Moesin 通过与细胞核中 Mediator 复合物的 Med15 亚基直接结合,促进热休克基因的反应。

IF 4.5 3区 生物学 Q1 BIOCHEMISTRY & MOLECULAR BIOLOGY
Open Biology Pub Date : 2024-10-01 Epub Date: 2024-10-02 DOI:10.1098/rsob.240110
Ildikó Kristó, Zoltán Kovács, Anikó Szabó, Péter Borkúti, Alexandra Gráf, Ádám Tamás Sánta, Aladár Pettkó-Szandtner, Edit Ábrahám, Viktor Honti, Zoltán Lipinszki, Péter Vilmos
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引用次数: 0

摘要

进化保守的肌动蛋白结合型 Ezrin、Radixin 和 Moesin(ERM)蛋白家族成员参与了细胞质中许多关键的细胞过程。在过去的几十年中,ERM 蛋白与肌动蛋白和其他细胞骨架成分一样,也被证明是细胞核的功能成分;然而,其核活动背后的分子机制仍不清楚。因此,我们的主要目的是鉴定单一果蝇ERM蛋白Moesin的核蛋白相互作用组。我们证明,Moesin通过与Mediator复合物的Med15亚基直接结合而与Mediator复合物直接相互作用,并且发现Moesin存在于Hsp70Ab热休克基因的调控区域是依赖于Med15的。Moesin和Med15都与热休克因子(Hsf)结合,它们是生理条件下Hsp基因正常表达所必需的。此外,我们还证实,Moesin、Med15 和 Hsf 能够结合肌动蛋白的单体形式,并在细胞核中形成复合物。这些结果阐明了 ERMs 在细胞核内发挥作用的机制。最后,我们介绍了果蝇 Moesin 和 Med15 的人类直向同源物之间的直接相互作用,这凸显了我们的发现在进化方面的意义。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Moesin contributes to heat shock gene response through direct binding to the Med15 subunit of the Mediator complex in the nucleus.

The members of the evolutionary conserved actin-binding Ezrin, Radixin and Moesin (ERM) protein family are involved in numerous key cellular processes in the cytoplasm. In the last decades, ERM proteins, like actin and other cytoskeletal components, have also been shown to be functional components of the nucleus; however, the molecular mechanism behind their nuclear activities remained unclear. Therefore, our primary aim was to identify the nuclear protein interactome of the single Drosophila ERM protein, Moesin. We demonstrate that Moesin directly interacts with the Mediator complex through direct binding to its Med15 subunit, and the presence of Moesin at the regulatory regions of the Hsp70Ab heat shock gene was found to be Med15-dependent. Both Moesin and Med15 bind to heat shock factor (Hsf), and they are required for proper Hsp gene expression under physiological conditions. Moreover, we confirmed that Moesin, Med15 and Hsf are able to bind the monomeric form of actin and together they form a complex in the nucleus. These results elucidate a mechanism by which ERMs function within the nucleus. Finally, we present the direct interaction of the human orthologues of Drosophila Moesin and Med15, which highlights the evolutionary significance of our finding.

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来源期刊
Open Biology
Open Biology BIOCHEMISTRY & MOLECULAR BIOLOGY-
CiteScore
10.00
自引率
1.70%
发文量
136
审稿时长
6-12 weeks
期刊介绍: Open Biology is an online journal that welcomes original, high impact research in cell and developmental biology, molecular and structural biology, biochemistry, neuroscience, immunology, microbiology and genetics.
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