Evidence map›Paper›PMID 24297939›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2013

Protein O-mannosylation is crucial for E-cadherin-mediated cell adhesion.

Mark Lommel, Patrick R Winterhalter, Tobias Willer, Maik Dahlhoff, Marlon R Schneider, Markus F Bartels, Ingrid Renner-Müller, Thomas Ruppert, Eckhard Wolf, Sabine Strahl

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.

0numbers the graph read from it
0cells of the map it votes in
46citing papers in PubMed
6.1field-weighted citation impact, top 3% 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, 85 citations in OpenAlex.

  1. Review
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  3. Recent progress inFood chemistry: X · 2024
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  15. Chemoenzymatic Assembly of Mammalian O-Mannose Glycans.Angewandte Chemie (International ed. in English) · 2018
    Article
  16. Review
  17. Discovery of an O-mannosylation pathway selectively serving cadherins and protocadherins.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  18. Article
  19. Review
  20. MammalianThe Journal of biological chemistry · 2017
    Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

10 authors at 2 institutions in 1 country.

Mark LommelCentre for Organismal Studies, Cell Chemistry and Center for Molecular Biology, University of Heidelberg, 69120 Heidelberg, Germany.
Patrick R Winterhalter
Tobias Willer
Maik Dahlhoff
Marlon R Schneider
Markus F Bartels
Ingrid Renner-Müller
Thomas Ruppert
Eckhard Wolf
Sabine Strahl
Ludwig-Maximilians-Universität München · DEHeidelberg University · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In recent years protein O-mannosylation has become a focus of attention as a pathomechanism underlying severe congenital muscular dystrophies associated with neuronal migration defects. A key feature of these disorders is the lack of O-mannosyl glycans on α-dystroglycan, resulting in abnormal basement membrane formation. Additional functions of O-mannosylation are still largely unknown. Here, we identify the essential cell-cell adhesion glycoprotein epithelial (E)-cadherin as an O-mannosylated protein and establish a functional link between O-mannosyl glycans and cadherin-mediated cell-cell adhesion. By genetically and pharmacologically blocking protein O-mannosyltransferases, we found that this posttranslational modification is essential for preimplantation development of the mouse embryo. O-mannosylation-deficient embryos failed to proceed from the morula to the blastocyst stage because of defects in the molecular architecture of cell-cell contact sites, including the adherens and tight junctions. Using mass spectrometry, we demonstrate that O-mannosyl glycans are present on E-cadherin, the major cell-adhesion molecule of blastomeres, and present evidence that this modification is generally conserved in cadherins. Further, the use of newly raised antibodies specific for an O-mannosyl-conjugated epitope revealed that these glycans are present on early mouse embryos. Finally, our cell-aggregation assays demonstrated that O-mannosyl glycans are crucial for cadherin-based cell adhesion. Our results redefine the significance of O-mannosylation in humans and other mammals, showing the immense impact of cadherins on normal as well as pathogenic cell behavior.

Indexed as

Adherens JunctionsAnimalsCadherinsCell AdhesionDNA PrimersDogsEmbryo, MammalianEmbryonic DevelopmentFluorescent Antibody TechniqueGlycosylationMadin Darby Canine Kidney CellsMannoseMass SpectrometryMicePolysaccharidesCadherinsDNA PrimersMannosePolysaccharidesmouse preimplantation developmentO-glycansPOMT1POMT2protein-glycosylation

Identifiers

PMID24297939
PMCPMC3876218
OpenAlexW2165186422

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.