Evidence map›Paper›PMID 26251439›Full record

ArticleJournal of cell science2015

Binding partners of the kinase domains in Drosophila obscurin and their effect on the structure of the flight muscle.

Anja Katzemich, Ryan J H West, Atsushi Fukuzawa, Sean T Sweeney, Mathias Gautel, John Sparrow, Belinda Bullard

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 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
1.3field-weighted citation impact, top 23% 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

23 citing papers in PubMed, 32 citations in OpenAlex.

  1. Article
  2. Developmental remodelling ofOpen biology · 2025
    Article
  3. The varied functions of the giant muscle scaffold protein obscurin.Frontiers in cell and developmental biology · 2025
    Review
  4. Article
  5. Article
  6. Obscurin Maintains Myofiber Identity in Extraocular Muscles.Investigative ophthalmology & visual science · 2024
    Article
  7. PK1 fromOpen biology · 2023
    Article
  8. Article
  9. Article
  10. Article
  11. Impaired Intracellular CaInternational journal of molecular sciences · 2022
    Article
  12. Article
  13. Article
  14. Review
  15. Review
  16. The M-band: The underestimated part of the sarcomere.Biochimica et biophysica acta. Molecular cell research · 2020
    Review
  17. Article
  18. Article
  19. Review
  20. Twitchin kinase inhibits muscle activity.Molecular biology of the cell · 2017
    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 at 2 institutions in 1 country.

Anja KatzemichDepartment of Biology, University of York, York YO10 5DD, UK.
Ryan J H WestDepartment of Biology, University of York, York YO10 5DD, UK.
Atsushi FukuzawaKing's College BHF Centre, Cardiovascular Division, London SE1 1UL, UK.
Sean T SweeneyDepartment of Biology, University of York, York YO10 5DD, UK.
Mathias GautelKing's College BHF Centre, Cardiovascular Division, London SE1 1UL, UK.
John SparrowDepartment of Biology, University of York, York YO10 5DD, UK.
Belinda BullardDepartment of Biology, University of York, York YO10 5DD, UK belinda.bullard@york.ac.uk.
University of York · GBKing's College London · GB

Funding

Biotechnology and Biological Sciences Research Council BB/1012273/1Medical Research Council MR/J010456/1
6 · The paper itself

Abstract

Drosophila obscurin (Unc-89) is a titin-like protein in the M-line of the muscle sarcomere. Obscurin has two kinase domains near the C-terminus, both of which are predicted to be inactive. We have identified proteins binding to the kinase domains. Kinase domain 1 bound Bällchen (Ball, an active kinase), and both kinase domains 1 and 2 bound MASK (a 400-kDa protein with ankyrin repeats). Ball was present in the Z-disc and M-line of the indirect flight muscle (IFM) and was diffusely distributed in the sarcomere. MASK was present in both the M-line and the Z-disc. Reducing expression of Ball or MASK by siRNA resulted in abnormalities in the IFM, including missing M-lines and multiple Z-discs. Obscurin was still present, suggesting that the kinase domains act as a scaffold binding Ball and MASK. Unlike obscurin in vertebrate skeletal muscle, Drosophila obscurin is necessary for the correct assembly of the IFM sarcomere. We show that Ball and MASK act downstream of obscurin, and both are needed for development of a well defined M-line and Z-disc. The proteins have not previously been identified in Drosophila muscle.

Indexed as

AnimalsDNA-Binding ProteinsDrosophilaDrosophila ProteinsFlight, AnimalMuscle ProteinsMuscle, SkeletalProtamine KinaseProtein BindingProtein Interaction Domains and MotifsProtein KinasesSarcomeresBall protein, DrosophilaDNA-Binding ProteinsDrosophila ProteinsMask protein, DrosophilaMuscle ProteinsProtamine KinaseProtein KinasesUnc-89 protein, DrosophilaBallDrosophilaMASKM-lineObscurinUnc-89

Identifiers

PMID26251439
PMCPMC4582401
OpenAlexW2338000368

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.