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小泛素样修饰蛋白与核质运输

SUMO and Nucleocytoplasmic Transport.

作者信息

Ptak Christopher, Wozniak Richard W

机构信息

Department of Cell Biology, University of Alberta, Edmonton, AB, T6G 2H7, Canada.

出版信息

Adv Exp Med Biol. 2017;963:111-126. doi: 10.1007/978-3-319-50044-7_7.

Abstract

The transport of proteins between the nucleus and cytoplasm occurs through nuclear pore complexes and is facilitated by numerous transport factors. These transport processes are often regulated by post-translational modification or, reciprocally, transport can function to control post-translational modifications through regulated transport of key modifying enzymes. This interplay extends to relationships between nucleocytoplasmic transport and SUMO-dependent pathways. Examples of protein sumoylation inhibiting or stimulating nucleocytoplasmic transport have been documented, both through its effects on the physical properties of cargo molecules and by directly regulating the functions of components of the nuclear transport machinery. Conversely, the nuclear transport machinery regulates the localization of target proteins and enzymes controlling dynamics of sumoylation and desumoylation thereby affecting the sumoylation state of target proteins. These inter-relationships between SUMO and the nucleocytoplasmic transport machinery, and the varied ways in which they occur, are discussed.

摘要

蛋白质在细胞核与细胞质之间的转运通过核孔复合体进行,并由众多转运因子协助。这些转运过程通常受翻译后修饰调控,反之,转运也可通过关键修饰酶的调控转运来控制翻译后修饰。这种相互作用延伸到核质转运与SUMO依赖途径之间的关系。蛋白质SUMO化抑制或刺激核质转运的例子已有记载,这既通过其对货物分子物理性质的影响,也通过直接调节核转运机制组分的功能来实现。相反,核转运机制调节靶蛋白和控制SUMO化与去SUMO化动态的酶的定位,从而影响靶蛋白的SUMO化状态。本文讨论了SUMO与核质转运机制之间的这些相互关系,以及它们发生的多种方式。

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