The hierarchical assembly of septins revealed by high-speed AFM.

The hierarchical assembly of septins revealed by high-speed AFM.
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DOI:
10.1038/s41467-020-18778-x
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发表时间:
2020-10-08
影响因子:
16.6
通讯作者:
Scheuring S
Scheuring S
中科院分区:
综合性期刊1区
文献类型:
--
作者:
Jiao F;Cannon KS;Lin YC;Gladfelter AS;Scheuring S

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septin是gtp结合蛋白,参与多种细胞过程,包括分裂和膜重塑。septin形成线性,回文异质复合物,可以在细丝和高阶结构中组装。结构研究揭示了多种septin结构,但关于装配动力学和路径的问题仍然存在。在这里,我们使用高速原子力显微镜(HS-AFM)和动力学建模,使我们能够确定septin丝的组装是一个扩散驱动的过程,而高阶结构的形成是复杂的,并且涉及自模板。微酸性的pH值和增加的单价离子浓度有利于细丝的组装、排列和配对。细丝对准和配对进一步有利于扩散驱动组装。配对是由隔素n端面介导的,可能对称或交错发生,可能对不同形状的高阶结构的形成很重要。多层结构通过底层的形态来模板化。分隔素c端面,即Cdc12的c端延伸,可能参与了膜结合。septin是gtp结合蛋白,参与多种细胞过程,包括分裂、极性维持和膜重塑。本文作者利用高速原子力显微镜发现,septin丝的组装是一个扩散驱动的过程,而septin的高阶组装涉及septin的自模板
Septins are GTP-binding proteins involved in diverse cellular processes including division and membrane remodeling. Septins form linear, palindromic heteromeric complexes that can assemble in filaments and higher-order structures. Structural studies revealed various septin architectures, but questions concerning assembly-dynamics and -pathways persist. Here we used high-speed atomic force microscopy (HS-AFM) and kinetic modeling which allowed us to determine that septin filament assembly was a diffusion-driven process, while formation of higher-order structures was complex and involved self-templating. Slightly acidic pH and increased monovalent ion concentrations favor filament-assembly, -alignment and -pairing. Filament-alignment and -pairing further favored diffusion-driven assembly. Pairing is mediated by the septin N-termini face, and may occur symmetrically or staggered, likely important for the formation of higher-order structures of different shapes. Multilayered structures are templated by the morphology of the underlying layers. The septin C-termini face, namely the C-terminal extension of Cdc12, may be involved in membrane binding. Septins are GTP-binding proteins involved in diverse cellular processes including division, polarity maintenance and membrane remodeling. Here authors use high-speed atomic force microscopy to show that assembly of septin filaments is a diffusion-driven process, while septin assembly into higher-order involves septin self-templating
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