Nuclear import of histones.
Nuclear import of histones.
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DOI：
10.1042/bst20200572
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发表时间：
2020-12-18
影响因子：
3.9
通讯作者：
Chook YM
中科院分区：
文献类型：
--
作者：
Bernardes NE;Chook YM
组蛋白从细胞质通过核膜转运到细胞核是一个调节细胞核中新组蛋白供应的细胞过程，是DNA复制和转录的关键。组蛋白的核输入由核转运受体的核转运蛋白家族的蛋白质介导。核转运蛋白通过称为核定位/输出序列的线性基序或通过货物中的折叠结构域识别其货物。核转运蛋白与核孔蛋白（形成核孔复合物的蛋白质）相互作用，以促进其货物转运到细胞核中。当与组蛋白结合时，核转运蛋白不仅起核输入受体的作用，而且还起分子伴侣的作用，保护组蛋白免受细胞质、核孔和可能的核中的非特异性相互作用。研究还表明，karyopherins可能参与组蛋白沉积到核小体。在这篇综述中，我们描述了过去二十年来关于核粒转运蛋白如何识别和转运核心组蛋白H3、H4、H2 A和H2 B以及连接组蛋白H1从细胞质到细胞核的结构和生化研究，其中核粒转运蛋白是这些组蛋白中每一种的主要核输入受体、核输入期间组蛋白的寡聚状态以及翻译后修饰的作用，组蛋白伴侣和RanGTP在调节这些核输入途径。
The transport of histones from the cytoplasm to the nucleus of the cell, through the nuclear membrane, is a cellular process that regulates the supply of new histones in the nucleus and is key for DNA replication and transcription. Nuclear import of histones is mediated by proteins of the karyopherin family of nuclear transport receptors. Karyopherins recognize their cargos through linear motifs known as nuclear localization/export sequences or through folded domains in the cargos. Karyopherins interact with nucleoporins, proteins that form the nuclear pore complex, to promote the translocation of their cargos into the nucleus. When binding to histones, karyopherins not only function as nuclear import receptors but also as chaperones, protecting histones from non-specific interactions in the cytoplasm, in the nuclear pore and possibly in the nucleus. Studies have also suggested that karyopherins might participate in histones deposition into nucleosomes. In this review we describe structural and biochemical studies from the last two decades on how karyopherins recognize and transport the core histone proteins H3, H4, H2A and H2B and the linker histone H1 from the cytoplasm to the nucleus, which karyopherin is the major nuclear import receptor for each of these histones, the oligomeric state of histones during nuclear import and the roles of post-translational modifications, histone-chaperones and RanGTP in regulating these nuclear import pathways.