{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,15]],"date-time":"2026-10-15T17:15:26Z","timestamp":1792084526163,"version":"4.4.0"},"reference-count":124,"publisher":"The Company of Biologists","issue":"6","funder":[{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"crossref","award":["R01 AR073236"],"award-info":[{"award-number":["R01 AR073236"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"crossref"}]},{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"crossref","award":["T32 GM007388"],"award-info":[{"award-number":["T32 GM007388"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"crossref"}]},{"DOI":"10.13039\/100031445","name":"New Jersey Commission on Cancer Research","doi-asserted-by":"crossref","award":["COCR25PDF001"],"award-info":[{"award-number":["COCR25PDF001"]}],"id":[{"id":"10.13039\/100031445","id-type":"DOI","asserted-by":"crossref"}]},{"name":"Sud Cook '39 Fund for the Prevention of Addiction to Alcohol and other Mind-altering Drugs"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2025,3,15]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n               <jats:p>The organization and mechanics of extracellular matrix (ECM) protein polymers determine tissue structure and function. Secreted ECM components are assembled into polymers via a cell-mediated process. The specific mechanisms that cells use for assembly are crucial for generating tissue-appropriate matrices. Fibronectin (FN) is a ubiquitous and abundant ECM protein that is assembled into a fibrillar matrix by a receptor-mediated process, and the FN matrix provides a foundation for incorporation of many other proteins into the ECM. In this Cell Science at a Glance article and the accompanying poster, we describe the domain organization of FN and the events that initiate and propagate a stable insoluble network of FN fibrils. We also discuss intracellular pathways that regulate FN assembly and the impact of changes in assembly on disease progression.<\/jats:p>","DOI":"10.1242\/jcs.263834","type":"journal-article","created":{"date-parts":[[2025,3,25]],"date-time":"2025-03-25T08:46:59Z","timestamp":1742892419000},"source":"Crossref","is-referenced-by-count":22,"title":["Fibronectin matrix assembly at a glance"],"prefix":"10.1242","volume":"138","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-0877-7186","authenticated-orcid":false,"given":"Yu","family":"Sun","sequence":"first","affiliation":[{"name":"Princeton University Department of Molecular Biology , , Princeton, NJ 08544 ,","place":["USA"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Aaron J.","family":"Hamlin","sequence":"additional","affiliation":[{"name":"Princeton University Department of Molecular Biology , , Princeton, NJ 08544 ,","place":["USA"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-1012-7593","authenticated-orcid":false,"given":"Jean E.","family":"Schwarzbauer","sequence":"additional","affiliation":[{"name":"Princeton University Department of Molecular Biology , , Princeton, NJ 08544 ,","place":["USA"]}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"237","published-online":{"date-parts":[[2025,3,25]]},"reference":[{"key":"2025032504445049900_JCS263834C1","doi-asserted-by":"publisher","first-page":"27863","DOI":"10.1016\/S0021-9258(18)46866-4","article-title":"Fibronectin self-association is mediated by complementary sites within the amino-terminal one-third of the molecule","volume":"269","author":"Aguirre","year":"1994","journal-title":"J. Biol. Chem."},{"key":"2025032504445049900_JCS263834C2","doi-asserted-by":"publisher","first-page":"24756","DOI":"10.1016\/S0021-9258(17)31456-4","article-title":"The short amino acid sequence Pro-His-Ser-Arg-Asn in human fibronectin enhances cell adhesive function","volume":"269","author":"Aota","year":"1994","journal-title":"J. Biol. Chem."},{"key":"2025032504445049900_JCS263834C3","doi-asserted-by":"publisher","first-page":"5139","DOI":"10.1073\/pnas.072650799","article-title":"Fibronectin extension and unfolding within cell matrix fibrils controlled by cytoskeletal tension","volume":"99","author":"Baneyx","year":"2002","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"2025032504445049900_JCS263834C4","doi-asserted-by":"publisher","first-page":"3957","DOI":"10.1016\/S0021-9258(17)41727-3","article-title":"Interactions between fibronectin and chondroitin sulfate are modulated by molecular context","volume":"269","author":"Barkalow","year":"1994","journal-title":"J. Biol. Chem."},{"key":"2025032504445049900_JCS263834C5","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1016\/j.matbio.2017.04.003","article-title":"The provisional matrix: setting the stage for tissue repair outcomes","volume":"60-61","author":"Barker","year":"2017","journal-title":"Matrix Biol."},{"key":"2025032504445049900_JCS263834C6","doi-asserted-by":"publisher","first-page":"e202004198","DOI":"10.1083\/jcb.202004198","article-title":". alphav-Class integrin binding to fibronectin is solely mediated by RGD and unaffected by an RGE mutation","volume":"219","author":"Benito-Jardon","year":"2020","journal-title":"J. Cell Biol."