ArticleJournal of cell science2022
A new mechanism of fibronectin fibril assembly revealed by live imaging and super-resolution microscopy.
Article in Journal of cell science, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 26 citations in OpenAlex.
- Fibrillar adhesion dynamics govern the timescales of nuclear mechano-response via the vimentin cytoskeleton.Nature materials · 2026Article
- Peritoneal macrophages regulate distal wound healing via endocrine release of plasma fibronectin.The Journal of clinical investigation · 2026Article
- A novel fibronectin-binding peptide reveals dynamic intermediate structures during matrix assembly.Scientific reports · 2025Article
- Extracellular ERp57 promotes fibronectin fibril formation during matrix assembly of articular cartilage.iScience · 2025Article
- Article
- EDA Fibronectin Microarchitecture and YAP Translocation during Wound Closure.ACS biomaterials science & engineering · 2025Article
- Fibronectin matrix assembly at a glance.Journal of cell science · 2025Review
- Mesodermal fibronectin controls cell shape, polarity, and mechanotransduction in the second heart field during cardiac outflow tract development.Developmental cell · 2025Article
- EDA Fibronectin Microarchitecture and YAP Translocation During Wound Closure.bioRxiv : the preprint server for biology · 2024Article
- A fibronectin gradient remodels mixed-phase mesoderm.Science advances · 2024Article
- Live imaging of Fibronectin 1a-mNeonGreen and Fibronectin 1b-mCherry knock-in alleles during early zebrafish development.Cells & development · 2024Article
- Assessing crosstalk in simultaneous multicolor single-molecule localization microscopy.Cell reports methods · 2023Article
- Initiation of fibronectin fibrillogenesis is an enzyme-dependent process.Cell reports · 2023Article
- Review
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Authors and funding
12 authors at 5 institutions in 1 country.
Funding
Abstract
Fibronectin (Fn1) fibrils have long been viewed as continuous fibers composed of extended, periodically aligned Fn1 molecules. However, our live-imaging and single-molecule localization microscopy data are inconsistent with this traditional view and show that Fn1 fibrils are composed of roughly spherical nanodomains containing six to eleven Fn1 dimers. As they move toward the cell center, Fn1 nanodomains become organized into linear arrays, in which nanodomains are spaced with an average periodicity of 105±17 nm. Periodical Fn1 nanodomain arrays can be visualized between cells in culture and within tissues; they are resistant to deoxycholate treatment and retain nanodomain periodicity in the absence of cells. The nanodomain periodicity in fibrils remained constant when probed with antibodies recognizing distinct Fn1 epitopes or combinations of antibodies recognizing epitopes spanning the length of Fn1. Treatment with FUD, a peptide that binds the Fn1 N-terminus and disrupts Fn1 fibrillogenesis, blocked the organization of Fn1 nanodomains into periodical arrays. These studies establish a new paradigm of Fn1 fibrillogenesis. This article has an associated First Person interview with the first author of the paper.
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Registered trials
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