Abstract
In C. elegans, lin-7 as well as lin-2/lin-10 is involved in the proper localization of the LET-23 receptor tyrosine kinase that regulates vulval induction. The mammalian homologue, mLin-7, forms a ternary complex with the mammalian homologues of LIN-2 and LIN-10 and localizes at cell–cell junctions in epithelial cells, but the mechanism of this localization of mLin-7 is unknown. Nectin is an immunoglobulin-like cell–cell adhesion molecule that is involved in organization of adherens and tight junctions in epithelial cells. Nectin is indirectly associated with the cadherin–catenin system and the actin cytoskeleton through afadin, an actin filament-binding protein. We showed here that mLin-7 localized at the nectin-based cell–cell junctions. This localization of mLin-7 required the interaction of nectin with afadin, but not the cadherin–catenin system or the actin cytoskeleton. mLin-7 did not directly interact with nectin or afadin. The results indicate that mLin-7 localizes at cell–cell junctions through the nectin–afadin system.
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Acknowledgements
We thank Dr M Takeichi (Kyoto University, Kyoto, Japan) for providing us with the anti-E-cadherin mAb (ECCD2), Dr Sh Tsukita (Kyoto University, Kyoto, Japan) for providing us with the anti-ZO-1 mAb and EL cells, and Dr K Yanagihara (National Cancer Center Research Institute, Tokyo, Japan) for providing us with HSC-39 cells. We are also grateful to Dr E Majima (Apro Science Company, Tokushima, Japan) and Dr M Takeuchi (KAN Research Institute, Inc., Kyoto, Japan) for mass spectrometry. The investigation was supported by grants-in-aid for Scientific Research and for Cancer Research from the Ministry of Education, Culture, Sports, Science, and Technology, Japan (2001).
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Yamamoto, Y., Mandai, K., Okabe, N. et al. Localization of mLin-7 at nectin-based cell–cell junctions. Oncogene 21, 2545–2554 (2002). https://doi.org/10.1038/sj.onc.1205335
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DOI: https://doi.org/10.1038/sj.onc.1205335
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