Evidence map›Paper›PMID 33859190›Full record

ArticleNature communications2021

Reconstitution of contractile actomyosin rings in vesicles.

Thomas Litschel, Charlotte F Kelley, Danielle Holz, Maral Adeli Koudehi, Sven K Vogel, Laura Burbaum, Naoko Mizuno, Dimitrios Vavylonis, Petra Schwille

Erratum issuedAbstract read
In one paragraph

Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 70 papers.

0numbers the graph read from it
0cells of the map it votes in
70citing papers in PubMed
–field-weighted citation impact
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

70 citing papers in PubMed.

  1. Devising a divisome for synthetic cells.Nature reviews. Chemistry · 2026
    Review
  2. Article
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  13. Review
  14. Building a Synthetic Cell Together.Nature communications · 2025
    Review
  15. Article
  16. Article
  17. Review
  18. Article
  19. Review
  20. Article

10 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

9 authors.

Thomas LitschelDepartment of Cellular and Molecular Biophysics, Max Planck Institute of Biochemistry, Martinsried, Germany.ORCID http://orcid.org/0000-0001-7123-8364
Charlotte F KelleyDepartment of Cellular and Molecular Biophysics, Max Planck Institute of Biochemistry, Martinsried, Germany.ORCID http://orcid.org/0000-0002-7684-9049
Danielle HolzDepartment of Physics, Lehigh University, Bethlehem, PA, USA.
Maral Adeli KoudehiDepartment of Physics, Lehigh University, Bethlehem, PA, USA.
Sven K VogelDepartment of Cellular and Molecular Biophysics, Max Planck Institute of Biochemistry, Martinsried, Germany.
Laura BurbaumDepartment of Cellular and Molecular Biophysics, Max Planck Institute of Biochemistry, Martinsried, Germany.
Naoko MizunoDepartment of Structural Cell Biology, Max Planck Institute of Biochemistry, Martinsried, Germany.ORCID http://orcid.org/0000-0002-1594-2821
Dimitrios VavylonisDepartment of Physics, Lehigh University, Bethlehem, PA, USA.
Petra SchwilleDepartment of Cellular and Molecular Biophysics, Max Planck Institute of Biochemistry, Martinsried, Germany. schwille@biochem.mpg.de.ORCID http://orcid.org/0000-0002-6106-4847

Funding

Molecular organization of pathways governing cell-shape formationZIAHL006264 · NHLBI · NATIONAL HEART, LUNG, AND BLOOD INSTITUTE · PI MIZUNO, NAOKO · 2021 to 2025
$11.6M
Modeling mechanisms in cytokinesis, cell polarization and motilityR35GM136372 · NIGMS · LEHIGH UNIVERSITY · PI Dimitrios Vavylonis · 2020 to 2026
$3.2M
Theoretical and experimental studies of distributed actin turnoverR01GM114201 · NIGMS · LEHIGH UNIVERSITY · PI VAVYLONIS, DIMITRIOS · 2016 to 2019
$1.1M
NIGMS NIH HHS R01 GM114201NIGMS NIH HHS R35 GM136372
6 · The paper itself

Abstract

One of the grand challenges of bottom-up synthetic biology is the development of minimal machineries for cell division. The mechanical transformation of large-scale compartments, such as Giant Unilamellar Vesicles (GUVs), requires the geometry-specific coordination of active elements, several orders of magnitude larger than the molecular scale. Of all cytoskeletal structures, large-scale actomyosin rings appear to be the most promising cellular elements to accomplish this task. Here, we have adopted advanced encapsulation methods to study bundled actin filaments in GUVs and compare our results with theoretical modeling. By changing few key parameters, actin polymerization can be differentiated to resemble various types of networks in living cells. Importantly, we find membrane binding to be crucial for the robust condensation into a single actin ring in spherical vesicles, as predicted by theoretical considerations. Upon force generation by ATP-driven myosin motors, these ring-like actin structures contract and locally constrict the vesicle, forming furrow-like deformations. On the other hand, cortex-like actin networks are shown to induce and stabilize deformations from spherical shapes.

Indexed as

Models, BiologicalActomyosinAnimalsCell DivisionCell LineDrosophilaHumansIntravital MicroscopyMicroscopy, ConfocalModels, MolecularRecombinant ProteinsSynthetic BiologyUnilamellar LiposomesActomyosinRecombinant ProteinsUnilamellar Liposomes

Identifiers

PMID33859190
PMCPMC8050101

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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 OpenQuestion graph.