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Vol. 19, Issue 11, 4687-4693, November 2008
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*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 Cell Biology, Department of Physiology and Cell Biology, Kobe University, Graduate School of Medicine, Kobe 650-0017, Japan; and
PRESTO, Japan Science and Technology Agency, Saitama 332–0012, Japan
Submitted May 28, 2008;
Revised July 16, 2008;
Accepted August 21, 2008
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 it 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 tight junctions (TJs), we found that tricellulin was incorporated into claudin-based TJs independently of binding to zona occludens-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 supports 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)
Abbreviations used: AJ, adherens junction; bTJ, bicellular tight junction; TJ, tight junction; tTJ, tricellular tight junction.