Evidence map›Paper›PMID 28114270›Full record

ArticleNature cell biology2017

Long-range self-organization of cytoskeletal myosin II filament stacks.

Shiqiong Hu, Kinjal Dasbiswas, Zhenhuan Guo, Yee-Han Tee, Visalatchi Thiagarajan, Pascal Hersen, Teng-Leong Chew, Samuel A Safran, Ronen Zaidel-Bar, Alexander D Bershadsky

Erratum issuedAbstract read
PubMed Publisher
In one paragraph

Article in Nature cell biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 104 papers.

0numbers the graph read from it
0cells of the map it votes in
104citing papers in PubMed
–field-weighted citation impact
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

104 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Nonmuscle myosin 2 turnover in cells is synergistically controlled by the tail and the motor domain.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  7. Article
  8. Myosin 2 - A general contractor for the cytoskeleton.Current opinion in cell biology · 2025
    Review
  9. Article
  10. Filament transport supports contractile steady states of actin networks.bioRxiv : the preprint server for biology · 2025
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Structure, regulation, and mechanisms of nonmuscle myosin-2.Cellular and molecular life sciences : CMLS · 2024
    Review
  16. LUZP1 regulates the maturation of contractile actomyosin bundles.Cellular and molecular life sciences : CMLS · 2024
    Article
  17. Article
  18. Article
  19. Article
  20. Article

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

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

10 authors.

Shiqiong HuMechanobiology Institute, National University of Singapore, Singapore 117411, Singapore.
Kinjal DasbiswasDepartment of Materials and Interfaces, Weizmann Institute of Science, Rehovot 76100, Israel.
Zhenhuan GuoMechanobiology Institute, National University of Singapore, Singapore 117411, Singapore.
Yee-Han TeeMechanobiology Institute, National University of Singapore, Singapore 117411, Singapore.
Visalatchi ThiagarajanMechanobiology Institute, National University of Singapore, Singapore 117411, Singapore.
Pascal HersenMechanobiology Institute, National University of Singapore, Singapore 117411, Singapore.
Teng-Leong ChewAdvanced Imaging Center, HHMI Janelia Research Campus, Ashburn, Virginia 20147, USA.
Samuel A SafranDepartment of Materials and Interfaces, Weizmann Institute of Science, Rehovot 76100, Israel.
Ronen Zaidel-BarMechanobiology Institute, National University of Singapore, Singapore 117411, Singapore.
Alexander D BershadskyMechanobiology Institute, National University of Singapore, Singapore 117411, Singapore.

Funding

Howard Hughes Medical Institute
6 · The paper itself

Abstract

Although myosin II filaments are known to exist in non-muscle cells, their dynamics and organization are incompletely understood. Here, we combined structured illumination microscopy with pharmacological and genetic perturbations, to study the process of actomyosin cytoskeleton self-organization into arcs and stress fibres. A striking feature of the myosin II filament organization was their 'registered' alignment into stacks, spanning up to several micrometres in the direction orthogonal to the parallel actin bundles. While turnover of individual myosin II filaments was fast (characteristic half-life time 60 s) and independent of actin filament turnover, the process of stack formation lasted a longer time (in the range of several minutes) and required myosin II contractility, as well as actin filament assembly/disassembly and crosslinking (dependent on formin Fmnl3, cofilin1 and α-actinin-4). Furthermore, myosin filament stack formation involved long-range movements of individual myosin filaments towards each other suggesting the existence of attractive forces between myosin II filaments. These forces, possibly transmitted via mechanical deformations of the intervening actin filament network, may in turn remodel the actomyosin cytoskeleton and drive its self-organization.

Indexed as

Actin CytoskeletonActomyosinCytoskeletonHalf-LifeHumansModels, BiologicalMuscle ContractionMyosin Type IIActomyosinMyosin Type II

Identifiers

PMID28114270

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.