The hierarchical assembly of septins revealed by high-speed AFM

Fang Jiao, Kevin S. Cannon, Yi-Chih Lin, Amy S. Gladfelter and Simon Scheuring ()
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Fang Jiao: Weill Cornell Medicine
Kevin S. Cannon: University of North Carolina and Chapel Hill
Yi-Chih Lin: Weill Cornell Medicine
Amy S. Gladfelter: University of North Carolina and Chapel Hill
Simon Scheuring: Weill Cornell Medicine

Nature Communications, 2020, vol. 11, issue 1, 1-13

Abstract: 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.

Date: 2020
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DOI: 10.1038/s41467-020-18778-x

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