Evidence map›Paper›PMID 20371600›Full record

ArticleThe Journal of biological chemistry2010

An O-glycosyltransferase promotes cell adhesion during development by influencing secretion of an extracellular matrix integrin ligand.

Liping Zhang, Duy T Tran, Kelly G Ten Hagen

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
2.6field-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

35 citing papers in PubMed, 55 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. In vivo models of mucin biosynthesis and function.Advanced drug delivery reviews · 2022
    Review
  5. RNAi-Mediated Silencing of Pgants Shows Core 1Frontiers in physiology · 2021
    Article
  6. Mucin-Type O-GalNAc Glycosylation in Health and Disease.Advances in experimental medicine and biology · 2021
    Article
  7. The Role of APPBiomolecules · 2020
    Review
  8. Differential splicing of the lectin domain of anThe Journal of biological chemistry · 2020
    Article
  9. Review
  10. Review
  11. Article
  12. Review
  13. Galnt11 regulates kidney function by glycosylating the endocytosis receptor megalin to modulate ligand binding.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  14. O-Linked glycosylation in Drosophila melanogaster.Current opinion in structural biology · 2019
    Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Two protein N-acetylgalactosaminyl transferases regulate synaptic plasticity by activity-dependent regulation of integrin signaling.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2014
    Article
  20. O-glycosylation regulates polarized secretion by modulating Tango1 stability.Proceedings of the National Academy of Sciences of the United States of America · 2014
    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 1 institution in 1 country.

Liping ZhangDevelopmental Glycobiology Unit, NIDCR, National Institutes of Health, Bethesda, Maryland 20892-4370, USA.
Duy T Tran
Kelly G Ten Hagen
National Institute of Dental and Craniofacial Research · US

Funding

Role of O-glycosylation in Animal DevelopmentZIADE000713 · NIDCR · NATIONAL INSTITUTE OF DENTAL & CRANIOFACIAL RESEARCH · PI TEN HAGEN, KELLY G · 2009 to 2025
$30.6M
Intramural NIH HHS
6 · The paper itself

Abstract

Protein secretion and localization are crucial during eukaryotic development, establishing local cell environments as well as mediating cell interactions, signaling, and adhesion. In this study, we demonstrate that the glycosyltransferase, pgant3, specifically modulates integrin-mediated cell adhesion by influencing the secretion and localization of the integrin ligand, Tiggrin. We demonstrate that Tiggrin is normally O-glycosylated and localized to the basal matrix where the dorsal and ventral cell layers adhere in wild type Drosophila wings. In pgant3 mutants, Tiggrin is no longer O-glycosylated and fails to be properly secreted to this basal cell layer interface, resulting in disruption of integrin-mediated cell adhesion in the wing. pgant3-mediated effects are dependent on enzymatic activity, as mutations that form a stable protein yet abrogate O-glycosyltransferase activity result in Tiggrin accumulation within the dorsal and ventral cells comprising the wing. Our results provide the first in vivo evidence for the role of O-glycosylation in the secretion of specific extracellular matrix proteins, thus altering the composition of the cellular "microenvironment" and thereby modulating developmentally regulated cell adhesion events. As alterations in cell adhesion are a hallmark of cancer progression, this work provides insight into the long-standing association between aberrant O-glycosylation and tumorigenesis.

Indexed as

Gene Expression Regulation, DevelopmentalAnimalsCell AdhesionChlorocebus aethiopsCOS CellsDrosophilaDrosophila ProteinsExtracellular MatrixFemaleGlycosyltransferasesIntegrinsLigandsMaleModels, BiologicalMutagenesisN-AcetylgalactosaminyltransferasesDrosophila ProteinsGlycosyltransferasesIntegrinsLigandsN-AcetylgalactosaminyltransferasesPgant3 protein, Drosophila

Identifiers

PMID20371600
PMCPMC2885228
OpenAlexW2019168420

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.