Evidence map›Paper›PMID 21920314›Full record

ArticleDevelopmental cell2011

Dlg3 trafficking and apical tight junction formation is regulated by nedd4 and nedd4-2 e3 ubiquitin ligases.

Claude A Van Campenhout, Andrea Eitelhuber, Christian J Gloeckner, Patrizia Giallonardo, Moritz Gegg, Heide Oller, Seth G N Grant, Daniel Krappmann, Marius Ueffing, Heiko Lickert

Open access · greenAbstract read
In one paragraph

Article in Developmental cell, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing 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

34 citing papers in PubMed, 54 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Evidence for a nuclear role forMolecular biology of the cell · 2021
    Article
  7. Article
  8. Article
  9. IL-13 Impairs Tight Junctions in Airway Epithelia.International journal of molecular sciences · 2019
    Article
  10. Review
  11. Functions of EpCAM in physiological processes and diseases (Review).International journal of molecular medicine · 2018
    Review
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Protein monoubiquitylation: targets and diverse functions.Genes to cells : devoted to molecular & cellular mechanisms · 2015
    Review
  18. Article
  19. Article
  20. Review
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

10 authors at 3 institutions in 2 countries.

Claude A Van CampenhoutInstitute of Stem Cell Research, Helmholtz Zentrum München, 85764 Neuherberg, Germany.
Andrea Eitelhuber
Christian J Gloeckner
Patrizia Giallonardo
Moritz Gegg
Heide Oller
Seth G N Grant
Daniel Krappmann
Marius Ueffing
Heiko Lickert
Helmholtz Zentrum München · DESTZ eyetrial · DEWellcome Sanger Institute · GB

Funding

European Research Council 242807
6 · The paper itself

Abstract

The Drosophila Discs large (Dlg) scaffolding protein acts as a tumor suppressor regulating basolateral epithelial polarity and proliferation. In mammals, four Dlg homologs have been identified; however, their functions in cell polarity remain poorly understood. Here, we demonstrate that the X-linked mental retardation gene product Dlg3 contributes to apical-basal polarity and epithelial junction formation in mouse organizer tissues, as well as to planar cell polarity in the inner ear. We purified complexes associated with Dlg3 in polarized epithelial cells, including proteins regulating directed trafficking and tight junction formation. Remarkably, of the four Dlg family members, Dlg3 exerts a distinct function by recruiting the ubiquitin ligases Nedd4 and Nedd4-2 through its PPxY motifs. We found that these interactions are required for Dlg3 monoubiquitination, apical membrane recruitment, and tight junction consolidation. Our findings reveal an unexpected evolutionary diversification of the vertebrate Dlg family in basolateral epithelium formation.

Indexed as

Amino Acid SequenceAnimalsCell PolarityEar, InnerEndosomal Sorting Complexes Required for TransportFemaleGuanylate KinasesMaleMembrane ProteinsMiceMice, Inbred C57BLMice, KnockoutMolecular Sequence DataNedd4 Ubiquitin Protein LigasesProtein TransportTight JunctionsDlgh3 protein, mouseEndosomal Sorting Complexes Required for TransportGuanylate KinasesMembrane ProteinsNedd4l protein, mouseNedd4 Ubiquitin Protein LigasesUbiquitin-Protein Ligases

Identifiers

PMID21920314
PMCPMC4452538
OpenAlexW2148325247

What OpenQuestion holds

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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.