Evidence map›Paper›PMID 18326652›Full record

ArticleBiophysical journal2008

Arp2/3 controls the motile behavior of N-WASP-functionalized GUVs and modulates N-WASP surface distribution by mediating transient links with actin filaments.

Vincent Delatour, Emmanuèle Helfer, Dominique Didry, Kim Hô Diêp Lê, Jean-François Gaucher, Marie-France Carlier, Guillaume Romet-Lemonne

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
2.8field-weighted citation impact, top 10% 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

22 citing papers in PubMed, 51 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Cytoskeleton Force Exertion in Bulk Cytoplasm.Frontiers in cell and developmental biology · 2020
    Review
  5. Article
  6. Article
  7. Actomyosin dynamics drive local membrane component organization in an in vitro active composite layer.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  8. Control of polarized assembly of actin filaments in cell motility.Cellular and molecular life sciences : CMLS · 2015
    Review
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Actin disassembly 'clock' and membrane tension determine cell shape and turning: a mathematical model.Journal of physics. Condensed matter : an Institute of Physics journal · 2010
    Article
  17. Article
  18. 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

7 authors at 3 institutions in 1 country.

Vincent DelatourCytoskeleton Dynamics and Motility, Laboratoire d'Enzymologie et Biochimie Structurales, Centre National de la Recherche Scientifique, Gif-sur-Yvette, France.
Emmanuèle Helfer
Dominique Didry
Kim Hô Diêp Lê
Jean-François Gaucher
Marie-France Carlier
Guillaume Romet-Lemonne
Laboratoire d'Enzymologie et Biochimie Structurales · FRCentre National de la Recherche Scientifique · FRUniversité Paris Cité · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Spatially controlled assembly of actin in branched filaments generates cell protrusions or the propulsion of intracellular vesicles and pathogens. The propulsive movement of giant unilamellar vesicles (GUVs) functionalized by N-WASP (full-length or truncated) is reconstituted in a biochemically controlled medium, and analyzed using phase contrast and fluorescence microscopy to elucidate the links between membrane components and the actin cytoskeleton that determine motile behavior. Actin-based propulsion displays a continuous regime or a periodic saltatory regime. The transition between the two regimes is controlled by the concentration of Arp2/3 complex, which branches filaments by interacting with N-WASP at the liposome surface. Saltatory motion is linked to cycles in the distribution of N-WASP at the membrane between a homogeneous and a segregated state. Comparison of the changes in distribution of N-WASP, Arp2/3, and actin during propulsion demonstrates that actin filaments bind to N-WASP, and that these bonds are transitory. This interaction, mediated by Arp2/3, drives N-WASP segregation. VC-fragments of N-WASP, that interact more weakly than N-WASP with the Arp2/3 complex, segregate less than N-WASP at the rear of the GUVs. GUV propulsion is inhibited by the presence of VCA-actin covalent complex, showing that the release of actin from the nucleator is required for movement. The balance between segregation and free diffusion determines whether continuous movement can be sustained. Computed surface distributions of N-WASP, derived from a theoretical description of this segregation-diffusion mechanism, account satisfactorily for the measured density profiles of N-WASP, Arp2/3 complex, and actin.

Indexed as

Actin CytoskeletonActin-Related Protein 2-3 ComplexBinding SitesMolecular Motor ProteinsMotionProtein BindingProtein ConformationSurface PropertiesUnilamellar LiposomesWiskott-Aldrich Syndrome Protein, NeuronalActin-Related Protein 2-3 ComplexMolecular Motor ProteinsUnilamellar LiposomesWiskott-Aldrich Syndrome Protein, Neuronal

Identifiers

PMID18326652
PMCPMC2397363
OpenAlexW2072866301

What OpenQuestion holds

Textmetadata
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.