{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,29]],"date-time":"2026-09-29T09:54:52Z","timestamp":1790675692481,"version":"4.1.0"},"reference-count":78,"publisher":"Wiley","license":[{"start":{"date-parts":[[2026,9,29]],"date-time":"2026-09-29T00:00:00Z","timestamp":1790640000000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"},{"start":{"date-parts":[[2026,9,29]],"date-time":"2026-09-29T00:00:00Z","timestamp":1790640000000},"content-version":"tdm","delay-in-days":0,"URL":"http:\/\/doi.wiley.com\/10.1002\/tdm_license_1.1"}],"funder":[{"DOI":"10.13039\/501100001659","name":"Deutsche Forschungsgemeinschaft","doi-asserted-by":"publisher","award":["384170921"],"award-info":[{"award-number":["384170921"]}],"id":[{"id":"10.13039\/501100001659","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001659","name":"Deutsche Forschungsgemeinschaft","doi-asserted-by":"publisher","award":["397484323"],"award-info":[{"award-number":["397484323"]}],"id":[{"id":"10.13039\/501100001659","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001659","name":"Deutsche Forschungsgemeinschaft","doi-asserted-by":"publisher","award":["468236352"],"award-info":[{"award-number":["468236352"]}],"id":[{"id":"10.13039\/501100001659","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001659","name":"Deutsche Forschungsgemeinschaft","doi-asserted-by":"publisher","award":["501530074"],"award-info":[{"award-number":["501530074"]}],"id":[{"id":"10.13039\/501100001659","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001659","name":"Deutsche Forschungsgemeinschaft","doi-asserted-by":"publisher","award":["INST 216\/1174\u20101 FUGG"],"award-info":[{"award-number":["INST 216\/1174\u20101 FUGG"]}],"id":[{"id":"10.13039\/501100001659","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001659","name":"Deutsche Forschungsgemeinschaft","doi-asserted-by":"publisher","award":["INST 216\/1397\u20101 FUGG"],"award-info":[{"award-number":["INST 216\/1397\u20101 FUGG"]}],"id":[{"id":"10.13039\/501100001659","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["febs.onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["The FEBS Journal"],"abstract":"<jats:p>Sclerostin (SOST) is a secreted glycoprotein that antagonizes Wnt and BMP signaling, however, the molecular mechanisms regulating its extracellular distribution and growth factor (GF) interactions remain poorly understood. Here, we identify fibrillin microfibrils as high\u2010affinity extracellular binding partners of SOST. Recombinant SOST bound specifically to fibrillin\u20101 positive fibers in cell culture and localized near the bead region of purified tissue fibrillin microfibrils. Surface plasmon resonance (SPR) mapping revealed that SOST recognizes the N\u2010terminal regions of fibrillin\u20101 and fibrillin\u20102 with nanomolar affinity, and deletion analysis identified the fibrillin\u2010unique N\u2010terminal (FUN) domain as the primary SOST binding site. Our findings further extend the SOST binding repertoire to include BMP\u201010 GF, as well as the prodomains (PDs) and PD\u2010GF complexes (CPLXs) of BMP\u20107 and BMP\u201010. Heparin interfered with SOST binding to BMP\u20107 PDs and CPLXs but not with the SOST\u2010fibrillin\u20101 interaction. SPR interaction experiments showed that SOST binding to fibrillin\u20101 occludes the BMP PD targeting site and that fibrillin\u20101\u2010bound SOST is unable to engage BMP\u20107 PDs. Molecular docking further supported this competitive mechanism by revealing overlapping interaction interfaces among SOST, BMP\u20107 CPLX, and fibrillin\u20101. Together, these findings establish SOST as a multifunctional ECM\u2010associated BMP modulator that links fibrillin microfibril scaffolds to the fine\u2010tuning of BMP and Wnt signaling.<\/jats:p>","DOI":"10.1111\/febs.70745","type":"journal-article","created":{"date-parts":[[2026,9,29]],"date-time":"2026-09-29T08:55:34Z","timestamp":1790672134000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["Sclerostin regulates bone morphogenetic protein (\n                    <scp>BMP<\/scp>\n                    ) bioavailability through interactions with\n                    <scp>BMP<\/scp>\n                    complexes and fibrillin microfibrils"],"prefix":"10.1111","author":[{"given":"Annkatrin","family":"Correns","sequence":"first","affiliation":[{"name":"Department of Pediatrics and Adolescent Medicine, Faculty of Medicine and University Hospital Cologne University of Cologne  Germany"},{"name":"Center for Biochemistry, Faculty of Medicine University Hospital of Cologne  Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Fady","family":"Marcous","sequence":"additional","affiliation":[{"name":"Department of Pediatrics and Adolescent Medicine, Faculty of Medicine and University Hospital Cologne University of Cologne  Germany"},{"name":"Center for Biochemistry, Faculty of Medicine University Hospital of Cologne  Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Steffen","family":"L\u00fctke","sequence":"additional","affiliation":[{"name":"Department of Pediatrics and