},{"key":"2025032504445049900_JCS263834C7","doi-asserted-by":"crossref","first-page":"77","DOI":"10.1007\/978-3-642-16555-9_3","article-title":"Collagens, suprastructures, and collagen fibril assembly","volume-title":"The Extracellular Matrix: An Overview","author":"Birk","year":"2011"},{"key":"2025032504445049900_JCS263834C8","doi-asserted-by":"publisher","first-page":"a005082","DOI":"10.1101\/cshperspect.a005082","article-title":"Extracellular matrix in development: insights from mechanisms conserved between invertebrates and vertebrates","volume":"3","author":"Brown","year":"2011","journal-title":"Cold Spring Harb. Perspect. Biol."},{"key":"2025032504445049900_JCS263834C9","doi-asserted-by":"publisher","first-page":"2601","DOI":"10.1074\/jbc.273.5.2601","article-title":"Fibronectin fibrillogenesis involves the heparin II binding domain of fibronectin","volume":"273","author":"Bultmann","year":"1998","journal-title":"J. Biol. Chem."},{"key":"2025032504445049900_JCS263834C10","doi-asserted-by":"publisher","first-page":"18558","DOI":"10.1074\/jbc.270.31.18558","article-title":"Heparin binding by fibronectin module III-13 involves six discontinuous basic residues brought together to form a cationic cradle","volume":"270","author":"Busby","year":"1995","journal-title":"J. Biol. Chem."},{"key":"2025032504445049900_JCS263834C11","doi-asserted-by":"publisher","first-page":"429","DOI":"10.1111\/cge.13424","article-title":"Mechanistic insights into the cellular effects of a novel FN1 variant associated with a spondylometaphyseal dysplasia","volume":"94","author":"Cadoff","year":"2018","journal-title":"Clin. Genet."},{"key":"2025032504445049900_JCS263834C12","doi-asserted-by":"publisher","first-page":"14805","DOI":"10.1074\/jbc.M112.435271","article-title":"Regulation of matrix assembly through rigidity-dependent fibronectin conformational changes","volume":"288","author":"Carraher","year":"2013","journal-title":"J. Biol. Chem."},{"key":"2025032504445049900_JCS263834C13","doi-asserted-by":"publisher","first-page":"2538","DOI":"10.1073\/pnas.0707730105","article-title":"Mutations in FN1 cause glomerulopathy with fibronectin deposits","volume":"105","author":"Castelletti","year":"2008","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"2025032504445049900_JCS263834C14","doi-asserted-by":"publisher","first-page":"349","DOI":"10.1002\/sca.4950190505","article-title":"High-resolution cryo-scanning electron microscopy study of the macromolecular structure of fibronectin fibrils","volume":"19","author":"Chen","year":"1997","journal-title":"Scanning"},{"key":"2025032504445049900_JCS263834C15","doi-asserted-by":"publisher","first-page":"1074","DOI":"10.1161\/ATVBAHA.108.181081","article-title":"Fibronectin is an important regulator of flow-induced vascular remodeling","volume":"29","author":"Chiang","year":"2009","journal-title":"Arterioscler. Thromb. Vasc. Biol."},{"key":"2025032504445049900_JCS263834C16","doi-asserted-by":"publisher","first-page":"927","DOI":"10.1091\/mbc.2.11.927","article-title":"Tenascin variants: differential binding to fibronectin and distinct distribution in cell cultures and tissues","volume":"2","author":"Chiquet-Ehrismann","year":"1991","journal-title":"Cell Reg."},{"key":"2025032504445049900_JCS263834C17","doi-asserted-by":"publisher","first-page":"347","DOI":"10.1016\/j.ccell.2019.01.007","article-title":"Integrin signaling in cancer: mechanotransduction, stemness, epithelial plasticity, and therapeutic resistance","volume":"35","author":"Cooper","year":"2019","journal-title":"Cancer Cell"},{"key":"2025032504445049900_JCS263834C18","doi-asserted-by":"publisher","first-page":"89","DOI":"10.1146\/annurev-cellbio-100109-104126","article-title":"Transmembrane signaling proteoglycans","volume":"26","author":"Couchman","year":"2010","journal-title":"Annu. Rev. Cell Dev. Biol."},{"key":"2025032504445049900_JCS263834C19","doi-asserted-by":"publisher","first-page":"1708","DOI":"10.1126\/science.1064829","article-title":"Taking cell-matrix adhesions to the third dimension","volume":"294","author":"Cukierman","year":"2001","journal-title":"Science"},{"key":"2025032504445049900_JCS263834C20","doi-asserted-by":"publisher","first-page":"2443","DOI":"10.3390\/cells10092443","article-title":"Fibronectin: molecular structure, fibrillar structure and mechanochemical signaling","volume":"10","author":"Dalton","year":"2021","journal-title":"Cells"},{"key":"2025032504445049900_JCS263834C21","doi-asserted-by":"publisher","first-page":"C536","DOI":"10.1152\/ajpcell.00226.2022","article-title":"Fibronectin isoforms in skeletal development and associated disorders","volume":"323","author":"Dinesh","year":"2022","journal-title":"Am. J. Physiol. Cell Physiol."},{"key":"2025032504445049900_JCS263834C22","doi-asserted-by":"publisher","first-page":"605","DOI":"10.1242\/jcs.100.3.605","article-title":"Arrangement of cellular fibronectin in noncollagenous fibrils in human fibroblast cultures","volume":"100","author":"Dzamba","year":"1991","journal-title":"J. Cell Sci."},{"key":"2025032504445049900_JCS263834C23","doi-asserted-by":"publisher","first-page":"7381","DOI":"10.1016\/S0021-9258(18)34388-6","article-title":"Arrangement of attachment-promoting, self-association, and heparin-binding sites in horse serum fibronectin","volume":"257","author":"Ehrismann","year":"1982","journal-title":"J. Biol. Chem."