Evidence map›Paper›PMID 31216217›Full record

ArticleMolecular biology of the cell2019

Reciprocal regulation of actomyosin organization and contractility in nonmuscle cells by tropomyosins and alpha-actinins.

Shiqiong Hu, Hanna Grobe, Zhenhuan Guo, Yu-Hsiu Wang, Bryant L Doss, Meng Pan, Benoit Ladoux, Alexander D Bershadsky, Ronen Zaidel-Bar

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.9field-weighted citation impact, top 16% 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

14 citing papers in PubMed, 26 citations in OpenAlex.

  1. Article
  2. Structure, regulation, and mechanisms of nonmuscle myosin-2.Cellular and molecular life sciences : CMLS · 2024
    Review
  3. Article
  4. Article
  5. Non-muscle myosin II and the plasticity of 3D cell migration.Frontiers in cell and developmental biology · 2022
    Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Cell response to substrate rigidity is regulated by active and passive cytoskeletal stress.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  12. Article
  13. Article
  14. 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

9 authors at 3 institutions in 3 countries.

Shiqiong HuMechanobiology Institute, National University of Singapore, Singapore 117411.
Hanna GrobeSackler Faculty of Medicine, Tel Aviv University, Tel Aviv, Yafo 6997801, Israel.
Zhenhuan GuoMechanobiology Institute, National University of Singapore, Singapore 117411.
Yu-Hsiu WangMechanobiology Institute, National University of Singapore, Singapore 117411.
Bryant L DossMechanobiology Institute, National University of Singapore, Singapore 117411.
Meng PanMechanobiology Institute, National University of Singapore, Singapore 117411.
Benoit LadouxInstitut Jacques Monod, Université de Paris and CNRS, 75205 Paris CEDEX 13, France.
Alexander D BershadskyMechanobiology Institute, National University of Singapore, Singapore 117411.
Ronen Zaidel-BarSackler Faculty of Medicine, Tel Aviv University, Tel Aviv, Yafo 6997801, Israel.
National University of Singapore · SGTel Aviv University · ILCentre National de la Recherche Scientifique · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Contractile arrays of actin and myosin II filaments drive many essential processes in nonmuscle cells, including migration and adhesion. Sequential organization of actin and myosin along one dimension is followed by expansion into a two-dimensional network of parallel actomyosin fibers, in which myosin filaments are aligned to form stacks. The process of stack formation has been studied in detail. However, factors that oppose myosin stack formation have not yet been described. Here, we show that tropomyosins act as negative regulators of myosin stack formation. Knockdown of any or all tropomyosin isoforms in rat embryonic fibroblasts resulted in longer and more numerous myosin stacks and a highly ordered actomyosin organization. The molecular basis for this, we found, is the competition between tropomyosin and alpha-actinin for binding actin. Surprisingly, excessive order in the actomyosin network resulted in smaller focal adhesions, lower tension within the network, and smaller traction forces. Conversely, disordered actomyosin bundles induced by alpha-actinin knockdown led to higher than normal tension and traction forces. Thus, tropomyosin acts as a check on alpha-actinin to achieve intermediate levels of myosin stacks matching the force requirements of the cell.

Indexed as

Muscle ContractionActin CytoskeletonActininActomyosinAnimalsBiomechanical PhenomenaFibroblastsFocal AdhesionsModels, BiologicalMyosin Type IIRatsStress FibersTropomyosinActininActomyosinMyosin Type IITropomyosin

Identifiers

PMID31216217
PMCPMC6727768
OpenAlexW2951900793

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.