Evidence map›Paper›PMID 33625865›Full record

ArticleMolecular biology of the cell2021

Fibronectin fibril alignment is established upon initiation of extracellular matrix assembly.

Carly M Garrison, Jean E Schwarzbauer

Open access · bronzeAbstract read
In one paragraph

Article in Molecular biology of the cell, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
2.0field-weighted citation impact, top 15% 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

17 citing papers in PubMed, 23 citations in OpenAlex.

  1. Article
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  3. Review
  4. Review
  5. Article
  6. Article
  7. Article
  8. FAK Differentially Mechanoregulates Cell Migration During Wound Closure.bioRxiv : the preprint server for biology · 2025
    Article
  9. Fibronectin matrix assembly at a glance.Journal of cell science · 2025
    Review
  10. Article
  11. Review
  12. Article
  13. Squishy matters - Corneal mechanobiology in health and disease.Progress in retinal and eye research · 2024
    Review
  14. Article
  15. Review
  16. Article
  17. 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 1 institution in 1 country.

Carly M GarrisonDepartment of Molecular Biology, Princeton University, Princeton, NJ 08544.
Jean E SchwarzbauerDepartment of Molecular Biology, Princeton University, Princeton, NJ 08544.
Princeton University · US

Funding

PREDOCTORAL TRAINING PROGRAM IN GENETICST32GM007388 · NIGMS · PRINCETON UNIVERSITY · PI CRISTEA, ILEANA M. · 1985 to 2022
$27.4M
Fibronectin-dependent mechanisms governing the assembly of a definitive extracellular matrixR01AR073236 · NIAMS · PRINCETON UNIVERSITY · PI SCHWARZBAUER, JEAN E · 2018 to 2022
$1.7M
NIAMS NIH HHS R01 AR073236NIGMS NIH HHS T32 GM007388
6 · The paper itself

Abstract

The physical structure of the extracellular matrix (ECM) is tissue-specific and fundamental to normal tissue function. Proper alignment of ECM fibers is essential for the functioning of a variety of tissues. While matrix assembly in general has been intensively investigated, little is known about the mechanisms required for formation of aligned ECM fibrils. We investigated the initiation of fibronectin (FN) matrix assembly using fibroblasts that assemble parallel ECM fibrils and found that matrix assembly sites, where FN fibrillogenesis is initiated, were oriented in parallel at the cell poles. We show that these polarized matrix assembly sites progress into fibrillar adhesions and ultimately into aligned FN fibrils. Cells that assemble an unaligned meshwork matrix form matrix assembly sites around the cell periphery, but the distribution of matrix assembly sites in these cells could be modulated through micropatterning or mechanical stretch. While an elongated cell shape corresponds with a polarized matrix assembly site distribution, these two features are not absolutely linked, since we discovered that transforming growth factor beta (TGF-β1) enhances matrix assembly site polarity and assembly of aligned fibrils independent of cell elongation. We conclude that the ultimate orientation of FN fibrils is determined by the alignment and distribution of matrix assembly sites that form during the initial stages of cell-FN interactions.

Indexed as

AnimalsBinding SitesCell Culture TechniquesCytoskeletonExtracellular MatrixFibroblastsFibronectinsHumansMiceNIH 3T3 CellsProtein BindingSignal TransductionTransforming Growth Factor betaTransforming Growth Factor beta1FibronectinsFN1 protein, humanTGFB1 protein, humanTransforming Growth Factor betaTransforming Growth Factor beta1

Identifiers

PMID33625865
PMCPMC8108514
OpenAlexW3133238214

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.