},{"key":"2025032504445049900_JCS263834C24","doi-asserted-by":"publisher","first-page":"10114","DOI":"10.1073\/pnas.91.21.10114","article-title":"Reversible unfolding of fibronectin type III and immunoglobulin domains provides the structural basis for stretch and elasticity of titin and fibronectin","volume":"91","author":"Erickson","year":"1994","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"2025032504445049900_JCS263834C25","doi-asserted-by":"publisher","first-page":"98","DOI":"10.1016\/j.sbi.2016.12.002","article-title":"Protein unfolding under isometric tension\u2014what force can integrins generate, and can it unfold FNIII domains?","volume":"42","author":"Erickson","year":"2017","journal-title":"Curr. Opin. Struct. Biol."},{"key":"2025032504445049900_JCS263834C26","doi-asserted-by":"publisher","first-page":"7275","DOI":"10.1038\/ncomms8275","article-title":"Molecular architecture of native fibronectin fibrils","volume":"6","author":"Fruh","year":"2015","journal-title":"Nat. Commun."},{"key":"2025032504445049900_JCS263834C27","doi-asserted-by":"publisher","first-page":"1319","DOI":"10.1177\/28.12.7014712","article-title":"Fibronectin presence in native collagen fibrils of human fibroblasts: immunoperoxidase and immunoferritin localization","volume":"28","author":"Furcht","year":"1980","journal-title":"J. Histochem. Cytochem."},{"key":"2025032504445049900_JCS263834C28","doi-asserted-by":"publisher","first-page":"999","DOI":"10.1083\/jcb.200707150","article-title":"Requirements for sulfate transport and the diastrophic dysplasia sulfate transporter in fibronectin matrix assembly","volume":"179","author":"Galante","year":"2007","journal-title":"J. Cell Biol."},{"key":"2025032504445049900_JCS263834C29","doi-asserted-by":"publisher","first-page":"739","DOI":"10.1091\/mbc.E20-08-0533","article-title":"Fibronectin fibril alignment is established upon initiation of extracellular matrix assembly","volume":"32","author":"Garrison","year":"2021","journal-title":"Mol. Biol. Cell"},{"key":"2025032504445049900_JCS263834C30","doi-asserted-by":"publisher","first-page":"e2373","DOI":"10.1371\/journal.pone.0002373","article-title":"Fibronectin unfolding revisited: modeling cell traction-mediated unfolding of the tenth type-III repeat","volume":"3","author":"Gee","year":"2008","journal-title":"PLoS ONE"},{"key":"2025032504445049900_JCS263834C31","doi-asserted-by":"publisher","first-page":"793","DOI":"10.1038\/35099066","article-title":"Transmembrane extracellular matrix-cytoskeleton crosstalk","volume":"2","author":"Geiger","year":"2001","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"2025032504445049900_JCS263834C32","doi-asserted-by":"publisher","first-page":"1079","DOI":"10.1242\/dev.119.4.1079","article-title":"Defects in mesoderm, neural tube and vascular development in mouse embryos lacking fibronectin","volume":"119","author":"George","year":"1993","journal-title":"Development"},{"key":"2025032504445049900_JCS263834C33","doi-asserted-by":"publisher","first-page":"200377","DOI":"10.1098\/rsob.200377","article-title":"Syndecan receptors: pericellular regulators in development and inflammatory disease","volume":"11","author":"Gopal","year":"2021","journal-title":"Open Biol"},{"key":"2025032504445049900_JCS263834C34","doi-asserted-by":"publisher","first-page":"3190","DOI":"10.1091\/mbc.e14-05-1026","article-title":"Studying early stages of fibronectin fibrillogenesis in living cells by atomic force microscopy","volume":"26","author":"Gudzenko","year":"2015","journal-title":"Mol. Biol. Cell"},{"key":"2025032504445049900_JCS263834C35","doi-asserted-by":"publisher","first-page":"1378","DOI":"10.1042\/BST20120103","article-title":"Rho family GTPases","volume":"40","author":"Hall","year":"2012","journal-title":"Biochem. Soc. Trans."},{"key":"2025032504445049900_JCS263834C36","doi-asserted-by":"publisher","first-page":"101479","DOI":"10.1016\/j.jbc.2021.101479","article-title":"Heparan sulfate is necessary for the early formation of nascent fibronectin and collagen I fibrils at matrix assembly sites","volume":"298","author":"Hill","year":"2022","journal-title":"J. Biol. Chem."},{"key":"2025032504445049900_JCS263834C37","doi-asserted-by":"publisher","first-page":"19183","DOI":"10.1016\/S0021-9258(17)32292-5","article-title":"Fibronectin's III-1 module contains a conformation-dependent binding site for the amino-terminal region of fibronectin","volume":"269","author":"Hocking","year":"1994","journal-title":"J. Biol. Chem."},{"key":"2025032504445049900_JCS263834C38","doi-asserted-by":"publisher","first-page":"431","DOI":"10.1083\/jcb.133.2.431","article-title":"A novel role for the integrin-binding III-10 module in fibronectin matrix assembly","volume":"133","author":"Hocking","year":"1996","journal-title":"J. Cell Biol."},{"key":"2025032504445049900_JCS263834C39","doi-asserted-by":"publisher","first-page":"25879","DOI":"10.1074\/jbc.M109.024125","article-title":"Fibronectin binds and enhances the activity of bone morphogenetic protein 1","volume":"284","author":"Huang","year":"2009","journal-title":"J. Biol. Chem."},{"key":"2025032504445049900_JCS263834C40","doi-asserted-by":"publisher","first-page":"e202204100","DOI":"10.1083\/jcb.202204100","article-title":"Fibroblasts secrete fibronectin under lamellipodia in a microtubule- and myosin II-dependent fashion","volume":"222","author":"Huet-Calderwood","year":"2023","journal-title":"J. Cell Biol."