Evidence map›Paper›PMID 26504173›Full record

ArticleThe Journal of cell biology2015

Synaptopodin couples epithelial contractility to α-actinin-4-dependent junction maturation.

Nivetha Kannan, Vivian W Tang

Erratum issuedAbstract read
In one paragraph

Article in The Journal of cell biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
2.4field-weighted citation impact, top 13% 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

29 citing papers in PubMed, 52 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Urinary podocyte markers in diabetic kidney disease.Kidney research and clinical practice · 2024
    Article
  8. Review
  9. Article
  10. Article
  11. Review
  12. Renal cell markers: lighthouses for managing renal diseases.American journal of physiology. Renal physiology · 2021
    Article
  13. Article
  14. Cadherin puncta are interdigitated dynamic actin protrusions necessary for stable cadherin adhesion.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  15. Article
  16. Article
  17. Article
  18. Actin protrusions push at apical junctions to maintain E-cadherin adhesion.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  19. Article
  20. Mechanosensing and Mechanotransduction at Cell-Cell Junctions.Cold Spring Harbor perspectives in biology · 2018
    Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

2 authors at 1 institution in 1 country.

Nivetha KannanProgram in Global Public Health, University of Illinois, Urbana-Champaign, Champaign, IL 61801.
Vivian W TangDepartment of Cell and Developmental Biology, University of Illinois, Urbana-Champaign, Champaign, IL 61801 vtang@illinois.edu.
University of Illinois Urbana-Champaign · US

Funding

Disrupting FSGS1-associated Actin Assembly in GlomerulosclerosisR01DK098398 · NIDDK · UNIVERSITY OF ILLINOIS AT URBANA-CHAMPAIGN · PI TANG, VIVIAN · 2013 to 2017
$1.4M
NIDDK NIH HHS R01 DK098398
6 · The paper itself

Abstract

The epithelial junction experiences mechanical force exerted by endogenous actomyosin activities and from interactions with neighboring cells. We hypothesize that tension generated at cell-cell adhesive contacts contributes to the maturation and assembly of the junctional complex. To test our hypothesis, we used a hydraulic apparatus that can apply mechanical force to intercellular junction in a confluent monolayer of cells. We found that mechanical force induces α-actinin-4 and actin accumulation at the cell junction in a time- and tension-dependent manner during junction development. Intercellular tension also induces α-actinin-4-dependent recruitment of vinculin to the cell junction. In addition, we have identified a tension-sensitive upstream regulator of α-actinin-4 as synaptopodin. Synaptopodin forms a complex containing α-actinin-4 and β-catenin and interacts with myosin II, indicating that it can physically link adhesion molecules to the cellular contractile apparatus. Synaptopodin depletion prevents junctional accumulation of α-actinin-4, vinculin, and actin. Knockdown of synaptopodin and α-actinin-4 decreases the strength of cell-cell adhesion, reduces the monolayer permeability barrier, and compromises cellular contractility. Our findings underscore the complexity of junction development and implicate a control process via tension-induced sequential incorporation of junctional components.

Indexed as

Mechanotransduction, CellularTensile StrengthActin CytoskeletonActininActinsActomyosinAdherens JunctionsAmino Acid SequenceAnimalsbeta CateninCell AdhesionCell Adhesion MoleculesCell LineDogsEpithelial CellsHumansActininActinsActomyosinbeta CateninCell Adhesion MoleculesMultiprotein ComplexesMyosin Type IISynaptophysinVinculin

Identifiers

PMID26504173
PMCPMC4621826
OpenAlexW1859152884

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.