Evidence map›Paper›PMID 25431137›Full record

ArticleJournal of cell science2015

Leiomodin 3 and tropomodulin 4 have overlapping functions during skeletal myofibrillogenesis.

Chinedu U Nworu, Robert Kraft, Daniel C Schnurr, Carol C Gregorio, Paul A Krieg

Open access · bronzeAbstract read
In one paragraph

Article in Journal of cell science, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
2.6field-weighted citation impact, top 10% 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

28 citing papers in PubMed, 42 citations in OpenAlex.

  1. Article
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  9. Journal of clinical medicine · 2022
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  15. Article
  16. Article
  17. Overview of the Muscle Cytoskeleton.Comprehensive Physiology · 2017
    Review
  18. 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

5 authors at 1 institution in 1 country.

Chinedu U NworuDepartment of Cellular and Molecular Medicine, Sarver Molecular Cardiovascular Research Program, University of Arizona, 1656 E. Mabel St, Tucson, AZ 85724, USA.
Robert KraftDepartment of Cellular and Molecular Medicine, Sarver Molecular Cardiovascular Research Program, University of Arizona, 1656 E. Mabel St, Tucson, AZ 85724, USA.
Daniel C SchnurrDepartment of Cellular and Molecular Medicine, Sarver Molecular Cardiovascular Research Program, University of Arizona, 1656 E. Mabel St, Tucson, AZ 85724, USA.
Carol C GregorioDepartment of Cellular and Molecular Medicine, Sarver Molecular Cardiovascular Research Program, University of Arizona, 1656 E. Mabel St, Tucson, AZ 85724, USA gregorio@email.arizona.edu.
Paul A KriegDepartment of Cellular and Molecular Medicine, Sarver Molecular Cardiovascular Research Program, University of Arizona, 1656 E. Mabel St, Tucson, AZ 85724, USA.
University of Arizona · US

Funding

Deciphering the Roles of Nebulin in Cardiac Myofibril AssemblyR01HL083146 · NHLBI · UNIVERSITY OF ARIZONA · PI GREGORIO, CAROL C · 2007 to 2011
$2.1M
Deciphering the role of the RNA-binding protein, FXR1, in cardiac muscle assemblyR01HL108625 · NHLBI · UNIVERSITY OF ARIZONA · PI GREGORIO, CAROL C · 2012 to 2015
$1.9M
Regulation of Vascular Endothelial Gene ExpressionR01HL093694 · NHLBI · UNIVERSITY OF ARIZONA · PI KRIEG, PAUL ANTHONY · 2009 to 2010
$744k
NHLBI NIH HHS HL083146NHLBI NIH HHS HL093694NHLBI NIH HHS HL108625NHLBI NIH HHS R01 HL083146NHLBI NIH HHS R01 HL093694NHLBI NIH HHS R01 HL108625
6 · The paper itself

Abstract

Precise regulation of thin filament length is essential for optimal force generation during muscle contraction. The thin filament capping protein tropomodulin (Tmod) contributes to thin filament length uniformity by regulating elongation and depolymerization at thin filament ends. The leiomodins (Lmod1-3) are structurally related to Tmod1-4 and also localize to actin filament pointed ends, but in vitro biochemical studies indicate that Lmods act instead as robust nucleators. Here, we examined the roles of Tmod4 and Lmod3 during Xenopus skeletal myofibrillogenesis. Loss of Tmod4 or Lmod3 resulted in severe disruption of sarcomere assembly and impaired embryonic movement. Remarkably, when Tmod4-deficient embryos were supplemented with additional Lmod3, and Lmod3-deficient embryos were supplemented with additional Tmod4, sarcomere assembly was rescued and embryonic locomotion improved. These results demonstrate for the first time that appropriate levels of both Tmod4 and Lmod3 are required for embryonic myofibrillogenesis and, unexpectedly, both proteins can function redundantly during in vivo skeletal muscle thin filament assembly. Furthermore, these studies demonstrate the value of Xenopus for the analysis of contractile protein function during de novo myofibril assembly.

Indexed as

Embryo, NonmammalianActin CytoskeletonAnimalsGene Expression Regulation, DevelopmentalMicrofilament ProteinsMuscle ContractionMuscle DevelopmentMuscle ProteinsMuscle, SkeletalMyocardiumSarcomeresTropomodulinXenopus laevisLMOD3 protein, humanMicrofilament ProteinsMuscle ProteinsTropomodulinActin thin filamentLeiomodinSarcomereSkeletal muscleTropomodulin

Identifiers

PMID25431137
PMCPMC4294772
OpenAlexW2071356593

What OpenQuestion holds

Textmetadata
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.