A direct interaction between the RNA-binding proteins Staufen and Tm1-I/C in the oskar mRNA transport complex.

IF 7.5 1区生物学 Q1 CELL BIOLOGY

Cell reports Pub Date : 2025-06-25 DOI:10.1016/j.celrep.2025.115906

Thomas Gaber, Thomas Monecke, Julia Grabowski, Bernd Simon, Tobias Williams, Vera Roman, Jeffrey Chao, Janosch Hennig, Anne Ephrussi, Dierk Niessing, Simone Heber

引用次数: 0

Abstract

In the Drosophila female germline, oskar messenger RNA is transported on microtubules from the nurse cells to the posterior pole of the oocyte, where it is translated. Transport of oskar transcripts from the nurse cells into the oocyte requires dynein, while localization of the mRNAs within the oocyte to the posterior pole is dependent upon kinesin-1. Staufen, a double-stranded RNA (dsRNA)-binding protein, has been shown to bind the oskar mRNA transport complex in the oocyte and inactivate dynein; however, it remains unclear how kinesin is activated. Here, using surface plasmon resonance, nuclear magnetic resonance spectroscopy, and RNA imaging within egg chambers, we demonstrate that Staufen directly interacts with Tropomyosin1-I/C (Tm1), a non-canonical kinesin adaptor. This work provides molecular evidence of how Staufen integrates into the oskar messenger ribonucleoprotein (mRNP) complex.

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oskar mRNA转运复合体中rna结合蛋白Staufen和Tm1-I/C之间的直接相互作用。

在果蝇雌性生殖系中，oskar信使RNA通过微管从育母细胞转运到卵母细胞的后极，并在那里被翻译。将oskar转录本从乳母细胞转运到卵母细胞需要动力蛋白，而将卵母细胞内的mrna定位到后极则取决于动力蛋白-1。Staufen是一种双链RNA （dsRNA）结合蛋白，已被证明可以结合卵母细胞中的oskar mRNA转运复合物并使动力蛋白失活；然而，目前还不清楚运动蛋白是如何被激活的。在这里，利用表面等离子体共振、核磁共振波谱和卵腔内的RNA成像，我们证明了Staufen直接与原肌球蛋白1- i /C （Tm1）相互作用，这是一种非规范的激酶受体。这项工作为Staufen如何融入奥斯卡信使核糖核蛋白（mRNP）复合体提供了分子证据。

本文章由计算机程序翻译，如有差异，请以英文原文为准。

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来源期刊

Cell reports CELL BIOLOGY-

CiteScore

13.80

自引率

1.10%

发文量

1305

审稿时长

77 days

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