Evidence map›Paper›PMID 29691404›Full record

ArticleNature communications2018

Capping protein-controlled actin polymerization shapes lipid membranes.

Katharina Dürre, Felix C Keber, Philip Bleicher, Fridtjof Brauns, Christian J Cyron, Jan Faix, Andreas R Bausch

Abstract read
In one paragraph

Article in Nature communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing 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

42 citing papers in PubMed.

  1. Article
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  9. Review
  10. Filament transport supports contractile steady states of actin networks.bioRxiv : the preprint server for biology · 2025
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  11. Review
  12. Article
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  17. Review
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  19. Article
  20. Membrane-dependent actin polymerization mediated by thebioRxiv : the preprint server for biology · 2023
    Article
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

7 authors.

Katharina DürreLehrstuhl für Zellbiophysik, Technische Universität München, James-Franck-Str. 1, D-85748, Garching, Germany.
Felix C KeberLehrstuhl für Zellbiophysik, Technische Universität München, James-Franck-Str. 1, D-85748, Garching, Germany.
Philip BleicherLehrstuhl für Zellbiophysik, Technische Universität München, James-Franck-Str. 1, D-85748, Garching, Germany.
Fridtjof BraunsArnold Sommerfeld Center for Theoretical Physics and Center for NanoScience, Department of Physics, Ludwig-Maximilians-Universität München, Theresienstraße 37, D-80333, München, Germany.
Christian J CyronLehrstuhl für Numerische Mechanik, Technische Universität München, Boltzmannstraße 15, D-85748, Garching, Germany.
Jan FaixInstitut für Biophysikalische Chemie, Medizinische Hochschule Hannover, Carl-Neuberg Straße 1, D-30625, Hannover, Germany.ORCID http://orcid.org/0000-0003-1803-9192
Andreas R BauschLehrstuhl für Zellbiophysik, Technische Universität München, James-Franck-Str. 1, D-85748, Garching, Germany. abausch@mytum.de.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Arp2/3 complex-mediated actin assembly at cell membranes drives the formation of protrusions or endocytic vesicles. To identify the mechanism by which different membrane deformations can be achieved, we reconstitute the basic membrane deformation modes of inward and outward bending in a confined geometry by encapsulating a minimal set of cytoskeletal proteins into giant unilamellar vesicles. Formation of membrane protrusions is favoured at low capping protein (CP) concentrations, whereas the formation of negatively bent domains is promoted at high CP concentrations. Addition of non-muscle myosin II results in full fission events in the vesicle system. The different deformation modes are rationalized by simulations of the underlying transient nature of the reaction kinetics. The relevance of the regulatory mechanism is supported by CP overexpression in mouse melanoma B16-F1 cells and therefore demonstrates the importance of the quantitative understanding of microscopic kinetic balances to address the diverse functionality of the cytoskeleton.

Indexed as

Actin Capping ProteinsActin-Related Protein 2-3 ComplexActinsAnimalsCell Line, TumorCytoskeletonMiceMyosin Type IIPolymerizationRabbitsSwineActin Capping ProteinsActin-Related Protein 2-3 ComplexActinsMyosin Type II

Identifiers

PMID29691404
PMCPMC5915599

What OpenQuestion holds

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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 OpenQuestion graph.