Evidence map›Paper›PMID 17182858›Full record

ArticleMolecular biology of the cell2007

Villin severing activity enhances actin-based motility in vivo.

Céline Revenu, Matthieu Courtois, Alphée Michelot, Cécile Sykes, Daniel Louvard, Sylvie Robine

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
0.5field-weighted citation impact, top 36% 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

21 citing papers in PubMed, 33 citations in OpenAlex.

  1. Article
  2. Article
  3. Bioinformatics analyses of the proteome ofFrontiers in immunology · 2025
    Article
  4. Article
  5. Article
  6. Article
  7. Charge-dependent interactions of monomeric and filamentous actin with lipid bilayers.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Enterocyte loss of polarity and gut wound healing rely upon the F-actin-severing function of villin.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. Review
  20. New insights into mechanism and regulation of actin capping protein.International review of cell and molecular biology · 2008
    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

6 authors at 1 institution in 1 country.

Céline RevenuLaboratoire de Morphogenèse et Signalisation Cellulaires, Unité Mixte de Recherche 144, Centre National de la Recherche Scientifique/Institut Curie, 75248 Paris Cedex 05, France.
Matthieu Courtois
Alphée Michelot
Cécile Sykes
Daniel Louvard
Sylvie Robine
Centre National de la Recherche Scientifique · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Villin, an actin-binding protein associated with the actin bundles that support microvilli, bundles, caps, nucleates, and severs actin in a calcium-dependant manner in vitro. We hypothesized that the severing activity of villin is responsible for its reported role in enhancing cell plasticity and motility. To test this hypothesis, we chose a loss of function strategy and introduced mutations in villin based on sequence comparison with CapG. By pyrene-actin assays, we demonstrate that this mutant has a strongly reduced severing activity, whereas nucleation and capping remain unaffected. The bundling activity and the morphogenic effects of villin in cells are also preserved in this mutant. We thus succeeded in dissociating the severing from the three other activities of villin. The contribution of villin severing to actin dynamics is analyzed in vivo through the actin-based movement of the intracellular bacteria Shigella flexneri in cells expressing villin and its severing variant. The severing mutations abolish the gain of velocity induced by villin. To further analyze this effect, we reconstituted an in vitro actin-based bead movement in which the usual capping protein is replaced by either the wild type or the severing mutant of villin. Confirming the in vivo results, villin-severing activity enhances the velocity of beads by more than two-fold and reduces the density of actin in the comets. We propose a model in which, by severing actin filaments and capping their barbed ends, villin increases the concentration of actin monomers available for polymerization, a mechanism that might be paralleled in vivo when an enterocyte undergoes an epithelio-mesenchymal transition.

Indexed as

Cell MovementActin Capping ProteinsActin CytoskeletonActinsAmino Acid SequenceAnimalsDogsHumansMicrofilament ProteinsMicrospheresModels, BiologicalMolecular Sequence DataMutant ProteinsMutationRabbitsShigella flexneriActin Capping ProteinsActinsMicrofilament ProteinsMutant Proteinsvillin

Identifiers

PMID17182858
PMCPMC1805090
OpenAlexW2103783368

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.