Membrane binding controls ordered self-assembly of animal septins

Septin Cell Cortex Cell membrane
DOI: 10.7554/elife.63349 Publication Date: 2021-04-13T12:19:00Z
ABSTRACT
Septins are conserved cytoskeletal proteins that regulate cell cortex mechanics. The mechanisms of their interactions with the plasma membrane remain poorly understood. Here, we show by cell-free reconstitution binding to flat lipid membranes requires electrostatic septins anionic lipids and promotes ordered self-assembly fly into filamentous meshworks. Transmission electron microscopy reveals both mammalian septin hexamers form arrays single paired filaments. Atomic force quartz crystal microbalance demonstrate filaments mechanically rigid, 12- 18-nm thick, double layers septins. By contrast, C-terminally truncated mutants 4-nm thin monolayers, indicating stacking C-terminal coiled coils on DSep2 Pnut subunits. Our work shows is required for provides new insights which may surface
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