Evidence map›Paper›PMID 21084302›Full record

ArticleThe Journal of biological chemistry2011

N-cadherin cell-cell adhesion complexes are regulated by fibronectin matrix assembly.

Craig T Lefort, Katherine Wojciechowski, Denise C Hocking

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
1.1field-weighted citation impact, top 25% 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

26 citing papers in PubMed, 41 citations in OpenAlex.

  1. Trial
  2. Article
  3. Article
  4. Mutations in fibronectin dysregulate chondrogenesis in skeletal dysplasia.Cellular and molecular life sciences : CMLS · 2024
    Article
  5. Review
  6. Autocrine IL-6 drives cell and extracellular matrix anisotropy in scar fibroblasts.Matrix biology : journal of the International Society for Matrix Biology · 2023
    Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Pectoral Fin Anomalies inJournal of developmental biology · 2019
    Article
  14. Article
  15. 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

3 authors at 1 institution in 1 country.

Craig T LefortDepartment of Biomedical Engineering, University of Rochester School of Medicine and Dentistry, Rochester, New York 14642, USA.
Katherine Wojciechowski
Denise C Hocking
University of Rochester · US

Funding

MULTIDISCIPLINARY TRAINING IN PULMONARY RESEARCHT32HL066988 · NHLBI · UNIVERSITY OF ROCHESTER · PI GEORAS, STEVE N, O'REILLY, MICHAEL A · 2001 to 2021
$8.1M
Ultrasound Technologies for Tissue EngineeringR01EB008368 · NIBIB · UNIVERSITY OF ROCHESTER · PI DALECKI, DIANE, HOCKING, DENISE C · 2007 to 2010
$1.9M
Engineered Matrix Mimetics: Novel Therapies for Wound RepairR01GM081513 · NIGMS · UNIVERSITY OF ROCHESTER · PI HOCKING, DENISE C · 2009 to 2012
$1.2M
NHLBI NIH HHS T32 HL066988NHLBI NIH HHS T32HL066988NIBIB NIH HHS EB008368NIBIB NIH HHS R01 EB008368NIGMS NIH HHS GM081513NIGMS NIH HHS R01 GM081513
6 · The paper itself

Abstract

Fibronectin is a principal component of the extracellular matrix. Soluble fibronectin molecules are assembled into the extracellular matrix as insoluble, fibrillar strands via a cell-dependent process. In turn, the interaction of cells with the extracellular matrix form of fibronectin stimulates cell functions critical for tissue repair. Cross-talk between cell-cell and cell-extracellular matrix adhesion complexes is essential for the organization of cells into complex, functional tissue during embryonic development and tissue remodeling. Here, we demonstrate that fibronectin matrix assembly affects the organization, composition, and function of N-cadherin-based adherens junctions. Using fibronectin-null mouse embryonic myofibroblasts, we identified a novel quaternary complex composed of N-cadherin, β-catenin, tensin, and actin that exists in the absence of a fibronectin matrix. In the absence of fibronectin, homophilic N-cadherin ligation recruited both tensin and α5β1 integrins into nascent cell-cell adhesions. Initiation of fibronectin matrix assembly disrupted the association of tensin and actin with N-cadherin, released α5β1 integrins and tensin from cell-cell contacts, stimulated N-cadherin reorganization into thin cellular protrusions, and decreased N-cadherin adhesion. Fibronectin matrix assembly has been shown to recruit α5β1 integrins and tensin into fibrillar adhesions. Taken together, these studies suggest that tensin serves as a common cytoskeletal link for integrin- and cadherin-based adhesions and that the translocation of α5β1 integrins from cell-cell contacts into fibrillar adhesions during fibronectin matrix assembly is a novel mechanism by which cell-cell and cell-matrix adhesions are coordinated.

Indexed as

Adherens JunctionsAnimalsAntigens, CDCadherinsCell AdhesionCell CommunicationCells, CulturedExtracellular MatrixFibroblastsFibronectinsHumansIntegrin alpha5Integrin beta1MiceMice, Mutant StrainsMicrofilament ProteinsAntigens, CDCadherinsCDH2 protein, humanCdh2 protein, mouseFibronectinsIntegrin alpha5Integrin beta1Microfilament ProteinsTensins

Identifiers

PMID21084302
PMCPMC3024807
OpenAlexW2089910171

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.