The Structural Biology of Septins and Their Filaments: An Update.

The Structural Biology of Septins and Their Filaments: An Update.
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DOI:
10.3389/fcell.2021.765085
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发表时间:
2021
影响因子:
5.5
通讯作者:
Garratt RC
Garratt RC
中科院分区:
生物学2区
文献类型:
--
作者:
Cavini IA;Leonardo DA;Rosa HVD;Castro DKSV;D'Muniz Pereira H;Valadares NF;Araujo APU;Garratt RC

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为了从机械的角度充分理解任何复杂的生化系统,有必要了解所涉及的分子成分的三维结构。septin及其低聚物、细丝和高阶配合物也不例外。事实上,不同的septin单体沿着丝状物的特定位置自发募集,代表了微妙分子识别的一个迷人的例子。在过去的几年里,关于这些重要的细胞骨架蛋白的结构信息的数量急剧增加。这使得我们可以更详细地描述它们各自的结构域和它们之间形成的不同界面,这是稳定高阶结构(如六聚体、八聚体和完全形成的细丝)的基础。这些结构的灵活性和单个界面的可塑性也开始被理解。此外,最近,已经阐明了细丝如何通过形成涉及c端域的反平行卷曲线圈而束成高阶结构。然而,即使有了这些进展,在我们完全了解septin组装体的结构和动力学如何与其生理作用相关,包括它们与生物膜和其他细胞骨架成分的相互作用之前,还有一段路要走。在这篇综述中,我们的目标是将目前可用的各种结构证据整合到一个更连贯的画面中。虽然说这已经完成有些夸张,但最近的进展似乎表明,这方面正在取得进展。
In order to fully understand any complex biochemical system from a mechanistic point of view, it is necessary to have access to the three-dimensional structures of the molecular components involved. Septins and their oligomers, filaments and higher-order complexes are no exception. Indeed, the spontaneous recruitment of different septin monomers to specific positions along a filament represents a fascinating example of subtle molecular recognition. Over the last few years, the amount of structural information available about these important cytoskeletal proteins has increased dramatically. This has allowed for a more detailed description of their individual domains and the different interfaces formed between them, which are the basis for stabilizing higher-order structures such as hexamers, octamers and fully formed filaments. The flexibility of these structures and the plasticity of the individual interfaces have also begun to be understood. Furthermore, recently, light has been shed on how filaments may bundle into higher-order structures by the formation of antiparallel coiled coils involving the C-terminal domains. Nevertheless, even with these advances, there is still some way to go before we fully understand how the structure and dynamics of septin assemblies are related to their physiological roles, including their interactions with biological membranes and other cytoskeletal components. In this review, we aim to bring together the various strands of structural evidence currently available into a more coherent picture. Although it would be an exaggeration to say that this is complete, recent progress seems to suggest that headway is being made in that direction.
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