Evidence map›Paper›PMID 24430873›Full record

ArticleMolecular biology of the cell2014

Critical roles for multiple formins during cardiac myofibril development and repair.

Michelle Rosado, Cynthia F Barber, Cristina Berciu, Steven Feldman, Susan J Birren, Daniela Nicastro, Bruce L Goode

Abstract read
In one paragraph

Article in Molecular biology of the cell, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing 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

36 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. The Mechanisms of Thin Filament Assembly and Length Regulation in Muscles.International journal of molecular sciences · 2022
    Review
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Ordering of myosin II filaments driven by mechanical forces: experiments and theory.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2018
    Review
  19. Article
  20. Article
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.

Michelle RosadoBiology Department and Rosenstiel Basic Medical Sciences Research Center, Brandeis University, Waltham, MA 02454.
Cynthia F Barber
Cristina Berciu
Steven Feldman
Susan J Birren
Daniela Nicastro
Bruce L Goode

Funding

Quantitative Neuroscience: Tools for Bridging Levels of AnalysisT32NS007292 · NINDS · BRANDEIS UNIVERSITY · PI GINA G TURRIGIANO · 1986 to 2026
$12.7M
Mouse CoreP30NS045713 · NINDS · BRANDEIS UNIVERSITY · PI ROSBASH, MICHAEL · 2003 to 2013
$7.8M
Regulation of formins and cell polarity in yeastR01GM083137 · NIGMS · BRANDEIS UNIVERSITY · PI GOODE, BRUCE L · 2008 to 2019
$4.3M
Regulation of Sympathetic Neuron Synaptic ActivityR01NS066977 · NINDS · BRANDEIS UNIVERSITY · PI BIRREN, SUSAN J · 2010 to 2013
$1.3M
NIGMS NIH HHS GM083137NIGMS NIH HHS R01 GM083137NINDS NIH HHS NS066977NINDS NIH HHS P30 NS045713NINDS NIH HHS P30 NS45713NINDS NIH HHS R01 NS066977NINDS NIH HHS T32 NS007292NINDS NIH HHS T32 NS07292
6 · The paper itself

Abstract

Cardiac and skeletal muscle function depends on the proper formation of myofibrils, which are tandem arrays of highly organized actomyosin contractile units called sarcomeres. How the architecture of these colossal molecular assemblages is established during development and maintained over the lifetime of an animal is poorly understood. We investigate the potential roles in myofibril formation and repair of formin proteins, which are encoded by 15 different genes in mammals. Using quantitative real-time PCR analysis, we find that 13 formins are differentially expressed in mouse hearts during postnatal development. Seven formins immunolocalize to sarcomeres in diverse patterns, suggesting that they have a variety of functional roles. Using RNA interference silencing, we find that the formins mDia2, DAAM1, FMNL1, and FMNL2 are required nonredundantly for myofibrillogenesis. Knockdown phenotypes include global loss of myofibril organization and defective sarcomeric ultrastructure. Finally, our analysis reveals an unanticipated requirement specifically for FMNL1 and FMNL2 in the repair of damaged myofibrils. Together our data reveal an unexpectedly large number of formins, with diverse localization patterns and nonredundant roles, functioning in myofibril development and maintenance, and provide the first evidence of actin assembly factors being required to repair myofibrils.

Indexed as

ActinsAnimalsAnimals, NewbornBridged Bicyclo Compounds, HeterocyclicCell DifferentiationForminsGene Expression Regulation, DevelopmentalHeterocyclic Compounds, 4 or More RingsIntracellular Signaling Peptides and ProteinsMiceMice, Inbred C57BLMicrofilament ProteinsMicrotubule-Associated ProteinsMuscle DevelopmentMyocardiumMyocytes, CardiacActinsblebbistatinBridged Bicyclo Compounds, HeterocyclicDaam1 protein, mouseDia2 protein, mouseFmnl1 protein, mouseFMNL2 protein, mouseForminsHeterocyclic Compounds, 4 or More RingsIntracellular Signaling Peptides and Proteinslatrunculin AMicrofilament ProteinsMicrotubule-Associated ProteinsNADPH DehydrogenaseProtein Isoformsrho GTP-Binding ProteinsRNA, Small InterferingThiazolidines

Identifiers

PMID24430873
PMCPMC3952851

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.