LAD-1, the Caenorhabditis elegans L1CAM homologue, participates in embryonic and gonadal morphogenesis and is a substrate for fibroblast growth factor receptor pathway-dependent phosphotyrosine-based signaling.

LAD-1, the Caenorhabditis elegans L1CAM homologue, participates in embryonic and gonadal morphogenesis and is a substrate for fibroblast growth factor receptor pathway-dependent phosphotyrosine-based signaling.
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DOI:
10.1083/jcb.200009004
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发表时间:
2001-08-20
期刊:
The Journal of cell biology
影响因子:
--
通讯作者:
Bennett V
Bennett V
中科院分区:
其他
文献类型:
--
作者:
Chen L;Ong B;Bennett V

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这项研究表明,L1样粘附(LAD-1),唯一的秀丽隐杆线虫同源的L1家族的神经元粘附分子,需要适当的发展的种系和早期胚胎和胚胎和性腺形态发生。此外,广泛表达的LAD-1与锚蛋白G结合,与C. elegans锚蛋白,p53 -44,在多个组织中的细胞-细胞接触部位。最后,我们表明,LAD-1是磷酸化的成纤维细胞生长因子受体(FGFR)的途径依赖性的方式上的酪氨酸残基的高度保守的锚蛋白结合基序,FIGQY,这是以前被证明废除的L1家族的细胞粘附分子(L1 CAM)结合锚蛋白在培养的细胞。免疫荧光研究显示,FIGQY-酪氨酸磷酸化的LAD-1不与非磷酸化的LAD-1或α-44锚蛋白共定位,而是定位于极化上皮和轴突-体壁肌肉连接中经受机械应力的位点。这些发现表明LAD-1与FGFR信号传导相关的新的不依赖于关节炎的作用。总之,这些结果表明,L1 CAMs构成了一个家庭的普遍存在的粘附分子,参与组织形态发生和维持组织的完整性在后生动物。
This study shows that L1-like adhesion (LAD-1), the sole Caenorhabditis elegans homologue of the L1 family of neuronal adhesion molecules, is required for proper development of the germline and the early embryo and embryonic and gonadal morphogenesis. In addition, the ubiquitously expressed LAD-1, which binds to ankyrin-G, colocalizes with the C. elegans ankyrin, UNC-44, in multiple tissues at sites of cell–cell contact. Finally, we show that LAD-1 is phosphorylated in a fibroblast growth factor receptor (FGFR) pathway-dependent manner on a tyrosine residue in the highly conserved ankyrin-binding motif, FIGQY, which was shown previously to abolish the L1 family of cell adhesion molecule (L1CAM) binding to ankyrin in cultured cells. Immunofluorescence studies revealed that FIGQY-tyrosine–phosphorylated LAD-1 does not colocalize with nonphosphorylated LAD-1 or UNC-44 ankyrin but instead is localized to sites that undergo mechanical stress in polarized epithelia and axon–body wall muscle junctions. These findings suggest a novel ankyrin-independent role for LAD-1 related to FGFR signaling. Taken together, these results indicate that L1CAMs constitute a family of ubiquitous adhesion molecules, which participate in tissue morphogenesis and maintaining tissue integrity in metazoans.
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