Implications of nectin-like molecule-2/IGSF4/RA175/SgIGSF/TSLC1/SynCAM1 in cell-cell adhesion and transmembrane protein localization in epithelial cells

被引:186
作者
Shingai, T
Ikeda, W
Kakunaga, S
Morimoto, K
Takekuni, K
Itoh, S
Satoh, K
Takeuchi, M
Imai, T
Monden, M
Takai, Y [1 ]
机构
[1] Osaka Univ, Fac Med, Grad Sch Med, Dept Biochem & Mol Biol, Osaka 5650871, Japan
[2] Osaka Univ, Fac Med, Grad Sch Med, Dept Surg & Clin Oncol, Osaka 5650871, Japan
[3] KAN Res Inst Inc, Shimogyo Ku, Kyoto 6008815, Japan
关键词
D O I
10.1074/jbc.M305387200
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Nectins are Ca2+-independent immunoglobulin-like cell-cell adhesion molecules that play roles in organization of a variety of cell-cell junctions in cooperation with or independently of cadherins. Four nectins have been identified. Five nectin-like molecules, which have domain structures similar to those of nectins, have been identified, and we characterized here nectin-like molecule-2 (Necl-2)/IGSF4/RA175/SgIGSF/TSLC1/SynCAM1. Necl-2 showed Ca2+-independent homophilic cell-cell adhesion activity. It furthermore showed Ca2+-independent heterophilic cell-cell adhesion activity with Necl-1/TSLL1/SynCAM3 and nectin-3. Necl-2 was widely expressed in rat tissues examined. Necl-2 localized at the basolateral plasma membrane in epithelial cells of the mouse gall bladder, but not at specialized cell-cell junctions, such as tight junctions, adherens junctions, and desmosomes. Nectins bind afadin, whereas Necl-2 did not bind afadin but bound Pals2, a membrane-associated guanylate kinase family member known to bind Lin-7, implicated in the proper localization of the Let-23 protein in Caenorhabditis elegans, the homologue of mammalian epidermal growth factor receptor. These results indicate the unique localization of Necl-2 and its possible involvement in localization of a transmembrane protein(s) through Pals2.
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页码:35421 / 35427
页数:7
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