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A more recent version of this article appeared on November 1, 2008
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Submitted on May 28, 2008
Revised on July 16, 2008
Accepted on August 21, 2008

*Department of Cell Biology, Faculty of Medicine, Kyoto University, Kyoto 606-8501, Japan;
Department of Molecular Cell Biology, Institute of DNA Medicine, The Jikei University School of Medicine, Tokyo 105-8461, Japan; ||Laboratory of Biological Science, Graduate School of Frontier Biosciences and Graduate School of Medicine, Osaka University, Suita, Osaka 565-0871, Japan; ¶Division of Cellular and Molecular Medicine, Kobe University Graduate School of Medicine, Kobe 650-0017, Japan;
PRESTO, Japan Science and Technology Agency, Saitama 332-0012, Japan
Monitoring Editor: Keith E. Mostov
The tricellular tight junction (tTJ) forms at the convergence of bicellular tight junctions (bTJs) where three epithelial cells meet in polarized epithelia and is required for the maintenance of the transepithelial barrier. Tricellulin is a four transmembrane domain protein recently identified as the first marker of tTJ, but little is known about how tricellulin is localized at tTJs. As for the molecular mechanism of association of tricellulin with TJs, we found that tricellulin was incorporated into claudin-based TJs independently of binding to ZO-1. Unexpectedly, exogenous expression of tricellulin increased cross-links of TJ strands in the plasma membrane. As for the molecular mechanisms for localization of tricellulin at tricellular junctions, we found that knockdown of occludin caused mislocalization of tricellulin to bTJs, implying that occludin support tricellular localization of tricellulin by excluding tricellulin from bTJs.
Present address: Institute for Chemical Research, Kyoto University, Uji, Kyoto 611-0011, Japan.
Address correspondence to:
Junichi Ikenouchi (ikenouti{at}scl.kyoto-u.ac.jp)
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