Evidence map›Paper›PMID 25737451›Full record

ArticleThe Journal of biological chemistry2015

Obstructor A organizes matrix assembly at the apical cell surface to promote enzymatic cuticle maturation in Drosophila.

Yanina-Yasmin Pesch, Dietmar Riedel, Matthias Behr

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
3.2field-weighted citation impact, top 8% 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

24 citing papers in PubMed, 74 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Frontiers in microbiology · 2026
    Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. The spider cuticle: a remarkable material toolbox for functional diversity.Philosophical transactions. Series A, Mathematical, physical, and engineering sciences · 2021
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Cuticular Structure Proteomics in the Pea AphidJournal of proteome research · 2020
    Article
  15. Article
  16. Article
  17. Article
  18. A comprehensive omics analysis and functional survey of cuticular proteins in the brown planthopper.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  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

3 authors at 3 institutions in 1 country.

Yanina-Yasmin PeschFrom the Department of Molecular Developmental Biology, Life & Medical Sciences Institute (LIMES), University of Bonn, 53115 Bonn, Germany, the Department of Cell & Developmental Biology, Translational Centre for Regenerative Medicine (TRM), University of Leipzig, 04103 Leipzig, Germany, and.
Dietmar Riedelthe Electron Microscopy Group, Max-Planck-Institute for Biophysical Chemistry, 37077 Göttingen, Germany.
Matthias BehrFrom the Department of Molecular Developmental Biology, Life & Medical Sciences Institute (LIMES), University of Bonn, 53115 Bonn, Germany, the Department of Cell & Developmental Biology, Translational Centre for Regenerative Medicine (TRM), University of Leipzig, 04103 Leipzig, Germany, and matthias.behr@uni-leipzig.de.
Leipzig University · DEMax Planck Institute for Biophysical Chemistry · DEUniversity of Bonn · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Assembly and maturation of the apical extracellular matrix (aECM) is crucial for protecting organisms, but underlying molecular mechanisms remain poorly understood. Epidermal cells secrete proteins and enzymes that assemble at the apical cell surface to provide epithelial integrity and stability during developmental growth and upon tissue damage. We analyzed molecular mechanisms of aECM assembly and identified the conserved chitin-binding protein Obst-A (Obstructor A) as an essential regulator. We show in Drosophila that Obst-A is required to coordinate protein and chitin matrix packaging at the apical cell surface during development. Secreted by epidermal cells, the Obst-A protein is specifically enriched in the apical assembly zone where matrix components are packaged into their highly ordered architecture. In obst-A null mutant larvae, the assembly zone is strongly diminished, resulting in severe disturbance of matrix scaffold organization and impaired aECM integrity. Furthermore, enzymes that support aECM stability are mislocalized. As a biological consequence, cuticle architecture, integrity, and function are disturbed in obst-A mutants, finally resulting in immediate lethality upon wounding. Our studies identify a new core organizing center, the assembly zone that controls aECM assembly at the apical cell surface. We propose a genetically conserved molecular mechanism by which Obst-A forms a matrix scaffold to coordinate trafficking and localization of proteins and enzymes in the newly deposited aECM. This mechanism is essential for maturation and stabilization of the aECM in a growing and remodeling epithelial tissue as an outermost barrier.

Indexed as

AmidohydrolasesAnimalsCarrier ProteinsChitinDrosophila melanogasterDrosophila ProteinsEmbryo, NonmammalianEpidermisEpithelial CellsExtracellular MatrixGene Expression Regulation, DevelopmentalLarvaLongevityProtein TransportSignal TransductionAmidohydrolasesCarrier ProteinsChitinDrosophila Proteinsknk protein, DrosophilaObst-A protein, Drosophilaserp protein, Drosophilaverm protein, DrosophilachitinCuticleDrosophilaEpidermisExtracellular MatrixFunctional GenomicsMembraneMolecular Genetics

Identifiers

PMID25737451
PMCPMC4400323
OpenAlexW2058203444

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.