β-catenin shows an overlapping sequence requirement but distinct molecular interactions for its bidirectional passage through nuclear pores
β-catenin shows an overlapping sequence requirement but distinct molecular interactions for its bidirectional passage through nuclear pores
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DOI：
10.1074/jbc.m405821200
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发表时间：
2004-08-06
影响因子：
4.8
通讯作者：
Imamoto, N
中科院分区：
文献类型：
--
作者：
Koike, M;Kose, S;Imamoto, N
β-连环蛋白是一种典型分子的实例，其可以自身以促进的方式通过核孔复合物（NPC）双向移位。在这项工作中，检查了β-连环蛋白的核输入和输出，以比较该分子的序列要求，并确定其双向NPC通道所需的分子相互作用是否不同。β-连环蛋白的缺失分析显示，犰狳重复10-12和C末端包括核迁移活动所需的最小区域。进一步解剖该片段表明，C末端尾在核迁移中起着重要作用。β-连环蛋白输出所需的区域与输入所需的区域基本重叠。因此，β-catenin的NPC易位是明显可逆的，这与先前报道的结果一致。然而，不同的转位分子阻断细胞核的β-连环蛋白的输入和输出的差异。本文的数据表明，β-连环蛋白显示出其输入和输出的重叠序列要求，但通过NPC的双向运动通过不同的分子相互作用进行。
beta-Catenin is an example of a typical molecule that can be translocated bidirectionally through nuclear pore complexes (NPCs) on its own in a facilitated manner. In this work the nuclear import and export of beta-catenin were examined to compare the sequence requirement of this molecule and to determine whether molecular interactions required for its bidirectional NPC passage are distinct or not. Deletion analysis of beta-catenin revealed that armadillo repeats 10-12 and the C terminus comprise the minimum region necessary for nuclear migration activity. Further dissection of this fragment showed that the C terminus tail plays an essential role in nuclear migration. The region of beta-catenin required for export substantially overlapped the region required for import. Therefore, the NPC translocation of beta-catenin is apparently reversible, which is consistent with findings reported previously. However, different translocating molecules blocked nuclear import and export of beta-catenin differentially. The data herein indicate that beta-catenin shows an overlapping sequence requirement for its import and export but that bidirectional movement through the NPC proceeds through distinct molecular interactions.