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    Membrane binding controls ordered selfassembly of animal septins

    Year: 2021

    Journal: eLife, Volume 10, APR 13

    Authors: Szuba, Agata; Bano, Fouzia; Castro-Linares, Gerard; Iv, Francois; Mavrakis, Manos; Richter, Ralf P.; Bertin, Aurelie; Koenderink, Gijsje H.

    Organizations: H2020 European Research Council [ERC StG 335672 MINICELL, ERC StG 306435 JELLY]; Biotechnology and Biological Sciences Research Council [BB/R000174/1]; Agence Nationale de la Recherche [ANR-13-JSV8-0002-01, ANR-17-CE13-0014]; Fondation ARC pour la Recherche sur le Cancer [PJA 20151203182]; Nederlandse Organisatie voor Wetenschappelijk Onderzoek [024.003.019]

    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 that binding to flat lipid membranes requires electrostatic interactions of septins with anionic lipids and promotes the ordered self-assembly of fly septins into filamentous meshworks. Transmission electron microscopy reveals that both fly and mammalian septin hexamers form arrays of single and paired filaments. Atomic force microscopy and quartz crystal microbalance demonstrate that the fly filaments form mechanically rigid, 12- to 18-nm thick, double layers of septins. By contrast, C-terminally truncated septin mutants form 4-nm thin monolayers, indicating that stacking requires the C-terminal coiled coils on DSep2 and Pnut subunits. Our work shows that membrane binding is required for fly septins to form ordered arrays of single and paired filaments and provides new insights into the mechanisms by which septins may regulate cell surface mechanics.
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