},{"key":"2025032504445049900_JCS263834C41","doi-asserted-by":"publisher","first-page":"521","DOI":"10.1016\/S0092-8674(00)81892-9","article-title":"Suppression of integrin activation: A novel function of a Ras\/Raf-initiated MAP kinase pathway","volume":"88","author":"Hughes","year":"1997","journal-title":"Cell"},{"key":"2025032504445049900_JCS263834C42","doi-asserted-by":"publisher","first-page":"14","DOI":"10.1016\/j.ceb.2018.08.004","article-title":"Signal transduction via integrin adhesion complexes","volume":"56","author":"Humphries","year":"2019","journal-title":"Curr. Opin. Cell Biol."},{"key":"2025032504445049900_JCS263834C43","doi-asserted-by":"crossref","DOI":"10.1007\/978-1-4612-3264-3","volume-title":"Fibronectins","author":"Hynes","year":"1990"},{"key":"2025032504445049900_JCS263834C44","doi-asserted-by":"publisher","first-page":"673","DOI":"10.1016\/S0092-8674(02)00971-6","article-title":"Integrins: bidirectional, allosteric signaling machines","volume":"110","author":"Hynes","year":"2002","journal-title":"Cell"},{"key":"2025032504445049900_JCS263834C45","doi-asserted-by":"publisher","first-page":"1216","DOI":"10.1126\/science.1176009","article-title":"The extracellular matrix: not just pretty fibrils","volume":"326","author":"Hynes","year":"2009","journal-title":"Science"},{"key":"2025032504445049900_JCS263834C46","doi-asserted-by":"publisher","first-page":"875","DOI":"10.1016\/0092-8674(78)90272-6","article-title":"Relationships between fibronectin (LETS protein) and actin","volume":"15","author":"Hynes","year":"1978","journal-title":"Cell"},{"key":"2025032504445049900_JCS263834C47","volume-title":"Extracellular Matrix Biology","author":"Hynes","year":"2012"},{"key":"2025032504445049900_JCS263834C48","doi-asserted-by":"publisher","first-page":"177","DOI":"10.1242\/jcs.00845","article-title":"FAK promotes organization of fibronectin matrix and fibrillar adhesions","volume":"117","author":"Ilic","year":"2004","journal-title":"J. Cell Sci."},{"key":"2025032504445049900_JCS263834C49","doi-asserted-by":"publisher","first-page":"e01907-20","DOI":"10.1128\/mBio.01907-20","article-title":"Syndecan-1 promotes Streptococcus pneumoniae corneal infection by facilitating the assembly of adhesive fibronectin fibrils","volume":"11","author":"Jinno","year":"2020","journal-title":"mBio"},{"key":"2025032504445049900_JCS263834C50","doi-asserted-by":"publisher","first-page":"15473","DOI":"10.1074\/jbc.274.22.15473","article-title":"The compact conformation of fibronectin is determined by intramolecular ionic interactions","volume":"274","author":"Johnson","year":"1999","journal-title":"J. Biol. Chem."},{"key":"2025032504445049900_JCS263834C51","doi-asserted-by":"publisher","first-page":"495","DOI":"10.1016\/j.ceb.2008.06.008","article-title":"Collagen fibrillogenesis: fibronectin, integrins, and minor collagens as organizers and nucleators","volume":"20","author":"Kadler","year":"2008","journal-title":"Curr. Opin. Cell Biol."},{"key":"2025032504445049900_JCS263834C52","doi-asserted-by":"publisher","first-page":"3445","DOI":"10.1074\/jbc.M805025200","article-title":"Probing the conformation of the fibronectin III1\u20132 domain by fluorescence resonance energy transfer","volume":"284","author":"Karuri","year":"2009","journal-title":"J. Biol. Chem."},{"key":"2025032504445049900_JCS263834C53","doi-asserted-by":"publisher","first-page":"493","DOI":"10.1242\/jcs.113.3.493","article-title":"Control of extracellular matrix assembly by syndecan-2 proteoglycan","volume":"113","author":"Klass","year":"2000","journal-title":"J. Cell Sci."},{"key":"2025032504445049900_JCS263834C54","doi-asserted-by":"publisher","first-page":"815","DOI":"10.1016\/j.ajhg.2017.09.019","article-title":"Mutations in fibronectin cause a subtype of Spondylometaphyseal dysplasia with \u201cCorner Fractures\u201d","volume":"101","author":"Lee","year":"2017","journal-title":"Am. J. Hum. Genet."},{"key":"2025032504445049900_JCS263834C55","doi-asserted-by":"publisher","first-page":"245","DOI":"10.1006\/jmbi.1998.1863","article-title":"Formation of amyloid-like fibrils by self-association of a partially unfolded fibronectin type III module","volume":"280","author":"Litvinovich","year":"1998","journal-title":"J. Mol. Biol."},{"key":"2025032504445049900_JCS263834C56","doi-asserted-by":"publisher","first-page":"104622","DOI":"10.1016\/j.jbc.2023.104622","article-title":"Nucleation of fibronectin fibril assembly requires binding between heparin and the 13th type III module of fibronectin","volume":"299","author":"Lovett","year":"2023","journal-title":"J. Biol. Chem."},{"key":"2025032504445049900_JCS263834C57","doi-asserted-by":"publisher","first-page":"631","DOI":"10.1016\/j.devcel.2020.01.007","article-title":"Basement membrane regulates fibronectin organization using sliding focal adhesions driven by a contractile winch","volume":"52","author":"Lu","year":"2020","journal-title":"Dev. Cell"},{"key":"2025032504445049900_JCS263834C58","doi-asserted-by":"publisher","first-page":"295","DOI":"10.1083\/jcb.139.1.295","article-title":"Modulation of cell-adhesive activity of fibronectin by the alternatively spliced EDA segment","volume":"139","author":"Manabe","year":"1997","journal-title":"J. Cell Biol."},{"key":"2025032504445049900_JCS263834C59","doi-asserted-by":"publisher","first-page":"4427","DOI":"10.1242\/jcs.02566","article-title":"Stimulatory effects of a three-dimensional microenvironment on cell-mediated fibronectin fibrillogenesis","volume":"118","author":"Mao","year":"2005","journal-title":"J. Cell Sci."