Evidence map›Paper›PMID 30518778›Full record

ArticleScientific reports2018

Calponin-3 is critical for coordinated contractility of actin stress fibers.

Katarzyna Ciuba, William Hawkes, Sari Tojkander, Konstantin Kogan, Ulrike Engel, Thomas Iskratsch, Pekka Lappalainen

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.5field-weighted citation impact, top 19% 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

16 citing papers in PubMed, 24 citations in OpenAlex.

  1. Molecules That Have Rarely Been Studied in Lymphatic Endothelial Cells.International journal of molecular sciences · 2024
    Review
  2. Review
  3. Article
  4. Evolution and function of calponin and transgelin.Frontiers in cell and developmental biology · 2023
    Review
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. TwoThe Journal of biological chemistry · 2020
    Article
  13. Review
  14. Article
  15. Article
  16. 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

7 authors at 4 institutions in 3 countries.

Katarzyna CiubaInsitute of Biotechnology, P.O. Box 56, 0014, University of Helsinki, Helsinki, Finland.
William HawkesSchool of Engineering and Materials Science, Queen Mary University of London, E1 4NS, London, UK.
Sari TojkanderSection of Pathology, Department of Veterinary Biosciences, University of Helsinki, Helsinki, Finland.
Konstantin KoganInsitute of Biotechnology, P.O. Box 56, 0014, University of Helsinki, Helsinki, Finland.
Ulrike EngelNikon Imaging Center at Heidelberg University and Centre for Organismal Studies (COS), Heidelberg University, Im Neuenheimer Feld 267, Heidelberg, 69120, Germany.
Thomas IskratschSchool of Engineering and Materials Science, Queen Mary University of London, E1 4NS, London, UK.
Pekka LappalainenInsitute of Biotechnology, P.O. Box 56, 0014, University of Helsinki, Helsinki, Finland. pekka.lappalainen@helsinki.fi.
University of Helsinki · FIHeidelberg University · DEKing's College London · GBQueen Mary University of London · GB

Funding

British Heart Foundation FS/14/30/30917
6 · The paper itself

Abstract

Contractile actomyosin bundles, stress fibers, contribute to morphogenesis, migration, and mechanosensing of non-muscle cells. In addition to actin and non-muscle myosin II (NMII), stress fibers contain a large array of proteins that control their assembly, turnover, and contractility. Calponin-3 (Cnn3) is an actin-binding protein that associates with stress fibers. However, whether Cnn3 promotes stress fiber assembly, or serves as either a positive or negative regulator of their contractility has remained obscure. Here, we applied U2OS osteosarcoma cells as a model system to study the function of Cnn3. We show that Cnn3 localizes to both NMII-containing contractile ventral stress fibers and transverse arcs, as well as to non-contractile dorsal stress fibers that do not contain NMII. Fluorescence-recovery-after-photobleaching experiments revealed that Cnn3 is a dynamic component of stress fibers. Importantly, CRISPR/Cas9 knockout and RNAi knockdown studies demonstrated that Cnn3 is not essential for stress fiber assembly. However, Cnn3 depletion resulted in increased and uncoordinated contractility of stress fibers that often led to breakage of individual actomyosin bundles within the stress fiber network. Collectively these results provide evidence that Cnn3 is dispensable for the assembly of actomyosin bundles, but that it is required for controlling proper contractility of the stress fiber network.

Indexed as

Calcium-Binding ProteinsCalponinsCell Line, TumorFluorescence Recovery After PhotobleachingGene SilencingHumansImaging, Three-DimensionalMicrofilament ProteinsOptical ImagingOsteosarcomaStress FibersCalcium-Binding ProteinsCalponinsMicrofilament Proteins

Identifiers

PMID30518778
PMCPMC6281606
OpenAlexW2902774345

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.