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你是谁取决于你的朋友是谁——核孔蛋白作为染色质结合复合物的组成部分。

You are who your friends are-nuclear pore proteins as components of chromatin-binding complexes.

机构信息

Cell and Molecular Biology Program, Department of Biology, San Diego State University, CA, USA.

出版信息

FEBS Lett. 2023 Nov;597(22):2769-2781. doi: 10.1002/1873-3468.14728. Epub 2023 Sep 7.

DOI:10.1002/1873-3468.14728
PMID:37652464
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC11081553/
Abstract

Nuclear pore complexes are large multicomponent protein complexes that are embedded in the nuclear envelope, where they mediate nucleocytoplasmic transport. In addition to supporting transport, nuclear pore components, termed nucleoporins (Nups), can interact with chromatin and influence genome function. A subset of Nups can also localize to the nuclear interior and bind chromatin intranuclearly, providing an opportunity to investigate chromatin-associated functions of Nups outside of the transport context. This review focuses on the gene regulatory functions of such intranuclear Nups, with a particular emphasis on their identity as components of several chromatin regulatory complexes. Recent proteomic screens have identified Nups as interacting partners of active and repressive epigenetic machinery, architectural proteins, and DNA replication complexes, providing insight into molecular mechanisms via which Nups regulate gene expression programs. This review summarizes these interactions and discusses their potential functions in the broader framework of nuclear genome organization.

摘要

核孔复合体是一种大型的多组分蛋白复合物,嵌入核膜中,介导核质转运。除了支持运输外,核孔复合体的成分,称为核孔蛋白(Nups),可以与染色质相互作用并影响基因组功能。一小部分 Nups 也可以定位于核内部并与染色质在核内结合,为研究核孔蛋白在运输背景之外的与染色质相关的功能提供了机会。本综述重点介绍了这种核内 Nups 的基因调控功能,特别强调了它们作为几个染色质调控复合物的组成部分的身份。最近的蛋白质组学筛选已经鉴定出 Nups 是活性和抑制性表观遗传机制、结构蛋白和 DNA 复制复合物的相互作用伙伴,为 Nups 调节基因表达程序的分子机制提供了深入了解。本综述总结了这些相互作用,并讨论了它们在核基因组组织的更广泛框架中的潜在功能。

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Barrier properties of Nup98 FG phases ruled by FG motif identity and inter-FG spacer length.核孔复合体蛋白 Nup98 FG 相的屏障特性由 FG 基序的身份和 FG 间隔区长度决定。
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Nucleoporins facilitate ORC loading onto chromatin.
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