},{"key":"2025032504445049900_JCS263834C60","doi-asserted-by":"publisher","first-page":"642","DOI":"10.1016\/j.matbio.2007.06.001","article-title":"The heparin III-binding domain of fibronectin (III4\u20135 repeats) binds to fibronectin and inhibits fibronectin matrix assembly","volume":"26","author":"Maqueda","year":"2007","journal-title":"Matrix Biol."},{"key":"2025032504445049900_JCS263834C61","doi-asserted-by":"publisher","first-page":"4711","DOI":"10.1096\/fj.09-151282","article-title":"The 12th-14th type III repeats of fibronectin function as a highly promiscuous growth factor-binding domain","volume":"24","author":"Martino","year":"2010","journal-title":"FASEB J."},{"key":"2025032504445049900_JCS263834C62","doi-asserted-by":"publisher","first-page":"4007","DOI":"10.1016\/j.cell.2023.07.036","article-title":"TGF-beta signaling in health and disease","volume":"186","author":"Massague","year":"2023","journal-title":"Cell"},{"key":"2025032504445049900_JCS263834C63","doi-asserted-by":"publisher","first-page":"41087","DOI":"10.1074\/jbc.M110.153692","article-title":"Extended binding site on fibronectin for the functional upstream domain of protein F1 of Streptococcus pyogenes","volume":"285","author":"Maurer","year":"2010","journal-title":"J. Biol. Chem."},{"key":"2025032504445049900_JCS263834C64","doi-asserted-by":"publisher","first-page":"213","DOI":"10.1080\/10409238.2016.1184224","article-title":"Dynamic structure of plasma fibronectin","volume":"51","author":"Maurer","year":"2016","journal-title":"Crit. Rev. Biochem. Mol. Biol."},{"key":"2025032504445049900_JCS263834C65","doi-asserted-by":"publisher","first-page":"2957","DOI":"10.1016\/S0021-9258(18)61453-X","article-title":"Fibronectin's cell-adhesive domain and an amino-terminal matrix assembly domain participate in its assembly into fibroblast pericellular matrix","volume":"262","author":"McDonald","year":"1987","journal-title":"J. Biol. Chem."},{"key":"2025032504445049900_JCS263834C66","doi-asserted-by":"publisher","first-page":"466","DOI":"10.1083\/jcb.97.2.466","article-title":"Binding of plasma fibronectin to cell layers of human skin fibroblasts","volume":"97","author":"McKeown-Longo","year":"1983","journal-title":"J. Cell Biol."},{"key":"2025032504445049900_JCS263834C67","doi-asserted-by":"publisher","first-page":"364","DOI":"10.1083\/jcb.100.2.364","article-title":"Interaction of the 70,000-mol. wt. amino terminal fragment of fibronectin with matrix-assembly receptor of fibroblasts","volume":"100","author":"McKeown-Longo","year":"1985","journal-title":"J. Cell Biol."},{"key":"2025032504445049900_JCS263834C68","first-page":"425","article-title":"The extracellular matrix: an overview","volume-title":"Biology of Extracellular Matrix","author":"Mecham","year":"2011"},{"key":"2025032504445049900_JCS263834C69","doi-asserted-by":"publisher","first-page":"112473","DOI":"10.1016\/j.celrep.2023.112473","article-title":"Initiation of fibronectin fibrillogenesis is an enzyme-dependent process","volume":"42","author":"Melamed","year":"2023","journal-title":"Cell Rep."},{"key":"2025032504445049900_JCS263834C70","doi-asserted-by":"publisher","first-page":"3601","DOI":"10.1091\/mbc.e02-05-0292","article-title":"Tenascin-C modulates matrix contraction via focal adhesion kinase- and Rho-mediated signaling pathways","volume":"13","author":"Midwood","year":"2002","journal-title":"Mol. Biol. Cell"},{"key":"2025032504445049900_JCS263834C71","doi-asserted-by":"publisher","first-page":"5670","DOI":"10.1091\/mbc.e04-08-0759","article-title":"Coregulation of fibronectin signaling and matrix contraction by tenascin-C and syndecan-4","volume":"15","author":"Midwood","year":"2004","journal-title":"Mol. Biol. Cell"},{"key":"2025032504445049900_JCS263834C72","doi-asserted-by":"publisher","first-page":"2342","DOI":"10.1091\/mbc.e14-03-0800","article-title":"Effects of high glucose on integrin activity and fibronectin matrix assembly by mesangial cells","volume":"25","author":"Miller","year":"2014","journal-title":"Mol. Biol. Cell"},{"key":"2025032504445049900_JCS263834C73","doi-asserted-by":"publisher","first-page":"516","DOI":"10.1016\/j.ceb.2006.08.011","article-title":"Integrin-regulated FAK-Src signaling in normal and cancer cells","volume":"18","author":"Mitra","year":"2006","journal-title":"Curr. Opin. Cell Biol."},{"key":"2025032504445049900_JCS263834C74","doi-asserted-by":"publisher","first-page":"193","DOI":"10.1038\/367193a0","article-title":"Superfibronectin is a functionally distinct form of fibronectin","volume":"367","author":"Morla","year":"1994","journal-title":"Nature"},{"key":"2025032504445049900_JCS263834C75","doi-asserted-by":"publisher","first-page":"100528","DOI":"10.1016\/j.mcpro.2023.100528","article-title":"Ten years of extracellular matrix proteomics: accomplishments, challenges, and future perspectives","volume":"22","author":"Naba","year":"2023","journal-title":"Mol. Cell. Proteomics"},{"key":"2025032504445049900_JCS263834C76","doi-asserted-by":"publisher","first-page":"M111.014647","DOI":"10.1074\/mcp.M111.014647","article-title":"The matrisome: in silico definition and in vivo characterization by proteomics of normal and tumor extracellular matrices","volume":"11","author":"Naba","year":"2012","journal-title":"Mol. Cell. Proteomics"},{"key":"2025032504445049900_JCS263834C77","doi-asserted-by":"publisher","first-page":"4297","DOI":"10.1128\/mcb.7.12.4297-4307.1987","article-title":"Alternative splicing of chicken fibronectin in embryos and in normal and transformed cells","volume":"7","author":"Norton","year":"1987","journal-title":"Mol. Cell. Biol."