Evidence map›Paper›PMID 33790983›Full record

ArticleNature physics2019

Large and reversible myosin-dependent forces in rigidity sensing.

James Lohner, Jean-Francois Rupprecht, Junquiang Hu, Nicola Mandriota, Mayur Saxena, Diego Pitta de Araujo, James Hone, Ozgur Sahin, Jacques Prost, Michael P Sheetz

Open access · greenAbstract read
In one paragraph

Article in Nature physics, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
2.5field-weighted citation impact, top 12% 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

17 citing papers in PubMed, 33 citations in OpenAlex.

  1. Article
  2. TiOAdvanced materials (Deerfield Beach, Fla.) · 2024
    Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Biophysical Approaches for Applying and Measuring Biological Forces.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2022
    Review
  10. Review
  11. Effects of forces on chromatin.APL bioengineering · 2021
    Review
  12. Review
  13. Article
  14. Review
  15. Article
  16. Article
  17. Dissecting fat-tailed fluctuations in the cytoskeleton with active micropost arrays.Proceedings of the National Academy of Sciences of the United States of America · 2019
    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

10 authors at 4 institutions in 3 countries.

James Lohnerfirst authors.
Jean-Francois Rupprechtfirst authors.
Junquiang HuDepartment of Biological Sciences, Columbia University, New York, New York 10027, USA.
Nicola MandriotaDepartment of Biological Sciences, Columbia University, New York, New York 10027, USA.
Mayur SaxenaDepartment of Biomedical Engineering, Columbia University, New York, New York 10027, USA.
Diego Pitta de AraujoMechanobiology Institute, National University of Singapore, 5A Engineering Drive 1, 117411 Singapore.
James HoneDepartment of Mechanical Engineering, Columbia University, New York, New York 10027, USA.
Ozgur SahinDepartment of Biological Sciences, Columbia University, New York, New York 10027, USA.
Jacques ProstMechanobiology Institute, National University of Singapore, 5A Engineering Drive 1, 117411 Singapore.
Michael P SheetzDepartment of Biological Sciences, Columbia University, New York, New York 10027, USA.
Columbia University · USNational University of Singapore · SGCentre National de la Recherche Scientifique · FRHealth First · US

Funding

Tropomyosin and tyrosine kinases in mechanics of cancerR01GM113022 · NIGMS · COLUMBIA UNIV NEW YORK MORNINGSIDE · PI SHEETZ, MICHAEL PATRICK · 2015 to 2018
$1.2M
NIGMS NIH HHS R01 GM113022
6 · The paper itself

Abstract

Cells sense the rigidity of their environment through localized pinching, which occurs when myosin molecular motors generate contractions within actin filaments anchoring the cell to its surroundings. We present high-resolution experiments performed on these elementary contractile units in cells. Our experimental results challenge the current understanding of molecular motor force generation. Surprisingly, bipolar myosin filaments generate much larger forces per motor than measured in single molecule experiments. Further, contraction to a fixed distance, followed by relaxation at the same rate, is observed over a wide range of matrix rigidities. Lastly, step-wise displacements of the matrix contacts are apparent during both contraction and relaxation. Building upon a generic two-state model of molecular motor collections, we interpret these unexpected observations as spontaneously emerging features of a collective motor behavior. Our approach explains why, in the cellular context, collections of resilient and slow motors contract in a stepwise fashion while collections of weak and fast motors do not. We thus rationalize the specificity of motor contractions implied in rigidity sensing compared to previous in vitro observations.

Identifiers

PMID33790983
PMCPMC8008990
OpenAlexW2932338525

What OpenQuestion holds

Textmetadata
LicenceTDM
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.