Evidence map›Paper›PMID 33847563›Full record

ArticleeLife2021

Membrane binding controls ordered self-assembly of animal septins.

Agata Szuba, Fouzia Bano, Gerard Castro-Linares, Francois Iv, Manos Mavrakis, Ralf P Richter, Aurélie Bertin, Gijsje H Koenderink

Open access · goldAbstract readVideo-Audio Media
In one paragraph

Article in eLife, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
6.0field-weighted citation impact, top 2% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

25 citing papers in PubMed, 68 citations in OpenAlex.

  1. Article
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  5. Article
  6. Optimization of Protoplast Preparation Conditions inJournal of fungi (Basel, Switzerland) · 2024
    Article
  7. Article
  8. Review
  9. Septin Organization and Dynamics for Budding Yeast Cytokinesis.Journal of fungi (Basel, Switzerland) · 2024
    Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Curvature sensing as an emergent property of multiscale assembly of septins.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  19. Article
  20. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

8 authors at 4 institutions in 3 countries.

Agata SzubaAMOLF, Department of Living Matter, Biological Soft Matter group, Amsterdam, Netherlands.
Fouzia BanoSchool of Biomedical Sciences, Faculty of Biological Sciences, Astbury Centre for Structural Molecular Biology, University of Leeds, Leeds, United Kingdom.ORCID 0000-0003-0634-7091
Gerard Castro-LinaresAMOLF, Department of Living Matter, Biological Soft Matter group, Amsterdam, Netherlands.
Francois IvInstitut Fresnel, CNRS, Aix-Marseille Univ, Centrale Marseille, Marseille, France.
Manos MavrakisInstitut Fresnel, CNRS, Aix-Marseille Univ, Centrale Marseille, Marseille, France.
Ralf P RichterSchool of Biomedical Sciences, Faculty of Biological Sciences, Astbury Centre for Structural Molecular Biology, University of Leeds, Leeds, United Kingdom.ORCID 0000-0003-3071-2837
Aurélie BertinLaboratoire Physico Chimie Curie, Institut Curie, PSL Research University, Paris, France.ORCID 0000-0002-3400-6887
Gijsje H KoenderinkAMOLF, Department of Living Matter, Biological Soft Matter group, Amsterdam, Netherlands.ORCID 0000-0002-7823-8807
Institute for Atomic and Molecular Physics · NLCentre National de la Recherche Scientifique · FRUniversity of Leeds · GBUniversité Paris Sciences et Lettres · FR

Funding

Biotechnology and Biological Sciences Research Council BB/R000174/1
6 · The paper itself

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.

Indexed as

AnimalsAnimals, Genetically ModifiedCell MembraneCryoelectron MicroscopyDrosophila melanogasterDrosophila ProteinsHumansLipid BilayersMembrane LipidsMicrofilament ProteinsMicroscopy, Atomic ForceMicroscopy, Electron, TransmissionProtein BindingProtein ConformationProtein MultimerizationQuartz Crystal Microbalance TechniquesDrosophila ProteinsLipid BilayersMembrane LipidsMicrofilament Proteinspnut protein, DrosophilaSeptinscell biologycell surface mechanicscortexcytoskeletonD. melanogasterhumanmolecular biophysicsplasma membranestructural biology

Identifiers

PMID33847563
PMCPMC8099429
OpenAlexW3154763487

What Socratic holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the Socratic graph.