},{"key":"2025032504445049900_JCS263834C78","doi-asserted-by":"publisher","first-page":"39143","DOI":"10.1074\/jbc.M509082200","article-title":"Domain unfolding plays a role in superfibronectin formation","volume":"280","author":"Ohashi","year":"2005","journal-title":"J. Biol. Chem."},{"key":"2025032504445049900_JCS263834C79","doi-asserted-by":"publisher","first-page":"2153","DOI":"10.1073\/pnas.96.5.2153","article-title":"Dynamics and elasticity of the fibronectin matrix in living cell culture visualized by fibronectin\u2013green fluorescent protein","volume":"96","author":"Ohashi","year":"1999","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"2025032504445049900_JCS263834C80","doi-asserted-by":"publisher","first-page":"1221","DOI":"10.1242\/jcs.115.6.1221","article-title":"Dual labeling of the fibronectin matrix and actin cytoskeleton with green fluorescent protein variants","volume":"115","author":"Ohashi","year":"2002","journal-title":"J. Cell Sci."},{"key":"2025032504445049900_JCS263834C81","doi-asserted-by":"publisher","first-page":"4584","DOI":"10.1021\/acs.biochem.7b00589","article-title":"Fibronectin conformation and assembly: analysis of fibronectin deletion mutants and Fibronectin Glomerulopathy (GFND) mutants","volume":"56","author":"Ohashi","year":"2017","journal-title":"Biochemistry"},{"key":"2025032504445049900_JCS263834C82","doi-asserted-by":"publisher","first-page":"3861","DOI":"10.1242\/jcs.00059","article-title":"Fibronectin at a glance","volume":"115","author":"Pankov","year":"2002","journal-title":"J. Cell Sci."},{"key":"2025032504445049900_JCS263834C83","doi-asserted-by":"publisher","first-page":"1075","DOI":"10.1083\/jcb.148.5.1075","article-title":"Integrin dynamics and matrix assembly: tensin-dependent translocation of alpha(5)beta(1) integrins promotes early fibronectin fibrillogenesis","volume":"148","author":"Pankov","year":"2000","journal-title":"J. Cell Biol."},{"key":"2025032504445049900_JCS263834C84","doi-asserted-by":"publisher","first-page":"107","DOI":"10.1016\/j.matbio.2017.11.012","article-title":"Heparin-fibronectin interactions in the development of extracellular matrix insolubility","volume":"67","author":"Raitman","year":"2018","journal-title":"Matrix Biol."},{"key":"2025032504445049900_JCS263834C85","doi-asserted-by":"publisher","first-page":"1093","DOI":"10.1177\/15353702221087175","article-title":"Implications of fibrotic extracellular matrix in diabetic retinopathy","volume":"247","author":"Resnikoff","year":"2022","journal-title":"Exp. Biol. Med. (Maywood)"},{"key":"2025032504445049900_JCS263834C86","doi-asserted-by":"publisher","first-page":"509","DOI":"10.1515\/bchm3.1985.366.1.509","article-title":"Aggregation and fibril formation of plasma fibronectin by heparin","volume":"366","author":"Richter","year":"1985","journal-title":"Biol. Chem. Hoppe Seyler"},{"key":"2025032504445049900_JCS263834C87","doi-asserted-by":"publisher","first-page":"375","DOI":"10.1146\/annurev.bi.57.070188.002111","article-title":"Fibronectin and its receptors","volume":"57","author":"Ruoslahti","year":"1988","journal-title":"Annu. Rev. Biochem."},{"key":"2025032504445049900_JCS263834C88","doi-asserted-by":"publisher","first-page":"846","DOI":"10.1091\/mbc.e08-08-0830","article-title":"Fibrillin assembly requires fibronectin","volume":"20","author":"Sabatier","year":"2009","journal-title":"Mol. Biol. Cell"},{"key":"2025032504445049900_JCS263834C89","doi-asserted-by":"publisher","first-page":"2805","DOI":"10.1073\/pnas.96.6.2805","article-title":"Syndecan-4 signals cooperatively with integrins in a Rho-dependent manner in the assembly of focal adhesions and actin stress fibers","volume":"96","author":"Saoncella","year":"1999","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"2025032504445049900_JCS263834C90","doi-asserted-by":"publisher","first-page":"a005066","DOI":"10.1101\/cshperspect.a005066","article-title":"Integrins and extracellular matrix in mechanotransduction","volume":"2","author":"Schwartz","year":"2010","journal-title":"Cold Spring Harb. Perspect. Biol."},{"key":"2025032504445049900_JCS263834C91","doi-asserted-by":"publisher","first-page":"1463","DOI":"10.1083\/jcb.113.6.1463","article-title":"Identification of the fibronectin sequences required for assembly of a fibrillar matrix","volume":"113","author":"Schwarzbauer","year":"1991","journal-title":"J. Cell Biol."},{"key":"2025032504445049900_JCS263834C92","doi-asserted-by":"publisher","first-page":"421","DOI":"10.1016\/0092-8674(83)90175-7","article-title":"Three different fibronectin mRNAs arise by alternative splicing within the coding region","volume":"35","author":"Schwarzbauer","year":"1983","journal-title":"Cell"},{"key":"2025032504445049900_JCS263834C93","doi-asserted-by":"publisher","first-page":"573","DOI":"10.1083\/jcb.134.2.573","article-title":"Altered rate of fibronectin matrix assembly by deletion of the first type III repeats","volume":"134","author":"Sechler","year":"1996","journal-title":"J. Cell Biol."