Evidence map›Paper›PMID 25131674›Full record

ArticleCurrent biology : CB2014

Endogenous species of mammalian nonmuscle myosin IIA and IIB include activated monomers and heteropolymers.

Maria S Shutova, Waldo A Spessott, Claudio G Giraudo, Tatyana Svitkina

Abstract read
In one paragraph

Article in Current biology : CB, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 89 papers.

0numbers the graph read from it
0cells of the map it votes in
89citing papers in PubMed
5.3field-weighted citation impact, top 4% 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

89 citing papers in PubMed, 124 citations in OpenAlex.

  1. Article
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  8. 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
  9. Article
  10. Article
  11. Myosin 2 - A general contractor for the cytoskeleton.Current opinion in cell biology · 2025
    Review
  12. Article
  13. Non-Muscle Myosin II A: Friend or Foe in Cancer?International journal of molecular sciences · 2024
    Review
  14. Structure, regulation, and mechanisms of nonmuscle myosin-2.Cellular and molecular life sciences : CMLS · 2024
    Review
  15. Article
  16. SuggestingCells · 2024
    Article
  17. Article
  18. Review
  19. Article
  20. Article

29 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

4 authors at 2 institutions in 1 country.

Maria S ShutovaDepartment of Biology, University of Pennsylvania, Philadelphia, PA 19104, USA.
Waldo A SpessottDepartment of Pathology and Laboratory Medicine, The Children's Hospital of Philadelphia, University of Pennsylvania, Philadelphia, PA 19104, USA.
Claudio G GiraudoDepartment of Pathology and Laboratory Medicine, The Children's Hospital of Philadelphia, University of Pennsylvania, Philadelphia, PA 19104, USA.
Tatyana SvitkinaDepartment of Biology, University of Pennsylvania, Philadelphia, PA 19104, USA. Electronic address: svitkina@sas.upenn.edu.
Children's Hospital of Philadelphia · USUniversity of Pennsylvania · US

Funding

Multifaceted roles of nonmuscle myosin II in cell adhesion and migrationR01GM095977 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI SVITKINA, TATYANA · 2013 to 2020
$2.7M
NIGMS NIH HHS GM095977NIGMS NIH HHS R01 GM095977
6 · The paper itself

Abstract

backgroundClass II myosins generate contractile forces in cells by polymerizing into bipolar filaments and pulling on anchored actin filaments. Nonmuscle myosin II (NMII) plays central roles during cell adhesion, migration, cytokinesis, and tissue morphogenesis. NMII is present in virtually all mammalian cell types as tissue-specific combinations of NMIIA, NMIIB, and NMIIC isoforms. It remains poorly understood how the highly dynamic NMII-actin contractile system begins to assemble at new cellular locations during cell migration and how incorporation of different NMII isoforms into this system is coordinated.

resultsUsing platinum replica electron microscopy in combination with immunogold labeling, we demonstrate that individual activated (phosphorylated on the regulatory light chain and unfolded) NMIIA and NMIIB molecules represent a functional form of NMII in motile cells and that NMIIA and NMIIB copolymerize into nascent bipolar filaments during contractile system assembly. Using subdiffraction stimulated emission depletion microscopy together with a pharmacological block-and-release approach, we report that NMIIA and NMIIB simultaneously incorporate into the cytoskeleton during initiation of contractile system assembly, whereas the characteristic rearward shift of NMIIB relative to NMIIA is established later in the course of NMII turnover.

conclusionsWe show existence of activated NMII monomers in cells, copolymerization of endogenous NMIIA and NMIIB molecules, and contribution of both isoforms, rather than only NMIIA, to early stages of the contractile system assembly. These data change the current paradigms about dynamics and functions of NMII and provide new conceptual insights into the organization and dynamics of the ubiquitous cellular machinery for contraction that acts in multiple cellular contexts.

Indexed as

Actin CytoskeletonAnimalsCell AdhesionCells, CulturedEmbryo, MammalianNonmuscle Myosin Type IIANonmuscle Myosin Type IIBPhosphorylationProtein IsoformsRatsNonmuscle Myosin Type IIANonmuscle Myosin Type IIBProtein Isoforms

Identifiers

PMID25131674
PMCPMC4160463
OpenAlexW2055343292

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.