ArticleThe Journal of biological chemistry2011
Fibronectin aggregation and assembly: the unfolding of the second fibronectin type III domain.
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 23 papers.
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Who cites it
23 citing papers in PubMed, 38 citations in OpenAlex.
- Cellular fibronectin exacerbates α-synuclein aggregation via integrin alpha4beta1 mediated PARP1 and SCD elevation.Neurotherapeutics : the journal of the American Society for Experimental NeuroTherapeutics · 2025Article
- Engineering programmable material-to-cell pathways via synthetic notch receptors to spatially control differentiation in multicellular constructs.Nature communications · 2024Article
- Astrocytic TIMP-1 regulates production of Anastellin, an inhibitor of oligodendrocyte differentiation and FTY720 responses.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Fibroblasts secrete fibronectin under lamellipodia in a microtubule- and myosin II-dependent fashion.The Journal of cell biology · 2023Article
- Anastellin impacts on the processing of extracellular matrix fibronectin and stimulates release of cytokines from coronary artery smooth muscle cells.Scientific reports · 2022Article
- Review
- Bioactive potential of natural biomaterials: identification, retention and assessment of biological properties.Signal transduction and targeted therapy · 2021Review
- Article
- Clinicopathologic Features and Outcomes in Fibronectin Glomerulopathy: A Case Series of 19 Patients.Frontiers in medicine · 2020Article
- Review
- Multiple Cryptic Binding Sites are Necessary for Robust Fibronectin Assembly: An In Silico Study.Scientific reports · 2017Article
- Cells lay their own tracks - optogenetic Cdc42 activation stimulates fibronectin deposition supporting directed migration.Journal of cell science · 2017Article
- Fibronectin Conformation and Assembly: Analysis of Fibronectin Deletion Mutants and Fibronectin Glomerulopathy (GFND) Mutants.Biochemistry · 2017Article
- Structure and unfolding of the third type III domain from human fibronectin.Biochemistry · 2015Article
- Fibronectin fibrillogenesis facilitates mechano-dependent cell spreading, force generation, and nuclear size in human embryonic fibroblasts.Integrative biology : quantitative biosciences from nano to macro · 2015Article
- Borrelia burgdorferi protein BBK32 binds to soluble fibronectin via the N-terminal 70-kDa region, causing fibronectin to undergo conformational extension.The Journal of biological chemistry · 2014Article
- Structural determinants of the interaction between the Haemophilus influenzae Hap autotransporter and fibronectin.Microbiology (Reading, England) · 2014Article
- A fibronectin-derived cell survival peptide belongs to a new class of epiviosamines.The Journal of investigative dermatology · 2014Article
- The structure of irisin reveals a novel intersubunit β-sheet fibronectin type III (FNIII) dimer: implications for receptor activation.The Journal of biological chemistry · 2013Article
- Fibronectin in tissue regeneration: timely disassembly of the scaffold is necessary to complete the build.Cellular and molecular life sciences : CMLS · 2013Review
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The mechanism of fibronectin (FN) assembly and the self-association sites are still unclear and contradictory, although the N-terminal 70-kDa region ((I)1-9) is commonly accepted as one of the assembly sites. We previously found that (I)1-9 binds to superfibronectin, which is an artificial FN aggregate induced by anastellin. In the present study, we found that (I)1-9 bound to the aggregate formed by anastellin and a small FN fragment, (III)1-2. An engineered disulfide bond in (III)2, which stabilizes folding, inhibited aggregation, but a disulfide bond in (III)1 did not. A gelatin precipitation assay showed that (I)1-9 did not interact with anastellin, (III)1, (III)2, (III)1-2, or several (III)1-2 mutants including (III)1-2KADA. (In contrast to previous studies, we found that the (III)1-2KADA mutant was identical in conformation to wild-type (III)1-2.) Because (I)1-9 only bound to the aggregate and the unfolding of (III)2 played a role in aggregation, we generated a (III)2 domain that was destabilized by deletion of the G strand. This mutant bound (I)1-9 as shown by the gelatin precipitation assay and fluorescence resonance energy transfer analysis, and it inhibited FN matrix assembly when added to cell culture. Next, we introduced disulfide mutations into full-length FN. Three disulfide locks in (III)2, (III)3, and (III)11 were required to dramatically reduce anastellin-induced aggregation. When we tested the disulfide mutants in cell culture, only the disulfide bond in (III)2 reduced the FN matrix. These results suggest that the unfolding of (III)2 is one of the key factors for FN aggregation and assembly.
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Registered trials
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