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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Nuclear localization of the p200ctn Armadillo-like catenin is counteracted by a nuclear export signal and by E-cadherin expression
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Nuclear localization of the p200ctn Armadillo-like catenin is counteracted by a nuclear export signal and by E-cadherin expression

机译：p200ctn类犰狳样连环蛋白的核定位被核输出信号和E-钙粘蛋白表达所抵消

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摘要

The Armadillo protein p120ctn associates with the cytoplasmic domain of cadherins and accumulates at cell-cell junctions. Paraticular Armadillo proteins such as beta-catenin and plakophillins show a partly nuclear location, suggesting gene-regulatory actaivities. For different human E-cadhering-negative carcinoma cancer cell lines we found expression of endogenous p120ctn in at the nucleus. Expression of E-cadherin directed p120ctn out of the nucleus. Previously, we reported that the human p120ctn gene might encode up to 32 protein isoforms as products of alternative splicing. Overexpression of p120ctn isoforms B in various cell lines resulted in cytoplasmic immunopositivity but never in nuclear staining. In contrast, upon expression of p120ctn cDNAs lacking exon B, the isoforms were detectable within both nuclei and cytoplasm. A putative nuclear export signal (NES) with a characteristic leucine-rich motif is encoded by exon B. This sequence element was shown to be required for nuclear export and to function autonomously when fused to a carrier protein and microinjected into cell nuclei. Moreover , the NES function of endogenously or exogenously expressed p120ctn isoforms B was sensitive to the nuclear export inhibitor leptomycin B. Expression of exogenous E-cadherin down-regulated nuclear p120ctn whereas activation of protein kinase C increased the level of nuclear p120ctn. These results reveal molecular mechanisms controlling the subcellular distribution of p120ctn.
机译：犰狳蛋白p120ctn与钙黏着蛋白的胞质域结合，并积累在细胞间连接处。副臂犰狳蛋白（例如β-catenin和plakophillins）显示出部分核位置，表明基因调节活性。对于不同的人E-cadhering-阴性癌细胞系，我们在细胞核中发现了内源性p120ctn的表达。 E-钙粘着蛋白的表达指导p120ctn脱离细胞核。以前，我们报道了人类p120ctn基因可能编码多达32种蛋白质同工型，作为替代剪接的产物。 p120ctn亚型B在各种细胞系中的过表达导致细胞质免疫阳性，但从未导致核染色。相反，表达缺少外显子B的p120ctn cDNA时，在细胞核和细胞质中都可检测到同工型。外显子B编码具有特征性的富含亮氨酸的基序的推定核输出信号（NES）。该序列元件被证明是核输出所必需的，并且在与载体蛋白融合并显微注射到细胞核中时具有自主功能。此外，内源性或外源表达的p120ctn亚型B的NES功能对核输出抑制剂瘦霉素B敏感。外源E-钙粘蛋白的表达下调了核p120ctn，而蛋白激酶C的激活增加了核p120ctn的水平。这些结果揭示了控制p120ctn亚细胞分布的分子机制。

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