Evidence map›Paper›PMID 28063874›Full record

ArticleDevelopmental biology2017

Polarity protein Par3/Bazooka follows myosin-dependent junction repositioning.

Mo Weng, Eric Wieschaus

Open access · greenAbstract read
In one paragraph

Article in Developmental biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
2.9field-weighted citation impact, top 9% 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

21 citing papers in PubMed, 38 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Transcriptional Control of Apical-Basal Polarity Regulators.International journal of molecular sciences · 2021
    Review
  7. Review
  8. Article
  9. Article
  10. Self-organized cytoskeletal alignment duringPhilosophical transactions of the Royal Society of London. Series B, Biological sciences · 2020
    Article
  11. Article
  12. Collective Migrations ofGenetics · 2020
    Review
  13. Article
  14. Article
  15. TheMolecular biology of the cell · 2019
    Article
  16. Article
  17. Review
  18. 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

2 authors at 2 institutions in 1 country.

Mo WengDepartment of Molecular Biology, Princeton University, USA.
Eric WieschausDepartment of Molecular Biology, Princeton University, USA; Howard Hughes Medical Institute, Princeton University, Princeton, NJ 08540, USA. Electronic address: efw@princeton.edu.
Howard Hughes Medical Institute · USPrinceton University · US

Funding

OOGENESIS AND EARLY EMBRYOGENESIS IN DROSOPHILAR37HD015587 · NICHD · PRINCETON UNIVERSITY · PI WIESCHAUS, ERIC F. · 1989 to 2015
$1.9M
Mechanosensitive remodeling of adherens junctions during snail-driven EMTK99HD088764 · NICHD · PRINCETON UNIVERSITY · PI WENG, MO · 2016 to 2017
$179k
NICHD NIH HHS K99 HD088764NICHD NIH HHS R37 HD015587
6 · The paper itself

Abstract

The polarity protein Par3/Bazooka (Baz) has been established as a central component of the apical basal polarity system that determines the position of cell-cell junctions in epithelial cells. Consistent with that view, we show that shortly before gastrulation in Drosophila, Baz protein in the mesoderm is down-regulated from junctional sites in response to Snail (Sna) expression. This down-regulation leads to a specific decrease in adherens junctions without affecting other E-Cadherin pools. However, we further show that, interactions between Baz and junctions are not unidirectional. During apical constriction and the internalization of the mesoderm, down-regulation of Baz is transiently blocked as adherens junctions shift apically and are strengthened in response to tension generated by contractile actomyosin. When such junction remodeling is prevented by down-regulating myosin, Baz is lost prematurely in mesodermal epithelium. During such apical shifts, Baz is initially left behind as the junction shifts position, but then re-accumulates at the new location of the junctions. On the dorsal side of the embryo, a similar pattern of myosin activity appears to limit the basal shift in junctions normally driven by Baz that controls epithelium folding. Our results suggest a model where the sensitivity of Baz to Sna expression leads to the Sna-dependent junction disassembly required for a complete epithelium-mesenchymal transition. Meanwhile this loss of Baz-dependent junction maintenance is countered by the myosin-based mechanism which promotes an apical shift and strengthening of junctions accompanied by a transient re-positioning and maintenance of Baz proteins.

Indexed as

ActomyosinAdherens JunctionsAnimalsDown-RegulationDrosophila melanogasterDrosophila ProteinsEpithelial-Mesenchymal TransitionEpitheliumFemaleIntracellular Signaling Peptides and ProteinsMaleMembrane ProteinsMesodermSnail Family Transcription FactorsActomyosinbaz protein, DrosophilaDrosophila ProteinsIntracellular Signaling Peptides and ProteinsMembrane ProteinsSnail Family Transcription Factorssna protein, Drosophila

Identifiers

PMID28063874
PMCPMC5515594
OpenAlexW2571262948

What OpenQuestion holds

Textmetadata
LicenceTDM
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.