},{"key":"2025032504445049900_JCS263834C94","doi-asserted-by":"publisher","first-page":"2563","DOI":"10.1091\/mbc.8.12.2563","article-title":"Modulatory roles for integrin activation and the synergy site of fibronectin during matrix assembly","volume":"8","author":"Sechler","year":"1997","journal-title":"Mol. Biol. Cell"},{"key":"2025032504445049900_JCS263834C95","doi-asserted-by":"publisher","first-page":"1081","DOI":"10.1083\/jcb.200102034","article-title":"A novel fibronectin binding site required for fibronectin fibril growth during matrix assembly","volume":"154","author":"Sechler","year":"2001","journal-title":"J. Cell Biol."},{"key":"2025032504445049900_JCS263834C96","doi-asserted-by":"publisher","first-page":"14359","DOI":"10.1016\/S0021-9258(17)43869-5","article-title":"Binding of fibronectin and its proteolytic fragments to glycosaminoglycans. Exposure of cryptic glycosaminoglycan-binding domains upon limited proteolysis","volume":"258","author":"Sekiguchi","year":"1983","journal-title":"J. Biol. Chem."},{"key":"2025032504445049900_JCS263834C97","doi-asserted-by":"publisher","first-page":"4936","DOI":"10.1021\/bi00365a032","article-title":"Human liver fibronectin complementary DNAs: identification of two different messenger RNAs possibly encoding the alpha and beta subunits of plasma fibronectin","volume":"25","author":"Sekiguchi","year":"1986","journal-title":"Biochemistry"},{"key":"2025032504445049900_JCS263834C98","doi-asserted-by":"publisher","first-page":"4039","DOI":"10.1242\/jcs.087858","article-title":"MT1-MMP regulates the turnover and endocytosis of extracellular matrix fibronectin","volume":"124","author":"Shi","year":"2011","journal-title":"J. Cell Sci."},{"key":"2025032504445049900_JCS263834C99","doi-asserted-by":"publisher","first-page":"675","DOI":"10.1016\/0092-8674(79)90040-0","article-title":"The fibronexus: a transmembrane association of fibronectin-containing fibers and bundles of 5 nm microfilaments in hamster and human fibroblasts","volume":"16","author":"Singer","year":"1979","journal-title":"Cell"},{"key":"2025032504445049900_JCS263834C100","doi-asserted-by":"publisher","first-page":"397","DOI":"10.1146\/annurev-cellbio-100109-104020","article-title":"Assembly of fibronectin extracellular matrix","volume":"26","author":"Singh","year":"2010","journal-title":"Annu. Rev. Cell Dev. Biol."},{"key":"2025032504445049900_JCS263834C101","doi-asserted-by":"publisher","first-page":"441","DOI":"10.1111\/j.1432-1033.1986.tb10464.x","article-title":"Complete primary structure of bovine plasma fibronectin","volume":"161","author":"Skorstengaard","year":"1986","journal-title":"Eur. J. Biochem."},{"key":"2025032504445049900_JCS263834C102","doi-asserted-by":"publisher","first-page":"3546","DOI":"10.1091\/mbc.e02-01-0048","article-title":"Fibronectin polymerization regulates the composition and stability of extracellular matrix fibrils and cell-matrix adhesions","volume":"13","author":"Sottile","year":"2002","journal-title":"Mol. Biol. Cell"},{"key":"2025032504445049900_JCS263834C103","doi-asserted-by":"publisher","first-page":"12840","DOI":"10.1016\/S0021-9258(18)98769-7","article-title":"Five type I modules of fibronectin form a functional unit that binds to fibroblasts and Staphylococcus aureus","volume":"266","author":"Sottile","year":"1991","journal-title":"J. Biol. Chem."},{"key":"2025032504445049900_JCS263834C104","doi-asserted-by":"publisher","first-page":"25","DOI":"10.1038\/s41556-018-0234-9","article-title":"Integrin activation by talin, kindlin and mechanical forces","volume":"21","author":"Sun","year":"2019","journal-title":"Nat. Cell Biol."},{"key":"2025032504445049900_JCS263834C105","doi-asserted-by":"publisher","first-page":"23430","DOI":"10.1074\/jbc.M103467200","article-title":"A 49-residue peptide from adhesin F1 of Streptococcus pyogenes inhibits fibronectin matrix assembly","volume":"276","author":"Tomasini-Johansson","year":"2001","journal-title":"J. Biol. Chem."},{"key":"2025032504445049900_JCS263834C106","doi-asserted-by":"publisher","first-page":"jcs260120","DOI":"10.1242\/jcs.260120","article-title":"A new mechanism of fibronectin fibril assembly revealed by live imaging and super-resolution microscopy","volume":"135","author":"Tomer","year":"2022","journal-title":"J. Cell Sci."},{"key":"2025032504445049900_JCS263834C107","doi-asserted-by":"publisher","first-page":"4587","DOI":"10.1242\/jcs.114.24.4587","article-title":"Fibulin-1 suppression of fibronectin-regulated cell adhesion and motility","volume":"114","author":"Twal","year":"2001","journal-title":"J. Cell Sci."},{"key":"2025032504445049900_JCS263834C108","doi-asserted-by":"publisher","first-page":"2575","DOI":"10.1038\/sj.emboj.7601694","article-title":"Interdomain association in fibronectin: insight into cryptic sites and fibrillogenesis","volume":"26","author":"Vakonakis","year":"2007","journal-title":"EMBO J."},{"key":"2025032504445049900_JCS263834C109","doi-asserted-by":"publisher","first-page":"655","DOI":"10.3390\/cells9030655","article-title":"Stimulation of fibronectin matrix assembly by lysine acetylation","volume":"9","author":"Vega","year":"2020","journal-title":"Cells"},{"key":"2025032504445049900_JCS263834C110","doi-asserted-by":"publisher","first-page":"37377","DOI":"10.1074\/jbc.M206286200","article-title":"Polymerization of type I and III collagens is dependent on fibronectin and enhanced by integrins alpha 11beta 1 and alpha 2beta 1","volume":"277","author":"Velling","year":"2002","journal-title":"J. Biol. Chem."},{"key":"2025032504445049900_JCS263834C111","doi-asserted-by":"publisher","first-page":"a005124","DOI":"10.1101\/cshperspect.a005124","article-title":"Cell-extracellular matrix interactions in normal and diseased skin","volume":"3","author":"Watt","year":"2011","journal-title":"Cold Spring Harb. Perspect. Biol."