Evidence map›Paper›PMID 29748378›Full record

ArticleJournal of cell science2018

Myosin-1c promotes E-cadherin tension and force-dependent recruitment of α-actinin to the epithelial cell junction.

Nivetha Kannan, Vivian W Tang

Open access · bronzeAbstract read
In one paragraph

Article in Journal of cell science, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.6field-weighted citation impact, top 18% 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

19 citing papers in PubMed, 26 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Characterization of early and late events of adherens junction assembly.bioRxiv : the preprint server for biology · 2024
    Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. 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
  14. Article
  15. Article
  16. Polarity during tissue repair, a multiscale problem.Current opinion in cell biology · 2020
    Review
  17. 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
  18. Article
  19. 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

2 authors at 1 institution in 1 country.

Nivetha KannanDepartment of Cell and Developmental Biology, University of Illinois, Urbana-Champaign, IL 61801 USA.ORCID 0000-0003-3776-5253
Vivian W TangDepartment of Cell and Developmental Biology, University of Illinois, Urbana-Champaign, IL 61801 USA vtang@illinois.edu.ORCID 0000-0002-8821-6548
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

Actomyosin II contractility in epithelial cell plays an essential role in tension-dependent adhesion strengthening. One key unsettling question is how cellular contraction transmits force to the nascent cell-cell adhesion when there is no stable attachment between the nascent adhesion complex and actin filament. Here, we show that myosin-1c is localized to the lateral membrane of polarized epithelial cells and facilitates the coupling between actin and cell-cell adhesion. Knockdown of myosin-1c compromised the integrity of the lateral membrane, reduced the generation of tension at E-cadherin, decreased the strength of cell-cell cohesion in an epithelial cell monolayer and prevented force-dependent recruitment of junctional α-actinin. Application of exogenous force to cell-cell adhesions in a myosin-1c-knockdown cell monolayer fully rescued the localization defect of α-actinin, indicating that junction mechanoregulation remains intact in myosin-1c-depleted cells. Our study identifies a role of myosin-1c in force transmission at the lateral cell-cell interface and underscores a non-junctional contribution to tension-dependent junction regulation.

Indexed as

ActininCadherinsEpithelial CellsHumansIntercellular JunctionsMyosin Type IIActininCadherinsMyosin Type IICell–cell adhesionJunctionMechanobiologyMyosinSynaptopodinα-actinin

Identifiers

PMID29748378
PMCPMC6031380
OpenAlexW2802517349

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.