The hierarchical assembly of septins revealed by high-speed AFM

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10.1038/s41467-020-18778-x
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Abstract
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.
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© The Author(s), 2020. This article is distributed under the terms of the Creative Commons Attribution License. The definitive version was published in Jiao, F., Cannon, K. S., Lin, Y. C., Gladfelter, A. S., & Scheuring, S. The hierarchical assembly of septins revealed by high-speed AFM. Nature Communications, 11(1), (2020): 5062, doi:10.1038/s41467-020-18778-x.
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Jiao, F., Cannon, K. S., Lin, Y. C., Gladfelter, A. S., & Scheuring, S. (2020). The hierarchical assembly of septins revealed by high-speed AFM. Nature Communications, 11(1), 5062.
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