Identification and functional analyses of novel proteins involved in the regulation of epithelial cell-cell adhesion
| Project/Area Number |
18370078
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| Research Category |
Grant-in-Aid for Scientific Research (B)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Cell biology
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| Research Institution | Kobe University |
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Principal Investigator |
FURUSE Mikio Kobe University, Graduate School of Medicine, Professor (90281089)
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| Project Period (FY) |
2006 – 2007
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| Project Status |
Completed (Fiscal Year 2007)
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| Budget Amount *help |
¥16,490,000 (Direct Cost: ¥14,600,000、Indirect Cost: ¥1,890,000)
Fiscal Year 2007: ¥8,190,000 (Direct Cost: ¥6,300,000、Indirect Cost: ¥1,890,000)
Fiscal Year 2006: ¥8,300,000 (Direct Cost: ¥8,300,000)
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| Keywords | epithelial cells / cell adhesion / tight junctions / adherens junctions / tricellular junctions / GAP / GFP |
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| Research Abstract |
To clarify the molecular mechanism behind the regulation of epithelial cell-cell adhesion, we looked for novel proteins that are localized at tight and adherens junctions by a novel expression cloning method based on subcellular localization, namely the fluorescence localization-based retrovirus-mediated expression cloning (FL-REX). Initially, we confirmed that cDNAs for various known components associated with tight and adherens junctions were indeed identified in this screening by using cDNA libraries generated from various epithelial cell lines. Then, we found that ARHGAP12 and SPAL3, potential GTPase activating proteins for small G proteins identified in this method, are concentrated into epithelial adherens junctions by immunoflureoscence staining. When SPAL3, which has a Rap-GAP domain, was overexpressed in cultured fibroblasts, the cells remarkably elongated. Furthermore, cultured epithelial cells overexpressing SPAL3 exhibited retardation in cell-cell junction formation, suggesting that SPAL3 is involved in the regulation of epithelial cell-cell adhesion via actin filaments. In addition, by using the FL-REX method, we have succeeded in identification of a novel membrane protein TRCX, which is localized at tricellular junctions and is involved in the barrier function of the epithelial cellular sheet. This result is expected to contribute to the future analyses of the molecular mechanism behind the formation and physiological functions of tricellular junctions, which have not been well analyzed yet.
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Report
(3 results)
Research Products
(26 results)
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[Journal Article] Identification of adherens junction-associated GTPase activating proteinsby the fluorescence localization-based expression cloning2008
Author(s)
Matsuda, M., Kobayashi, Y., Masuda, S., Adachi, M., Watanabe, T., Yamashita, JK., Nishi, E., Tsukita, S., Furuse, M.
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Journal Title
Exp. Cell Res. 314
Pages: 939-949
Description
「研究成果報告書概要(欧文)」より
Related Report
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[Journal Article] Megaintestine in claudin-15-deficient mice2008
Author(s)
Tamura, A., Kitano, Y., Hata, M., Katsuno, T., Moriwaki, K., Sasaki, H., Hayashi, H., Suzuki, Y, Noda, T., Furuse, M., Tsukita, S., Tsukita, S.
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Journal Title
Gastroenterology 134
Pages: 523-534
Description
「研究成果報告書概要(欧文)」より
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[Journal Article] Molecular characterization of angiomotin/JEAP family proteins : interaction with MUPP1/Patj and their endogenous properties.2007
Author(s)
Sugihara-Mizuno, Y., Adachi, M., Kobayashi, Y, Hamazaki, Y, Nishimura, M., Imai, T., Furuse, M., Tsukita, S.
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Journal Title
Genes Cells 12
Pages: 473-486
Description
「研究成果報告書概要(欧文)」より
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[Journal Article] ZO-1 and ZO-2 independently determine where claudins are polymerized in tight junction strand formation.2006
Author(s)
Umeda, K., Ikenouchi, J., Katahira-Tayama, S., Furuse, K., Sasaki, H., Nakayama, M., Matsui, T., Tsukita, S., Furuse, M., Tsukita, S.
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Description
「研究成果報告書概要(欧文)」より
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