ArticleMolecular biology of the cell2009
Fibrillin assembly requires fibronectin.
Article in Molecular biology of the cell, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 146 papers.
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Who cites it
146 citing papers in PubMed, 251 citations in OpenAlex.
- SNED1 modulates ECM architecture and cell proliferation via its LDV integrin-binding motif.Journal of cell science · 2026Article
- SNED1 fibrillar assembly in the extracellular matrix requires fibronectin and collagen I.Journal of cell science · 2026Article
- The aorta in Marfan syndrome: from molecular mechanisms to mechanobiological dysfunction.Cardiovascular research · 2026Review
- Fibronectin-induced overactivation of αNature communications · 2026Article
- SNED1 fibrillar assembly in the extracellular matrix requires fibronectin and collagen I.bioRxiv : the preprint server for biology · 2026Article
- A macrophage-induced subpopulation of mesenchymal cells expressing Fcer1g contributes to wound-induced fibrosis.Nature communications · 2026Article
- Combined ADAMTS10 and ADAMTS17 inactivation exacerbates bone shortening and skin phenotypes.Life science alliance · 2025Article
- Glucocorticoid treatment rescues early lethality in a mouse model of geleophysic dysplasia.Communications biology · 2025Article
- Impact of N-linked glycans on the dual short fibulin/LTBP-4 axes regulating elastogenesis.The FEBS journal · 2025Article
- Exploring thoracic aorta ECM alterations in Marfan syndrome: insights into aorta wall structure.Scientific reports · 2025Article
- Fibronectin matrix assembly at a glance.Journal of cell science · 2025Review
- Mechanical forces in the tumor microenvironment: roles, pathways, and therapeutic approaches.Journal of translational medicine · 2025Review
- Calcification of the elastic component: the impact on the cardiovascular system.Frontiers in cardiovascular medicine · 2025Review
- TGFβ-mediated inhibition of hypodermal adipocyte progenitor differentiation promotes wound-induced skin fibrosis.Cell proliferation · 2025Article
- Extracellular matrix dysregulation in aging, calcification, and cancer diseases: insights into cellular senescence, inflammation, and novel therapeutic strategies.International journal of biological sciences · 2025Review
- Mutations in fibronectin dysregulate chondrogenesis in skeletal dysplasia.Cellular and molecular life sciences : CMLS · 2024Article
- Cytokine priming enhances the antifibrotic effects of human adipose derived mesenchymal stromal cells conditioned medium.Stem cell research & therapy · 2024Article
- Identification of a fibronectin-binding protein signature associated with idiopathic pulmonary fibrosis.Cells & development · 2024Article
- TGF-β1 Drives Integrin-Dependent Pericyte Migration and Microvascular Destabilization in Fibrotic Disease.The American journal of pathology · 2024Article
- Microfibril-associated glycoprotein 4 forms octamers that mediate interactions with elastogenic proteins and cells.Nature communications · 2024Article
86 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 2 countries.
Funding
Abstract
Fibrillins constitute the major backbone of multifunctional microfibrils in elastic and nonelastic extracellular matrices. Proper assembly mechanisms are central to the formation and function of these microfibrils, and their properties are often compromised in pathological circumstances such as in Marfan syndrome and in other fibrillinopathies. Here, we have used human dermal fibroblasts to analyze the assembly of fibrillin-1 in dependence of other matrix-forming proteins. siRNA knockdown experiments demonstrated that the assembly of fibrillin-1 is strictly dependent on the presence of extracellular fibronectin fibrils. Immunolabeling performed at the light and electron microscopic level showed colocalization of fibrillin-1 with fibronectin fibrils at the early stages of the assembly process. Protein-binding assays demonstrated interactions of fibronectin with a C-terminal region of fibrillin-1, -2, and -3 and with an N-terminal region of fibrillin-1. The C-terminal half of fibrillin-2 and -3 had propensities to multimerize, as has been previously shown for fibrillin-1. The C-terminal of all three fibrillins interacted strongly with fibronectin as multimers, but not as monomers. Mapping studies revealed that the major binding interaction between fibrillins and fibronectin involves the collagen/gelatin-binding region between domains FNI(6) and FNI(9).
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Registered trials
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.