Evidence map›Paper›PMID 22232703›Full record

ArticleThe Journal of cell biology2012

α-Actinin-4/FSGS1 is required for Arp2/3-dependent actin assembly at the adherens junction.

Vivian W Tang, William M Brieher

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 81 papers.

0numbers the graph read from it
0cells of the map it votes in
81citing papers in PubMed
9.2field-weighted citation impact, top 1% 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

81 citing papers in PubMed, 156 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Review
  5. Characterization of early and late events of adherens junction assembly.bioRxiv : the preprint server for biology · 2024
    Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Review
  12. Article
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  14. Article
  15. Hexagonal patterning of the Drosophila eye.Developmental biology · 2021
    Review
  16. Article
  17. 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
  18. Review
  19. Podocyte Sphingolipid Signaling in Nephrotic Syndrome.Cellular physiology and biochemistry : international journal of experimental cellular physiology, biochemistry, and pharmacology · 2021
    Review
  20. F-Actin Dysplasia Involved in Organ of Corti Deformity inFrontiers in molecular neuroscience · 2021
    Article

21 more citing papers are in PubMed but not listed here.

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 1 institution in 1 country.

Vivian W TangDepartment of Cell and Developmental Biology, University of Illinois, Urbana, IL 61801, USA.
William M Brieher
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

We have developed an in vitro assay to study actin assembly at cadherin-enriched cell junctions. Using this assay, we demonstrate that cadherin-enriched junctions can polymerize new actin filaments but cannot capture preexisting filaments, suggesting a mechanism involving de novo synthesis. In agreement with this hypothesis, inhibition of Arp2/3-dependent nucleation abolished actin assembly at cell-cell junctions. Reconstitution biochemistry using the in vitro actin assembly assay identified α-actinin-4/focal segmental glomerulosclerosis 1 (FSGS1) as an essential factor. α-Actinin-4 specifically localized to sites of actin incorporation on purified membranes and at apical junctions in Madin-Darby canine kidney cells. Knockdown of α-actinin-4 decreased total junctional actin and inhibited actin assembly at the apical junction. Furthermore, a point mutation of α-actinin-4 (K255E) associated with FSGS failed to support actin assembly and acted as a dominant negative to disrupt actin dynamics at junctional complexes. These findings demonstrate that α-actinin-4 plays an important role in coupling actin nucleation to assembly at cadherin-based cell-cell adhesive contacts.

Indexed as

Actin CytoskeletonActininActin-Related Protein 2-3 ComplexActinsAdherens JunctionsAnimalsCadherinsCell AdhesionCell LineDogsPoint MutationPolymerizationActininActin-Related Protein 2-3 ComplexActinsCadherins

Identifiers

PMID22232703
PMCPMC3255975
OpenAlexW2000684972

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.