Evidence map›Paper›PMID 22022566›Full record

ArticlePloS one2011

Stretching actin filaments within cells enhances their affinity for the myosin II motor domain.

Taro Q P Uyeda, Yoshiaki Iwadate, Nobuhisa Umeki, Akira Nagasaki, Shigehiko Yumura

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 86 papers.

0numbers the graph read from it
0cells of the map it votes in
86citing papers in PubMed
4.1field-weighted citation impact, top 6% 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

86 citing papers in PubMed, 157 citations in OpenAlex.

  1. Review
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  13. Vascular mechanotransduction.Physiological reviews · 2023
    Review
  14. Article
  15. Tuning immunity through tissue mechanotransduction.Nature reviews. Immunology · 2023
    Review
  16. Non-muscle myosin 2 at a glance.Journal of cell science · 2023
    Review
  17. Article
  18. Review
  19. Article
  20. Article

26 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

5 authors at 2 institutions in 1 country.

Taro Q P UyedaNational Institute of Advanced Industrial Science and Technology, Tsukuba, Ibaraki, Japan. t-uyeda@aist.go.jp
Yoshiaki Iwadate
Nobuhisa Umeki
Akira Nagasaki
Shigehiko Yumura
National Institute of Advanced Industrial Science and Technology · JPYamaguchi University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

To test the hypothesis that the myosin II motor domain (S1) preferentially binds to specific subsets of actin filaments in vivo, we expressed GFP-fused S1 with mutations that enhanced its affinity for actin in Dictyostelium cells. Consistent with the hypothesis, the GFP-S1 mutants were localized along specific portions of the cell cortex. Comparison with rhodamine-phalloidin staining in fixed cells demonstrated that the GFP-S1 probes preferentially bound to actin filaments in the rear cortex and cleavage furrows, where actin filaments are stretched by interaction with endogenous myosin II filaments. The GFP-S1 probes were similarly enriched in the cortex stretched passively by traction forces in the absence of myosin II or by external forces using a microcapillary. The preferential binding of GFP-S1 mutants to stretched actin filaments did not depend on cortexillin I or PTEN, two proteins previously implicated in the recruitment of myosin II filaments to stretched cortex. These results suggested that it is the stretching of the actin filaments itself that increases their affinity for the myosin II motor domain. In contrast, the GFP-fused myosin I motor domain did not localize to stretched actin filaments, which suggests different preferences of the motor domains for different structures of actin filaments play a role in distinct intracellular localizations of myosin I and II. We propose a scheme in which the stretching of actin filaments, the preferential binding of myosin II filaments to stretched actin filaments, and myosin II-dependent contraction form a positive feedback loop that contributes to the stabilization of cell polarity and to the responsiveness of the cells to external mechanical stimuli.

Indexed as

Actin CytoskeletonDictyosteliumGene Knockout TechniquesGreen Fluorescent ProteinsModels, BiologicalMolecular ProbesMutant ProteinsMyosin Type IIPhalloidineProtein Structure, TertiaryProtein TransportRhodaminesGreen Fluorescent ProteinsMolecular ProbesMutant ProteinsMyosin Type IIPhalloidinerhodamine-phalloidinRhodamines

Identifiers

PMID22022566
PMCPMC3192770
OpenAlexW2125495005

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.