Implications of nectin-like molecule-2/IGSF4/RA175/SgIGSF/TSLC1/SynCAM1 in cell-cell adhesion and transmembrane protein localization in epithelial cells
Implications of nectin-like molecule-2/IGSF4/RA175/SgIGSF/TSLC1/SynCAM1 in cell-cell adhesion and transmembrane protein localization in epithelial cells
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DOI：
10.1074/jbc.m305387200
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发表时间：
2003-09-12
影响因子：
4.8
通讯作者：
Takai, Y
中科院分区：
文献类型：
--
作者：
Shingai, T;Ikeda, W;Takai, Y
Nectin是一种钙离子非依赖性免疫球蛋白样细胞间粘附分子，与钙粘蛋白协同或独立于钙粘蛋白，在多种细胞间连接的组织中发挥作用。已鉴定出四种连接素。已经鉴定了五种具有与nectin相似的结构域的nectin样分子，并且我们在这里表征了nectin样分子-2（Necl-2）/IGSF 4/RA 175/SgIGSF/TSLC 1/SynCAM 1。Necl-2显示出不依赖于Ca~（2+）的嗜同性细胞间粘附活性。它还显示出与Necl-1/TSLL1/SynCAM 3和nectin-3的Ca2+非依赖性异嗜性细胞-细胞粘附活性。Necl-2在大鼠组织中广泛表达。necl-2定位于基底侧质膜在小鼠胆囊上皮细胞，但不是在专门的细胞-细胞连接，如紧密连接，粘附连接，桥粒。Nectin结合afadin，而Necl-2不结合afadin但结合Pals2，Pals2是已知结合Lin-7的膜相关鸟苷酸激酶家族成员，涉及秀丽隐杆线虫中Let-23蛋白的适当定位，哺乳动物表皮生长因子受体的同源物。这些结果表明Necl-2的独特定位及其可能参与跨膜蛋白通过Pals2的定位。
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.