},{"key":"2025032504445049900_JCS263834C112","doi-asserted-by":"publisher","first-page":"45","DOI":"10.1016\/j.biocel.2014.09.023","article-title":"The NTR domain of procollagen C-proteinase enhancer-1 (PCPE-1) mediates PCPE-1 binding to syndecans-1, -2 and -4 as well as fibronectin","volume":"57","author":"Weiss","year":"2014","journal-title":"Int. J. Biochem. Cell Biol."},{"key":"2025032504445049900_JCS263834C113","doi-asserted-by":"publisher","first-page":"227","DOI":"10.1083\/jcb.132.1.227","article-title":"\u03b21 integrin-dependent and -independent polymerization of fibronectin","volume":"132","author":"Wennerberg","year":"1996","journal-title":"J. Cell Biol."},{"key":"2025032504445049900_JCS263834C114","doi-asserted-by":"publisher","first-page":"750","DOI":"10.1002\/jcp.20886","article-title":"Continuous requirement for pp60-Src and phospho-paxillin during fibronectin matrix assembly by transformed cells","volume":"210","author":"Wierzbicka-Patynowski","year":"2007","journal-title":"J. Cell. Physiol."},{"key":"2025032504445049900_JCS263834C115","doi-asserted-by":"publisher","first-page":"32970","DOI":"10.1074\/jbc.M201283200","article-title":"Syndecan-4 modulates focal adhesion kinase phosphorylation","volume":"277","author":"Wilcox-Adelman","year":"2002","journal-title":"J. Biol. Chem."},{"key":"2025032504445049900_JCS263834C116","doi-asserted-by":"publisher","first-page":"665","DOI":"10.1002\/j.1460-2075.1986.tb04265.x","article-title":"Adhesion and cytoskeletal organisation of fibroblasts in response to fibronectin fragments","volume":"5","author":"Woods","year":"1986","journal-title":"EMBO J."},{"key":"2025032504445049900_JCS263834C117","doi-asserted-by":"publisher","first-page":"272","DOI":"10.1016\/0014-4827(88)90461-2","article-title":"Fibronectin fibril formation involves cell interactions with two fibronectin domains","volume":"177","author":"Woods","year":"1988","journal-title":"Exp. Cell Res."},{"key":"2025032504445049900_JCS263834C118","doi-asserted-by":"publisher","first-page":"1737","DOI":"10.1091\/mbc.7.11.1737","article-title":"Fibronectin receptor functions in embryonic cells deficient in \u03b15\u03b21 integrin can be replaced by \u03b1v integrins","volume":"7","author":"Yang","year":"1996","journal-title":"Mol. Biol. Cell"},{"key":"2025032504445049900_JCS263834C119","doi-asserted-by":"publisher","first-page":"617","DOI":"10.1038\/s41580-024-00716-0","article-title":"Fibroblast and myofibroblast activation in normal tissue repair and fibrosis","volume":"25","author":"Younesi","year":"2024","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"2025032504445049900_JCS263834C120","doi-asserted-by":"publisher","first-page":"a004911","DOI":"10.1101\/cshperspect.a004911","article-title":"Basement membranes: cell scaffoldings and signaling platforms","volume":"3","author":"Yurchenco","year":"2011","journal-title":"Cold Spring Harb. Perspect. Biol."},{"key":"2025032504445049900_JCS263834C121","doi-asserted-by":"publisher","first-page":"191","DOI":"10.1038\/35008607","article-title":"Dynamics and segregation of cell-matrix adhesions in cultured fibroblasts","volume":"2","author":"Zamir","year":"2000","journal-title":"Nat. Cell Biol."},{"key":"2025032504445049900_JCS263834C122","doi-asserted-by":"publisher","first-page":"1415","DOI":"10.1091\/mbc.8.8.1415","article-title":"Lysophosphatidic acid and microtubule-destabilizing agents stimulate fibronectin matrix assembly through Rho-dependent actin stress fiber formation and cell contraction","volume":"8","author":"Zhang","year":"1997","journal-title":"Mol. Biol. Cell"},{"key":"2025032504445049900_JCS263834C123","doi-asserted-by":"publisher","first-page":"330","DOI":"10.1016\/j.matbio.2006.12.004","article-title":"Quantification of fibronectin matrix assembly sites using a novel ELISA assay","volume":"26","author":"Zheng","year":"2007","journal-title":"Matrix Biol."},{"key":"2025032504445049900_JCS263834C124","doi-asserted-by":"publisher","first-page":"539","DOI":"10.1083\/jcb.141.2.539","article-title":"Rho-mediated contractility exposes a cryptic site in fibronectin and induces fibronectin matrix assembly","volume":"141","author":"Zhong","year":"1998","journal-title":"J. Cell Biol."}],"container-title":["Journal of Cell Science"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/journals.biologists.com\/jcs\/article-pdf\/doi\/10.1242\/jcs.263834\/3640657\/jcs263834.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/journals.biologists.com\/jcs\/article-pdf\/doi\/10.1242\/jcs.263834\/3640657\/jcs263834.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,3,25]],"date-time":"2025-03-25T08:47:13Z","timestamp":1742892433000},"score":1,"resource":{"primary":{"URL":"https:\/\/journals.biologists.com\/jcs\/article\/138\/6\/jcs263834\/367491\/Fibronectin-matrix-assembly-at-a-glance"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2025,3,15]]},"references-count":124,"journal-issue":{"issue":"6","published-print":{"date-parts":[[2025,3,15]]}},"URL":"https:\/\/doi.org\/10.1242\/jcs.263834","relation":{},"ISSN":["0021-9533","1477-9137"],"issn-type":[{"value":"0021-9533","type":"print"},{"value":"1477-9137","type":"electronic"}],"subject":[],"published":{"date-parts":[[2025,3,15]]},"article-number":"jcs263834"}}