Szuba, A, Bano, F, Castro Linares, G et al. (5 more authors) (2021) Membrane binding controls ordered self-assembly of animal septins. eLife, 10. ISSN 2050-084X
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 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.
Metadata
Item Type: | Article |
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Authors/Creators: |
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Copyright, Publisher and Additional Information: | © 2021, Szuba et al. This article is distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use and redistribution provided that the original author and source are credited. |
Dates: |
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Institution: | The University of Leeds |
Academic Units: | The University of Leeds > Faculty of Biological Sciences (Leeds) > School of Biomedical Sciences (Leeds) |
Funding Information: | Funder Grant number EU - European Union GA 306435 BBSRC (Biotechnology & Biological Sciences Research Council) BB/R000174/1 |
Depositing User: | Symplectic Publications |
Date Deposited: | 14 May 2021 10:56 |
Last Modified: | 14 May 2021 10:56 |
Status: | Published |
Publisher: | eLife Sciences Publications |
Identification Number: | 10.7554/elife.63349 |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:173955 |