Evidence map›Paper›PMID 25550404›Full record

ArticleEMBO reports2015

Actomyosin bundles serve as a tension sensor and a platform for ERK activation.

Hiroaki Hirata, Mukund Gupta, Sri Ram Krishna Vedula, Chwee Teck Lim, Benoit Ladoux, Masahiro Sokabe

Open access · greenAbstract read
In one paragraph

Article in EMBO reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
2.4field-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

37 citing papers in PubMed, 71 citations in OpenAlex.

  1. Actin cytoskeletal dynamics in hepatic myofibroblasts and fibrosis.Nature reviews. Gastroenterology & hepatology · 2026
    Review
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  5. Review
  6. Article
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  9. Emerging roles and mechanisms of ERK pathway mechanosensing.Cellular and molecular life sciences : CMLS · 2023
    Review
  10. Article
  11. Gravity's effect on biology.Frontiers in physiology · 2023
    Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. ERK signaling for cell migration and invasion.Frontiers in molecular biosciences · 2022
    Review
  17. Article
  18. FRET Visualization of Cyclic Stretch-Activated ERKFrontiers in cell and developmental biology · 2022
    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

6 authors at 3 institutions in 3 countries.

Hiroaki HirataMechanobiology Institute, National University of Singapore, Singapore, Singapore.
Mukund GuptaMechanobiology Institute, National University of Singapore, Singapore, Singapore.
Sri Ram Krishna VedulaMechanobiology Institute, National University of Singapore, Singapore, Singapore.
Chwee Teck LimMechanobiology Institute, National University of Singapore, Singapore, Singapore Department of Biomedical Engineering, National University of Singapore, Singapore, Singapore Department of Mechanical Engineering, National University of Singapore, Singapore, Singapore.
Benoit LadouxMechanobiology Institute, National University of Singapore, Singapore, Singapore Institut Jacques Monod (IJM), CNRS UMR 7592 Université Paris Diderot, Paris, France.
Masahiro SokabeMechanobiology Institute, National University of Singapore, Singapore, Singapore Mechanobiology Laboratory, Nagoya University Graduate School of Medicine, Nagoya, Japan msokabe@med.nagoya-u.ac.jp.
National University of Singapore · SGCentre National de la Recherche Scientifique · FRNagoya University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Tensile forces generated by stress fibers drive signal transduction events at focal adhesions. Here, we report that stress fibers per se act as a platform for tension-induced activation of biochemical signals. The MAP kinase, ERK is activated on stress fibers in a myosin II-dependent manner. In myosin II-inhibited cells, uniaxial stretching of cell adhesion substrates restores ERK activation on stress fibers. By quantifying myosin II- or mechanical stretch-mediated tensile forces in individual stress fibers, we show that ERK activation on stress fibers correlates positively with tensile forces acting on the fibers, indicating stress fibers as a tension sensor in ERK activation. Myosin II-dependent ERK activation is also observed on actomyosin bundles connecting E-cadherin clusters, thus suggesting that actomyosin bundles, in general, work as a platform for tension-dependent ERK activation.

Indexed as

ActomyosinAnimalsCell LineExtracellular Signal-Regulated MAP KinasesFocal AdhesionsHumansMechanotransduction, CellularMiceMyosin Type IINIH 3T3 CellsStress FibersTensile StrengthActomyosinExtracellular Signal-Regulated MAP KinasesMyosin Type IIcontractilitymechanotransductionstress fibertensile force

Identifiers

PMID25550404
PMCPMC4328752
OpenAlexW2152233928

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.