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首页> 外文期刊>Cell communication & adhesion >Tumor-derived mutated E-cadherin influences beta-catenin localization and increases susceptibility to actin cytoskeletal changes induced by pervanadate
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Tumor-derived mutated E-cadherin influences beta-catenin localization and increases susceptibility to actin cytoskeletal changes induced by pervanadate

机译：肿瘤来源的突变的E-钙粘着蛋白影响β-catenin的定位并增加对过氧钒酸盐诱导的肌动蛋白细胞骨架变化的敏感性

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摘要

E-cadherin participates in homophilic cell-to-cell adhesion and is localized to intercellular junctions of the adherens type. In the present study, we investigated the localization of adherens junction components in cells expressing mutant E-cadherin derivatives which had been previously cloned from diffuse-type gastric carcinoma. The mutations are in frame deletions of exons 8 or 9 and a point mutation in exon 8 and affect the extracellular domain of E-cadherin. Our findings indicate that E-cadherin mutated in exon 8 causes beta-catenin staining at lateral cell-to-cell contact sites and, in addition, abnormally located beta-catenin in the perinuclear region. Moreover, the various mutant E-cadherin derivatives increased the steady-state levels of alpha- and beta-catenin and were found in association with these catenins even after induction of tyrosine phosphorylation by pervanadate. Sustained pervanadate treatment led, however, to rounding-up of cells and induction of filopodia, changes which were first detectable in cells expressing E-cadherin mutated in exon 8. The deterioration of the cell contact was not accompanied with disassembly of the E-cadherin-catenin complex. Based on these observations, we propose a model whereby in the presence of mutant E-cadherin tyrosine phosphorylation of components of the cell adhesion complex triggers loss of cell-to-cell contact and actin cytoskeletal changes which are not caused by the disruption of the E-cadherin-catenin complex per se, but instead might be due to phosphorylation of other signaling molecules or activation of proteins involved in the regulation of the actin cytoskeleton. [References: 75]
机译：E-钙粘着蛋白参与同源的细胞间粘附，并位于粘附类型的细胞间连接处。在本研究中，我们调查了表达突变E-钙粘蛋白衍生物的细胞中粘附连接成分的定位，该突变E-钙粘蛋白衍生物先前已从弥散型胃癌中克隆出来。突变发生在外显子8或9的框内缺失和外显子8的点突变中，并影响E-钙粘蛋白的胞外域。我们的研究结果表明，外显子8中的E-钙粘着蛋白突变会导致侧面细胞与细胞接触部位的β-catenin染色，此外，核周围区域的β-catenin异常定位。此外，各种突变的E-钙粘着蛋白衍生物增加了α-和β-连环蛋白的稳态水平，甚至在过氧钒酸盐诱导酪氨酸磷酸化后也发现与这些连环蛋白相关。持续的过氧钒酸盐处理导致细胞聚集和丝状伪足的发生，这些变化首先在表达E-钙粘蛋白的细胞中在外显子8中发生了突变。细胞接触的恶化并没有伴随着E-钙粘蛋白的拆卸-catenin复合物。基于这些观察，我们提出了一个模型，在存在突变的E-钙粘蛋白酪氨酸磷酸化的情况下，细胞粘附复合物的成分会触发细胞间接触的丧失和肌动蛋白细胞骨架的变化，而这种变化不是由E的破坏引起的-钙粘着蛋白-连环蛋白复合物本身，但可能是由于其他信号分子的磷酸化或肌动蛋白细胞骨架调节中涉及的蛋白质的激活。 [参考：75]

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