Evidence map›Paper›PMID 21149568›Full record

ArticleThe Journal of cell biology2010

Formin follows function: a muscle-specific isoform of FHOD3 is regulated by CK2 phosphorylation and promotes myofibril maintenance.

Thomas Iskratsch, Stephan Lange, Joseph Dwyer, Ay Lin Kho, Cris dos Remedios, Elisabeth Ehler

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 72 papers.

0numbers the graph read from it
0cells of the map it votes in
72citing papers in PubMed
3.1field-weighted citation impact, top 9% 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

72 citing papers in PubMed, 123 citations in OpenAlex.

  1. Review
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  14. Review
  15. Daam2 phosphorylation by CK2α negatively regulates Wnt activity during white matter development and injury.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  16. FHODs: Nuclear tethered formins for nuclear mechanotransduction.Frontiers in cell and developmental biology · 2023
    Review
  17. Review
  18. The Mechanisms of Thin Filament Assembly and Length Regulation in Muscles.International journal of molecular sciences · 2022
    Review
  19. Biophysical reviews · 2021
    Article
  20. Article

12 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

6 authors at 4 institutions in 4 countries.

Thomas IskratschThe Muscle Cell Biology Section, Randall Division of Cell and Molecular Biophysics, British Heart Foundation Research Excellence Centre, King's College London, London SE1 1UL, England, UK.
Stephan Lange
Joseph Dwyer
Ay Lin Kho
Cris dos Remedios
Elisabeth Ehler
British Heart Foundation · GBInstitute of Molecular Biology and Biophysics · RUUniversity of California, San Diego · USUniversity of Sydney · AU

Funding

British Heart FoundationMedical Research Council G0400153
6 · The paper itself

Abstract

Members of the formin family are important for actin filament nucleation and elongation. We have identified a novel striated muscle-specific splice variant of the formin FHOD3 that introduces a casein kinase 2 (CK2) phosphorylation site. The specific targeting of muscle FHOD3 to the myofibrils in cardiomyocytes is abolished in phosphomutants or by the inhibition of CK2. Phosphorylation of muscle FHOD3 also prevents its interaction with p62/sequestosome 1 and its recruitment to autophagosomes. Furthermore, we show that muscle FHOD3 efficiently promotes the polymerization of actin filaments in cardiomyocytes and that the down-regulation of its expression severely affects myofibril integrity. In murine and human cardiomyopathy, we observe reduced FHOD3 expression with a concomitant isoform switch and change of subcellular targeting. Collectively, our data suggest that a muscle-specific isoform of FHOD3 is required for the maintenance of the contractile structures in heart muscle and that its function is regulated by posttranslational modification.

Indexed as

Amino Acid SequenceAnimalsCasein Kinase IIChlorocebus aethiopsCOS CellsForminsHumansMiceMicrofilament ProteinsMolecular Sequence DataMyocardiumMyocytes, CardiacMyofibrilsPhosphorylationProtein IsoformsRatsCasein Kinase IIFHOD3 protein, humanForminsMicrofilament ProteinsProtein Isoforms

Identifiers

PMID21149568
PMCPMC3002041
OpenAlexW2044788731

What OpenQuestion holds

Textmetadata
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.