Evidence map›Paper›PMID 7490299›Full record

ArticleThe Journal of cell biology1995

Myosin II filament assemblies in the active lamella of fibroblasts: their morphogenesis and role in the formation of actin filament bundles.

A B Verkhovsky, T M Svitkina, G G Borisy

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 156 papers.

0numbers the graph read from it
0cells of the map it votes in
156citing papers in PubMed
3.6field-weighted citation impact, top 7% 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

156 citing papers in PubMed, 319 citations in OpenAlex.

  1. Article
  2. Article
  3. 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
  4. Article
  5. Myosin 2 - A general contractor for the cytoskeleton.Current opinion in cell biology · 2025
    Review
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  7. Article
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  16. Non-muscle myosin 2 filaments are processive in cells.bioRxiv : the preprint server for biology · 2023
    Article
  17. Article
  18. Article
  19. Article
  20. Imaging Cytoskeleton Components by Electron Microscopy.Methods in molecular biology (Clifton, N.J.) · 2022
    Article

96 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

3 authors at 1 institution in 1 country.

A B VerkhovskyLaboratory of Molecular Biology, University of Wisconsin, Madison 53706, USA.
T M Svitkina
G G Borisy
University of Wisconsin–Madison · US

Funding

MECHANISM AND CONTROL OF MICROTUBULE ASSEMBLYR01GM025062 · NIGMS · UNIVERSITY OF WISCONSIN MADISON · PI BORISY, GARY G · 1985 to 2003
$1.9M
MECHANISM AND CONTROL OF MICROTUBULE ASSEMBLYR37GM025062 · NIGMS · UNIVERSITY OF WISCONSIN MADISON · PI BORISY, GARY G · 1989 to 1998
–
NIGMS NIH HHS GM 25062
6 · The paper itself

Abstract

The morphogenesis of myosin II structures in active lamella undergoing net protrusion was analyzed by correlative fluorescence and electron microscopy. In rat embryo fibroblasts (REF 52) microinjected with tetramethylrhodamine-myosin II, nascent myosin spots formed close to the active edge during periods of retraction and then elongated into wavy ribbons of uniform width. The spots and ribbons initially behaved as distinct structural entities but subsequently aligned with each other in a sarcomeric-like pattern. Electron microscopy established that the spots and ribbons consisted of bipolar minifilaments associated with each other at their head-containing ends and arranged in a single row in an "open" zig-zag conformation or as a "closed" parallel stack. Ribbons also contacted each other in a nonsarcomeric, network-like arrangement as described previously (Verkhovsky and Borisy, 1993. J. Cell Biol. 123:637-652). Myosin ribbons were particularly pronounced in REF 52 cells, but small ribbons and networks were found also in a range of other mammalian cells. At the edge of the cell, individual spots and open ribbons were associated with relatively disordered actin filaments. Further from the edge, myosin filament alignment increased in parallel with the development of actin bundles. In actin bundles, the actin cross-linking protein, alpha-actinin, was excluded from sites of myosin localization but concentrated in paired sites flanking each myosin ribbon, suggesting that myosin filament association may initiate a pathway for the formation of actin filament bundles. We propose that zig-zag assemblies of myosin II filaments induce the formation of actin bundles by pulling on an actin filament network and that co-alignment of actin and myosin filaments proceeds via folding of myosin II filament assemblies in an accordion-like fashion.

Indexed as

3T3 CellsActininActinsAnimalsCell LineCell Line, TransformedChick EmbryoChlorocebus aethiopsFibroblastsFluorescent Antibody TechniqueHumansImmunohistochemistryMiceMicroscopy, ImmunoelectronMorphogenesisMyosinsActininActinsMyosins

Identifiers

PMID7490299
PMCPMC2200006
OpenAlexW2008544686

What OpenQuestion holds

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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.