Septin higher-order structure on yeast membranes in vitro

James A. Goodchild, Brandy N. Curtis, Yangang Pan, Yining Jiang, Fang Jiao, Amy S. Gladfelter and Simon Scheuring ()
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James A. Goodchild: Department of Anesthesiology
Brandy N. Curtis: Department of Biochemistry and Biophysics
Yangang Pan: Department of Anesthesiology
Yining Jiang: Department of Anesthesiology
Fang Jiao: Chinese Academy of Sciences
Amy S. Gladfelter: Department of Cell Biology
Simon Scheuring: Department of Anesthesiology

Nature Communications, 2025, vol. 16, issue 1, 1-11

Abstract: Abstract Septins are cytoskeletal proteins that form filaments and higher-order structures, and remodel membranes in a variety of processes. Structural and cell biological studies provided atomic- and micro-scale details, but the understanding of septin assembly at the mesoscale is limited. Here, we used high-speed atomic force microscopy (HS-AFM) to analyze yeast septin assembly on yeast supported lipid bilayers (SLBs). We found the coexistence of three lipid phases in yeast membranes, where septin polymerized selectively on the liquid-disordered phase. Septin filaments adhered to membranes with a conserved face; and paired filaments, previously reported in less native environments, were not observed. Additionally, septin filaments exhibited lateral and longitudinal alignment. We used HS-AFM force-sweep experiments to disrupt septin structures and observe organizational recovery through self-templating. Finally, septin filaments stacked, where higher layer filament alignment was templated by the layer below. Thus, septins encode their 3D-structural organization, likely tunable by the membrane and bulk environment.

Date: 2025
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DOI: 10.1038/s41467-025-60344-w

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