核通道蛋白与核转运受体的相互作用:结构观点。

IF 2.9 4区 生物学 Q3 BIOCHEMISTRY & MOLECULAR BIOLOGY
Biological Chemistry Pub Date : 2023-05-22 Print Date: 2023-07-26 DOI:10.1515/hsz-2023-0155
Ralph H Kehlenbach, Piotr Neumann, Ralf Ficner, Achim Dickmanns
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引用次数: 0

摘要

可溶性核转运受体和固定的核通道蛋白是核质转运机制的核心。核通道蛋白的一个子集包含特征性和重复性FG(苯丙氨酸甘氨酸)基序,这是控制大分子在细胞核和细胞质之间运输的核孔复合体(NPC)渗透屏障的基础。FG基序可以相互作用和/或与转运受体相互作用,介导它们在NPC中的易位。同源和异型FG相互作用的分子细节已经在结构水平上进行了分析。在这篇综述中,我们重点讨论了核通道蛋白与核转运受体的相互作用。除了作为相互作用点的传统FG基序外,一项彻底的结构分析使我们在核通道蛋白和转运受体之间的结合界面上识别出了其他类似的基序。对所有已知的人类核通道蛋白的详细分析揭示了大量这样的含有苯丙氨酸的基序,这些基序不埋在相应蛋白质的预测3D结构中,而是构成溶剂可及表面积的一部分。只有富含常规FG重复序列的核通道蛋白也富含这些基序。核通道蛋白上对转运受体的这种潜在的低亲和力结合位点的额外层可能对转运复合物与核孔的相互作用产生强烈影响,从而影响核质转运的效率。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Interaction of nucleoporins with nuclear transport receptors: a structural perspective.

Soluble nuclear transport receptors and stationary nucleoporins are at the heart of the nucleocytoplasmic transport machinery. A subset of nucleoporins contains characteristic and repetitive FG (phenylalanine-glycine) motifs, which are the basis for the permeability barrier of the nuclear pore complex (NPC) that controls transport of macromolecules between the nucleus and the cytoplasm. FG-motifs can interact with each other and/or with transport receptors, mediating their translocation across the NPC. The molecular details of homotypic and heterotypic FG-interactions have been analyzed at the structural level. In this review, we focus on the interactions of nucleoporins with nuclear transport receptors. Besides the conventional FG-motifs as interaction spots, a thorough structural analysis led us to identify additional similar motifs at the binding interface between nucleoporins and transport receptors. A detailed analysis of all known human nucleoporins revealed a large number of such phenylalanine-containing motifs that are not buried in the predicted 3D-structure of the respective protein but constitute part of the solvent-accessible surface area. Only nucleoporins that are rich in conventional FG-repeats are also enriched for these motifs. This additional layer of potential low-affinity binding sites on nucleoporins for transport receptors may have a strong impact on the interaction of transport complexes with the nuclear pore and, thus, the efficiency of nucleocytoplasmic transport.

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来源期刊
Biological Chemistry
Biological Chemistry 生物-生化与分子生物学
CiteScore
7.20
自引率
0.00%
发文量
63
审稿时长
4-8 weeks
期刊介绍: Biological Chemistry keeps you up-to-date with all new developments in the molecular life sciences. In addition to original research reports, authoritative reviews written by leading researchers in the field keep you informed about the latest advances in the molecular life sciences. Rapid, yet rigorous reviewing ensures fast access to recent research results of exceptional significance in the biological sciences. Papers are published in a "Just Accepted" format within approx.72 hours of acceptance.
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