Adolescent Medicine, Faculty of Medicine and University Hospital Cologne University of Cologne  Germany"},{"name":"Center for Biochemistry, Faculty of Medicine University Hospital of Cologne  Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Matthias","family":"M\u00f6rgelin","sequence":"additional","affiliation":[{"name":"Division of Infection Medicine, Department of Clinical Sciences Lund University  Sweden"},{"name":"Colzyx AB  Lund Sweden"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0009-0008-2843-7577","authenticated-orcid":false,"given":"Philipp","family":"Barnowski","sequence":"additional","affiliation":[{"name":"Department of Pediatrics and Adolescent Medicine, Faculty of Medicine and University Hospital Cologne University of Cologne  Germany"},{"name":"Center for Biochemistry, Faculty of Medicine University Hospital of Cologne  Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ariane G.","family":"Furlan","sequence":"additional","affiliation":[{"name":"Department of Pediatrics and Adolescent Medicine, Faculty of Medicine and University Hospital Cologne University of Cologne  Germany"},{"name":"Center for Biochemistry, Faculty of Medicine University Hospital of Cologne  Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Nathalie H.","family":"Schr\u00f6der","sequence":"additional","affiliation":[{"name":"Institute of Molecular Medicine III University Hospital Duesseldorf, Heinrich Heine University Duesseldorf  Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Bodo","family":"Levkau","sequence":"additional","affiliation":[{"name":"Institute of Molecular Medicine III University Hospital Duesseldorf, Heinrich Heine University Duesseldorf  Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sarah","family":"Riek","sequence":"additional","affiliation":[{"name":"Medical Faculty Bonn, Institute of Physiology I University of Bonn  Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Martin","family":"Mollenhauer","sequence":"additional","affiliation":[{"name":"Heart Center, Department of Cardiology, Faculty of Medicine and University Hospital Cologne University of Cologne  Germany"},{"name":"Center for Molecular Medicine Cologne (CMMC) University of Cologne  Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Manuel","family":"Koch","sequence":"additional","affiliation":[{"name":"Center for Biochemistry, Faculty of Medicine University Hospital of Cologne  Germany"},{"name":"Institute for Dental Research and Oral Musculoskeletal Biology, Faculty of Medicine and University Hospital Cologne University of Cologne  Germany"},{"name":"Center for Dental, Oral and Maxillofacial Medicine (Central Facilities) University Hospital Cologne  Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-3932-1242","authenticated-orcid":false,"given":"Gerhard","family":"Sengle","sequence":"additional","affiliation":[{"name":"Department of Pediatrics and Adolescent Medicine, Faculty of Medicine and University Hospital Cologne University of Cologne  Germany"},{"name":"Center for Biochemistry, Faculty of Medicine University Hospital of Cologne  Germany"},{"name":"Center for Molecular Medicine Cologne (CMMC) University of Cologne  Germany"},{"name":"Cologne Center for Musculoskeletal Biomechanics (CCMB)  Germany"},{"name":"Cologne Excellence Cluster on Cellular Stress Responses in Ageing\u2010Associated Diseases (CECAD) University of Cologne  Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2026,9,29]]},"reference":[{"key":"e_1_2_10_2_1","doi-asserted-by":"crossref","first-page":"1216","DOI":"10.1126\/science.1176009","article-title":"The extracellular matrix: not just pretty fibrils","volume":"326","author":"Hynes RO","year":"2009","journal-title":"Science"},{"key":"e_1_2_10_3_1","doi-asserted-by":"crossref","first-page":"3","DOI":"10.1016\/j.matbio.2015.05.002","article-title":"The fibrillin microfibril scaffold: a niche for growth factors and mechanosensation?","volume":"47","author":"Sengle G","year":"2015","journal-title":"Matrix 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genetic disease, have elevated bone formation markers, higher bone density, and greater derived polar moment of inertia than normal","volume":"88","author":"Wergedal JE","year":"2003","journal-title":"J Clin Endocrinol Metab"},{"key":"e_1_2_10_32_1","doi-asserted-by":"crossref","first-page":"497","DOI":"10.1007\/s00439-011-0947-3","article-title":"Identification of signal peptide domain SOST mutations in autosomal dominant craniodiaphyseal dysplasia","volume":"129","author":"Kim SJ","year":"2011","journal-title":"Hum Genet"},{"key":"e_1_2_10_33_1","doi-asserted-by":"crossref","first-page":"577","DOI":"10.1086\/318811","article-title":"Bone dysplasia sclerosteosis results from loss of the SOST gene product, a novel cystine knot\u2010containing protein","volume":"68","author":"Brunkow ME","year":"2001","journal-title":"Am J Hum Genet"},{"key":"e_1_2_10_34_1","doi-asserted-by":"crossref","first-page":"537","DOI":"10.1093\/hmg\/10.5.537","article-title":"Increased bone density in 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