Unraveling the mechanisms and evolution of a two-domain module in IQGAP proteins for controlling eukaryotic cytokinesis.

Unraveling the mechanisms and evolution of a two-domain module in IQGAP proteins for controlling eukaryotic cytokinesis.
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DOI:
10.1016/j.celrep.2023.113510
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发表时间:
2023-12-26
期刊:
影响因子:
8.8
通讯作者:
Bi E
Bi E
中科院分区:
生物学1区
文献类型:
--
作者:
Wang K;Okada H;Wloka C;Bi E

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IQGAP蛋白家族在不同生物体的胞质分裂中起着至关重要的作用,但其潜在的机制尚不完全清楚。在这项研究中,我们证明了在萌芽酵母、分裂酵母和人类细胞中,IQGAP使用一个双结构域模块来调节它们的定位以及胞质分裂过程中肌动球蛋白环的组装和拆卸。值得注意的是,这些IQGAP中的钙蛋白同源结构域(CHD)以不同的特异性与不同的细胞F-肌动蛋白结构结合,而这些IQGAP中紧邻CHD下游的非保守结构域都针对分裂位点,但在时机、定位强度和结合伙伴方面有所不同。我们还证明了人类IQGAP3与肌球蛋白和肌球蛋白-II的作用类似,在胞质分裂中介导了香草素的作用。总体而言,我们的发现强调了IQGAP调节远缘生物胞质分裂的两个结构域的机制以及它们的进化保守和分歧。IQGAP蛋白家族如何在胞质分裂中发挥作用还不是很清楚。Wang等人。据报道,来自萌芽酵母、分裂酵母和哺乳动物细胞的IQGAP使用双域策略来控制它们自己的定位以及胞质分裂过程中肌动球蛋白环的组装和功能。
The IQGAP family of proteins plays a crucial role in cytokinesis across diverse organisms, but the underlying mechanisms are not fully understood. In this study, we demonstrate that IQGAPs in budding yeast, fission yeast, and human cells use a two-domain module to regulate their localization as well as the assembly and disassembly of the actomyosin ring during cytokinesis. Strikingly, the calponin homology domains (CHDs) in these IQGAPs bind to distinct cellular F-actin structures with varying specificity, whereas the non-conserved domains immediately downstream of the CHDs in these IQGAPs all target the division site, but differ in timing, localization strength, and binding partners. We also demonstrate that human IQGAP3 acts in parallel to septins and myosin-IIs to mediate the role of anillin in cytokinesis. Collectively, our findings highlight the two-domain mechanism by which IQGAPs regulate cytokinesis in distantly related organisms as well as their evolutionary conservation and divergence. How the IQGAP family of proteins functions in cytokinesis is not well understood. Wang et al. report that IQGAPs from budding yeast, fission yeast, and mammalian cells use a two-domain strategy to control their own localization as well as the assembly and function of the actomyosin ring during cytokinesis.
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