Translocation of beta-catenin into the nucleus independent of interactions with FG-rich nucleoporins.
Translocation of beta-catenin into the nucleus independent of interactions with FG-rich nucleoporins.
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DOI：
10.1016/s0014-4827(03)00370-7
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发表时间：
2003-11
影响因子：
3.7
通讯作者：
E. Suh;B. Gumbiner
中科院分区：
文献类型：
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作者：
E. Suh;B. Gumbiner
β-连环蛋白的核输入不依赖于经典的核定位信号（NLS）核输入因子。在这里，我们测试的假设，β-连环蛋白直接与核孔蛋白介导自己的运输。我们发现，β-catenin，不像importin-β，不与Phe/Gly（FG）-重复丰富的核孔蛋白或核孔蛋白（NUPS）可检测地相互作用。此外，与含有NLS的蛋白质不同，β-连环蛋白核输入不受麦胚凝集素（WGA）或过量输入素-β的抑制。这些结果表明β-连环蛋白核转位不涉及与FG-Nups的直接相互作用。然而，β-连环蛋白有两个区域可以将其靶向细胞核，并且其输入是冷敏感的，表明β-连环蛋白核输入仍然是一个活跃的过程。转运被可溶形式的C-钙粘蛋白胞质结构域阻断，表明核靶向信号的掩蔽可能是调节β-连环蛋白亚细胞定位的机制。
β-Catenin nuclear import has been found to be independent of classical nuclear localization signal (NLS) nuclear import factors. Here, we test the hypothesis that β-catenin interacts directly with nuclear pore proteins to mediate its own transport. We show that β-catenin, unlike importin-β, does not interact detectably with Phe/Gly(FG)-repeat-rich nuclear pore proteins or nucleoporins (Nups). Moreover, unlike NLS-containing proteins, β-catenin nuclear import is not inhibited by wheat germ agglutinin (WGA) or excess importin-β. These results suggest β-catenin nuclear translocation does not involve direct interactions with FG-Nups. However, β-catenin has two regions that can target it to the nucleus, and its import is cold sensitive, indicating that β-catenin nuclear import is still an active process. Transport is blocked by a soluble form of the C-cadherin cytoplasmic domain, suggesting that masking of the nuclear targeting signal may be a mechanism of regulating β-catenin subcellular localization.