Membrane binding controls ordered self-assembly of animal septins.


Journal

eLife
ISSN: 2050-084X
Titre abrégé: Elife
Pays: England
ID NLM: 101579614

Informations de publication

Date de publication:
13 04 2021
Historique:
received: 22 09 2020
accepted: 12 04 2021
pubmed: 14 4 2021
medline: 27 10 2021
entrez: 13 4 2021
Statut: epublish

Résumé

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.

Identifiants

pubmed: 33847563
doi: 10.7554/eLife.63349
pii: 63349
pmc: PMC8099429
doi:
pii:

Substances chimiques

Drosophila Proteins 0
Lipid Bilayers 0
Membrane Lipids 0
Microfilament Proteins 0
pnut protein, Drosophila 0
Septins EC 3.6.1.-

Types de publication

Journal Article Research Support, Non-U.S. Gov't Video-Audio Media

Langues

eng

Sous-ensembles de citation

IM

Subventions

Organisme : Biotechnology and Biological Sciences Research Council
ID : BB/R000174/1
Pays : United Kingdom

Informations de copyright

© 2021, Szuba et al.

Déclaration de conflit d'intérêts

AS, FB, GC, FI, MM, RR, AB, GK No competing interests declared

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Auteurs

Agata Szuba (A)

AMOLF, Department of Living Matter, Biological Soft Matter group, Amsterdam, Netherlands.

Fouzia Bano (F)

School of Biomedical Sciences, Faculty of Biological Sciences, Astbury Centre for Structural Molecular Biology, University of Leeds, Leeds, United Kingdom.
School of Physics and Astronomy, Faculty of Engineering and Physical Sciences, University of Leeds, Leeds, United Kingdom.
Bragg Centre for Materials Research, University of Leeds, Leeds, United Kingdom.

Gerard Castro-Linares (G)

AMOLF, Department of Living Matter, Biological Soft Matter group, Amsterdam, Netherlands.
Department of Bionanoscience, Kavli Institute of Nanoscience Delft, Delft University of Technology, Delft, Netherlands.

Francois Iv (F)

Institut Fresnel, CNRS, Aix-Marseille Univ, Centrale Marseille, Marseille, France.

Manos Mavrakis (M)

Institut Fresnel, CNRS, Aix-Marseille Univ, Centrale Marseille, Marseille, France.

Ralf P Richter (RP)

School of Biomedical Sciences, Faculty of Biological Sciences, Astbury Centre for Structural Molecular Biology, University of Leeds, Leeds, United Kingdom.
School of Physics and Astronomy, Faculty of Engineering and Physical Sciences, University of Leeds, Leeds, United Kingdom.
Bragg Centre for Materials Research, University of Leeds, Leeds, United Kingdom.

Aurélie Bertin (A)

Laboratoire Physico Chimie Curie, Institut Curie, PSL Research University, Paris, France.
Sorbonne Université, Paris, France.

Gijsje H Koenderink (GH)

AMOLF, Department of Living Matter, Biological Soft Matter group, Amsterdam, Netherlands.
Department of Bionanoscience, Kavli Institute of Nanoscience Delft, Delft University of Technology, Delft, Netherlands.

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