Evidence map›Paper›PMID 20150894›Full record

ArticleThe EMBO journal2010

Force generated by actomyosin contraction builds bridges between adhesive contacts.

Olivier M Rossier, Nils Gauthier, Nicolas Biais, Wynn Vonnegut, Marc-Antoine Fardin, Philip Avigan, Evan R Heller, Anurag Mathur, Saba Ghassemi, Michael S Koeckert and 2 more

Open access · greenAbstract read
In one paragraph

Article in The EMBO journal, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 65 papers.

0numbers the graph read from it
0cells of the map it votes in
65citing papers in PubMed
6.5field-weighted citation impact, top 3% 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

65 citing papers in PubMed, 112 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Nanofiber curvature with Rho GTPase activity increases mouse embryonic fibroblast random migration velocity.Integrative biology : quantitative biosciences from nano to macro · 2021
    Article
  9. Microorganisms · 2021
    Article
  10. Article
  11. Article
  12. Cellular Contact Guidance Emerges from Gap Avoidance.Cell reports. Physical science · 2020
    Article
  13. The Research Advance of Cell BridgesFrontiers in bioengineering and biotechnology · 2020
    Review
  14. A Tale of Two States: Normal and Transformed, With and Without Rigidity Sensing.Annual review of cell and developmental biology · 2019
    Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Molecular stretching modulates mechanosensing pathways.Protein science : a publication of the Protein Society · 2017
    Review

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

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

12 authors at 1 institution in 1 country.

Olivier M RossierDepartment of Biological Sciences, Columbia University, New York, NY, USA.
Nils Gauthier
Nicolas Biais
Wynn Vonnegut
Marc-Antoine Fardin
Philip Avigan
Evan R Heller
Anurag Mathur
Saba Ghassemi
Michael S Koeckert
James C Hone
Michael P Sheetz
Columbia University · US

Funding

Nanomedicine development center for mechanobiologyPN2EY016586 · NEI · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI DUSTIN, MICHAEL LORAN · 2005 to 2014
$23.0M
NEI NIH HHS PN2 EY016586
6 · The paper itself

Abstract

Extracellular matrices in vivo are heterogeneous structures containing gaps that cells bridge with an actomyosin network. To understand the basis of bridging, we plated cells on surfaces patterned with fibronectin (FN)-coated stripes separated by non-adhesive regions. Bridges developed large tensions where concave cell edges were anchored to FN by adhesion sites. Actomyosin complexes assembled near those sites (both actin and myosin filaments) and moved towards the centre of the non-adhesive regions in a treadmilling network. Inhibition of myosin-II (MII) or Rho-kinase collapsed bridges, whereas extension continued over adhesive areas. Inhibition of actin polymerization (latrunculin-A, jasplakinolide) also collapsed the actomyosin network. We suggest that MII has distinct functions at different bridge regions: (1) at the concave edges of bridges, MIIA force stimulates actin filament assembly at adhesions and (2) in the body of bridges, myosin cross-links actin filaments and stimulates actomyosin network healing when breaks occur. Both activities ensure turnover of actin networks needed to maintain stable bridges from one adhesive region to another.

Indexed as

ActinsActomyosinCytoskeletonKineticsMuscle ContractionMyosinsrho-Associated KinasesActinsActomyosinMyosinsrho-Associated Kinases

Identifiers

PMID20150894
PMCPMC2845274
OpenAlexW2146785599

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.