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Originally published as MBC in Press, 10.1091/mbc.E03-05-0321 on December 29, 2003

Vol. 15, Issue 3, 1077-1088, March 2004

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A Novel Role of Nectins in Inhibition of the E-Cadherin–induced Activation of Rac and Formation of Cell-Cell Adherens Junctions

Takashi Hoshino *, Kazuya Shimizu *, Tomoyuki Honda *, Tomomi Kawakatsu *, Taihei Fukuyama *, Takeshi Nakamura {dagger}, Michiyuki Matsuda {dagger}, and Yoshimi Takai * {ddagger}

* Department of Molecular Biology and Biochemistry, Osaka University Graduate School of Medicine/Faculty of Medicine, Suita 565-0871, Japan; {dagger} Department of Tumor Virology, Research Institute for Microbial Diseases, Osaka University, Suita 565-0871, Japan

Submitted May 22, 2003; Revised October 24, 2003; Accepted November 28, 2003
Monitoring Editor: Suzanne Pfeffer

Nectins are Ca2+-independent immunoglobulin (Ig)-like cell-cell adhesion molecules. The trans-interactions of nectins recruit cadherins to the nectin-based cell-cell adhesion, resulting in formation of cell-cell adherens junctions (AJs) in epithelial cells and fibroblasts. The trans-interaction of E-cadherin induces activation of Rac small G protein, whereas the trans-interactions of nectins induce activation of not only Rac but also Cdc42 small G protein. We showed by the fluorescent resonance energy transfer (FRET) imaging that the trans-interaction of E-cadherin induced dynamic activation and inactivation of Rac, which led to dynamic formation and retraction of lamellipodia. Moreover, we found here that the nectins, which did not trans-interact with other nectins (non–trans-interacting nectins), inhibited the E-cadherin–induced activation of Rac and reduced the velocity of the formation of the E-cadherin-based cell-cell AJs. The inhibitory effect of non–trans-interacting nectins was suppressed by the activation of Cdc42 induced by the trans-interactions of nectins. These results indicate a novel role of nectins in regulation of the E-cadherin–induced activation of Rac and formation of cell-cell AJs.

Abbreviations used: aa, amino acid(s); AJs, adherens junctions; Cef, the extracellular fragment of E-cadherin fused to the IgG Fc; CRIB, Cdc42 and Rac interactive binding domain; DIC, differential interference contrast; F-actin, actin filaments; FRET, fluorescent resonance energy transfer; GFP, green fluorescent protein; IMD, intensity modulated display; mAb, monoclonal antibody; MDCK, Madin-Darby canine kidney; Nef, the extracellular fragment of nectin fused to the IgG Fc; pAb, polyclonal Ab; PI3 kinase, phosphatidylinositol-3 kinase.

Article published online ahead of print. Mol. Biol. Cell 10.1091/mbc.E03–05–0321. Article and publication date are available at www.molbiolcell.org/cgi/doi/10.1091/mbc.E03-05-0321.

Online version of this article contains video material. Online version is available at www.molbiolcell.org.

{ddagger} Corresponding author. E-mail address: ytakai{at}molbio.med.osakau.ac.jp.




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