Evidence map›Paper›PMID 24794494›Full record

ArticleJournal of cell science2014

The conserved transmembrane proteoglycan Perdido/Kon-tiki is essential for myofibrillogenesis and sarcomeric structure in Drosophila.

Juan J Pérez-Moreno, Marcus Bischoff, Maria D Martín-Bermudo, Beatriz Estrada

Open access · hybridAbstract read
In one paragraph

Article in Journal of cell science, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.0field-weighted citation impact, top 31% 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

18 citing papers in PubMed, 25 citations in OpenAlex.

  1. Myotendinous Junction development and repair.Journal of orthopaedic translation · 2026
    Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Developmental origin of tendon diversity inFrontiers in physiology · 2023
    Review
  7. LanB1 Cooperates With Kon-Tiki During Embryonic Muscle Migration inFrontiers in cell and developmental biology · 2021
    Article
  8. Review
  9. Article
  10. Review
  11. Article
  12. Article
  13. Review
  14. Proteoglycan form and function: A comprehensive nomenclature of proteoglycans.Matrix biology : journal of the International Society for Matrix Biology · 2015
    Review
  15. Article
  16. Article
  17. Article
  18. 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

4 authors at 2 institutions in 1 country.

Juan J Pérez-MorenoCentro Andaluz de Biología del Desarrollo, Universidad Pablo de Olavide-CSIC, 41013 Seville, Spain.
Marcus BischoffDepartment of Zoology, University of Cambridge, Downing Street, Cambridge, CB2 3EJ, UK bestmar@upo.es.
Maria D Martín-BermudoCentro Andaluz de Biología del Desarrollo, Universidad Pablo de Olavide-CSIC, 41013 Seville, Spain.
Beatriz EstradaCentro Andaluz de Biología del Desarrollo, Universidad Pablo de Olavide-CSIC, 41013 Seville, Spain bestmar@upo.es.
Centro Andaluz de Biología del Desarrollo · ESUniversidad Pablo de Olavide · ES

Funding

Wellcome Trust 096645Wellcome Trust WT096645MA
6 · The paper itself

Abstract

Muscle differentiation requires the assembly of high-order structures called myofibrils, composed of sarcomeres. Even though the molecular organization of sarcomeres is well known, the mechanisms underlying myofibrillogenesis are poorly understood. It has been proposed that integrin-dependent adhesion nucleates myofibrils at the periphery of the muscle cell to sustain sarcomere assembly. Here, we report a role for the gene perdido (perd, also known as kon-tiki, a transmembrane chondroitin proteoglycan) in myofibrillogenesis. Expression of perd RNAi in muscles, prior to adult myogenesis, can induce misorientation and detachment of Drosophila adult abdominal muscles. In comparison to controls, perd-depleted muscles contain fewer myofibrils, which are localized at the cell periphery. These myofibrils are detached from each other and display a defective sarcomeric structure. Our results demonstrate that the extracellular matrix receptor Perd has a specific role in the assembly of myofibrils and in sarcomeric organization. We suggest that Perd acts downstream or in parallel to integrins to enable the connection of nascent myofibrils to the Z-bands. Our work identifies the Drosophila adult abdominal muscles as a model to investigate in vivo the mechanisms behind myofibrillogenesis.

Indexed as

AnimalsDrosophilaDrosophila ProteinsMembrane ProteinsMuscle DevelopmentMuscle ProteinsProteoglycansSarcomeresDrosophila ProteinsMembrane ProteinsMuscle ProteinsProteoglycansAN2Chondroitin sulfate proteoglycanCSPG4IntegrinKon-tikiMCSPMuscleMyofibrilMyogenesisNG2PerdidoSarcomere

Identifiers

PMID24794494
PMCPMC4095857
OpenAlexW2027296287

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.