osaka University Graduate School of Medicine/Faculty of Medicine, 2-2 Yamada-oka Suita, Osaka 565-0871 and the KAN Research Institute, Inc., 93 Chudoji-Awatamachi, Shimogyo-ku, Kyoto 600-8815, Japan

Nectins are Ca²⁺-independent immunoglobulin-like cell-cell adhesion molecules that are involved in formation of cadherin-based adherens junctions (AJs). The nectin-based cell-cell adhesion induces activation of Cdc42 and Rac small G proteins, which eventually enhances the formation of AJs through reorganization of the actin cytoskeleton. Although evidence has accumulated that nectins recruit cadherins to the nectin-based cell-cell adhesion sites through their cytoplasm-associated proteins, afadin and catenins, it is not fully understood how nectins are physically associated with cadherins. Here we identified a rat counterpart of the human LIM domain only 7 (LMO7) as an afadin- and -actinin-binding protein. Rat LMO7 has two splice variants, LMO7a and LMO7b, consisting of 1,729 and 1,395 amino acids, respectively. LMO7 has calponin homology, PDZ, and LIM domains. Western blotting revealed that LMO7 was expressed ubiquitously in various rat tissues. Immunofluorescence and immunoelectron microscopy revealed that LMO7 localized at cell-cell AJs, where afadin localized, in epithelial cells of rat gallbladder. In addition, LMO7 localized at the cytoplasmic faces of apical membranes in the same epithelial cells. We furthermore revealed that LMO7 bound -actinin, an actin filament-bundling protein, which bound to -catenin. Immunoprecipitation analysis revealed that LMO7 was associated with both the nectin-afadin and E-cadherin-catenin systems. LMO7 was assembled at the cell-cell adhesion sites after both the nectin-afadin and E-cadherin-catenin systems had been assembled. These results indicate that LMO7 is an afadin- and -actinin-binding protein that connects the nectin-afadin and E-cadherin-catenin systems through -actinin.

Received for publication, February 23, 2004 , and in revised form, May 3, 2004.

^* This work was supported by grants-in-aid for Scientific Research and for Cancer Research from the Ministry of Education, Science, Sports, Culture, and Technology, Japan, and by the NOVARTIS Foundation (Japan) for the Promotion of Science (to K. I.). 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.

^¶ To whom correspondence should be addressed. Tel.: 81-6-6879-3410; Fax: 81-6-6879-3419; E-mail: ytakai{at}molbio.med.osaka-u.ac.jp.

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