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The role of Bni5 in the regulation of septin higher-order structure formation

机译:Bni5在调控Septin高阶结构形成中的作用

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Septins are a family of conserved cytoskeletal proteins playing an essential role in cytokinesis and in many other cellular processes in fungi and animals. In budding yeast Saccharomyces cerevisiae, septins form filaments and higher-order structures at the mother-bud neck depending on the particular stage of the cell cycle. Septin structures at the division plane serve as a scaffold to recruit the proteins required for particular cellular processes. The formation and localization of septin structures at particular stages of the cell cycle also determine functionality of these proteins. Many different proteins participate in regulating septin assembly. Despite recent developments, we are only beginning to understand how specific protein-protein interactions lead to changes in the polymerization of septin filaments or assembly of higher-order structures. Here, using fluorescence and electron microscopy, we found that Bni5 crosslinks septin filaments into networks by bridging pairs or multiple filaments, forming structures that resemble railways. Furthermore, Bni5 appears to be a substrate of the Elm1 protein kinase in vitro. Moreover, Elm1 induces in the presence of Bni5 disassembly of long septin filaments, suggesting that these proteins may participate in the hourglass to double ring transition. This work gives new insight into the regulatory role of Bni5 in the structural changes of septins.
机译:Septins是一类保守的细胞骨架蛋白,在真菌和动物的胞质分裂和许多其他细胞过程中起着至关重要的作用。在出芽的酿酒酵母中,视细胞周期的特定阶段而定,隔膜在母芽颈处形成细丝和更高阶的结构。分裂平面上的Septin结构充当支架,以募集特定细胞过程所需的蛋白质。隔膜蛋白结构在细胞周期特定阶段的形成和定位也决定了这些蛋白质的功能。许多不同的蛋白质参与调节Septin组装。尽管有最新进展,我们才刚刚开始了解特定的蛋白质-蛋白质相互作用如何导致Septin丝聚合或高阶结构组装中的变化。在这里,使用荧光和电子显微镜,我们发现Bni5通过桥接成对的或多根细丝,将septin细丝交联成网络,形成类似于铁路的结构。此外,Bni5似乎是体外Elm1蛋白激酶的底物。此外,Elm1会在Bni5分离的情况下诱导长的Septin长丝分解,提示这些蛋白质可能参与了沙漏到双环的过渡。这项工作为Bni5在Septins结构变化中的调控作用提供了新的见解。

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