Evidence map›Paper›PMID 22467859›Full record

ArticleJournal of cell science2012

The function of the M-line protein obscurin in controlling the symmetry of the sarcomere in the flight muscle of Drosophila.

Anja Katzemich, Nina Kreisköther, Alexander Alexandrovich, Christopher Elliott, Frieder Schöck, Kevin Leonard, John Sparrow, Belinda Bullard

Erratum issuedOpen access · greenAbstract read
In one paragraph

Article in Journal of cell science, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 46 papers.

0numbers the graph read from it
0cells of the map it votes in
46citing papers in PubMed
2.4field-weighted citation impact, top 11% 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

46 citing papers in PubMed, 68 citations in OpenAlex.

  1. Article
  2. Article
  3. Developmental remodelling ofOpen biology · 2025
    Article
  4. The varied functions of the giant muscle scaffold protein obscurin.Frontiers in cell and developmental biology · 2025
    Review
  5. Article
  6. Obscurin Maintains Myofiber Identity in Extraocular Muscles.Investigative ophthalmology & visual science · 2024
    Article
  7. Article
  8. Structure of theInternational journal of molecular sciences · 2023
    Article
  9. Article
  10. PK1 fromOpen biology · 2023
    Article
  11. Article
  12. Sarcomere maturation: function acquisition, molecular mechanism, and interplay with other organelles.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2022
    Review
  13. Impaired Intracellular CaInternational journal of molecular sciences · 2022
    Article
  14. Article
  15. Article
  16. Article
  17. Impaired muscle morphology in aDisease models & mechanisms · 2020
    Article
  18. CryoEM structure ofLife science alliance · 2020
    Article
  19. Review
  20. Article
4 · The record

Corrections and comments

  • Erratum issued
5 · Who and what money

Authors and funding

8 authors at 4 institutions in 2 countries.

Anja KatzemichDepartment of Biology, University of York, York, UK.
Nina Kreisköther
Alexander Alexandrovich
Christopher Elliott
Frieder Schöck
Kevin Leonard
John Sparrow
Belinda Bullard
University of York · GBKing's College London · GBPhilipps University of Marburg · DEWellcome Trust · GB

Funding

Canadian Institutes of Health Research MOP-93727Medical Research Council
6 · The paper itself

Abstract

Obscurin (also known as Unc-89 in Drosophila) is a large modular protein in the M-line of Drosophila muscles. Drosophila obscurin is similar to the nematode protein UNC-89. Four isoforms are found in the muscles of adult flies: two in the indirect flight muscle (IFM) and two in other muscles. A fifth isoform is found in the larva. The larger IFM isoform has all the domains that were predicted from the gene sequence. Obscurin is in the M-line throughout development of the embryo, larva and pupa. Using P-element mutant flies and RNAi knockdown flies, we have investigated the effect of decreased obscurin expression on the structure of the sarcomere. Embryos, larvae and pupae developed normally. In the pupa, however, the IFM was affected. Although the Z-disc was normal, the H-zone was misaligned. Adults were unable to fly and the structure of the IFM was irregular: M-lines were missing and H-zones misplaced or absent. Isolated thick filaments were asymmetrical, with bare zones that were shifted away from the middle of the filaments. In the sarcomere, the length and polarity of thin filaments depends on the symmetry of adjacent thick filaments; shifted bare zones resulted in abnormally long or short thin filaments. We conclude that obscurin in the IFM is necessary for the development of a symmetrical sarcomere in Drosophila IFM.

Indexed as

AnimalsDrosophilaFemaleGene ExpressionImmunoprecipitationMaleMuscle ProteinsMuscle, SkeletalProtein IsoformsSarcomeresMuscle ProteinsProtein Isoforms

Identifiers

PMID22467859
PMCPMC3516378
OpenAlexW2096707568

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.