{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,26]],"date-time":"2026-09-26T10:17:23Z","timestamp":1790417843556,"version":"4.1.0"},"reference-count":127,"publisher":"Portland Press Ltd.","issue":"7","content-domain":{"domain":["portlandpress.com"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[2016,4,1]]},"abstract":"<jats:p>The 10\u201312\u00a0nm diameter microfibrils of the extracellular matrix (ECM) impart both structural and regulatory properties to load-bearing connective tissues. The main protein component is the calcium-dependent glycoprotein fibrillin, which assembles into microfibrils at the cell surface in a highly regulated process involving specific proteolysis, multimerization and glycosaminoglycan interactions. In higher metazoans, microfibrils act as a framework for elastin deposition and modification, resulting in the formation of elastic fibres, but they can also occur in elastin-free tissues where they perform structural roles. Fibrillin microfibrils are further engaged in a number of cell matrix interactions such as with integrins, bone morphogenetic proteins (BMPs) and the large latent complex of transforming growth factor-\u03b2 (TGF\u03b2). Fibrillin-1 (FBN1) mutations are associated with a range of heritable connective disorders, including Marfan syndrome (MFS) and the acromelic dysplasias, suggesting that the roles of 10\u201312\u00a0nm diameter microfibrils are pleiotropic. In recent years the use of molecular, cellular and whole-organism studies has revealed that the microfibril is not just a structural component of the ECM, but through its network of cell and matrix interactions it can exert profound regulatory effects on cell function. In this review we assess what is known about the molecular properties of fibrillin that enable it to assemble into the 10\u201312\u00a0nm diameter microfibril and perform such diverse roles.<\/jats:p>","DOI":"10.1042\/bj20151108","type":"journal-article","created":{"date-parts":[[2016,3,29]],"date-time":"2016-03-29T09:09:05Z","timestamp":1459242545000},"page":"827-838","update-policy":"https:\/\/doi.org\/10.1042\/crossmark_policy","source":"Crossref","is-referenced-by-count":53,"title":["New insights into the structure, assembly and biological roles of 10\u201312 nm connective tissue microfibrils from fibrillin-1 studies"],"prefix":"10.1042","volume":"473","author":[{"given":"Sacha A.","family":"Jensen","sequence":"first","affiliation":[{"name":"Department of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, U.K."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Penny A.","family":"Handford","sequence":"additional","affiliation":[{"name":"Department of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, U.K."}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"288","published-online":{"date-parts":[[2016,3,29]]},"reference":[{"key":"2021112216353415500_B1","doi-asserted-by":"publisher","first-page":"2499","DOI":"10.1083\/jcb.103.6.2499","article-title":"Fibrillin, a new 350-kD glycoprotein, is a component of extracellular microfibrils","volume":"103","author":"Sakai","year":"1986","journal-title":"J. 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