{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"institution":[{"name":"bioRxiv"}],"indexed":{"date-parts":[[2026,9,28]],"date-time":"2026-09-28T16:17:28Z","timestamp":1790612248667,"version":"4.1.0"},"posted":{"date-parts":[[2026,3,17]]},"group-title":"Cell Biology","reference-count":45,"publisher":"openRxiv","license":[{"start":{"date-parts":[[2026,3,17]],"date-time":"2026-03-17T00:00:00Z","timestamp":1773705600000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by-nc-nd\/4.0\/"}],"funder":[{"DOI":"10.13039\/100000057","name":"National Institute of General Medical Sciences","doi-asserted-by":"crossref","award":["R01GM148423"],"award-info":[{"award-number":["R01GM148423"]}],"id":[{"id":"10.13039\/100000057","id-type":"DOI","asserted-by":"crossref"}]},{"DOI":"10.13039\/100000050","name":"National Heart Lung and Blood Institute","doi-asserted-by":"crossref","award":["HL144459"],"award-info":[{"award-number":["HL144459"]}],"id":[{"id":"10.13039\/100000050","id-type":"DOI","asserted-by":"crossref"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"accepted":{"date-parts":[[2026,3,17]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n                <jats:p>\n                  The extracellular matrix (ECM) is a complex scaffold of proteins that supports multicellular structures. Interactions between cells and the ECM via receptors, like integrins, govern cellular phenotypes (\n                  <jats:italic>e.g.<\/jats:italic>\n                  , proliferation, adhesion), but also contribute to ECM assembly. Understanding how ECM-receptor interactions regulate matrix assembly is critical to uncover how alterations of the ECM cause or accompany congenital diseases, cancer, or fibrosis.\n                <\/jats:p>\n                <jats:p>SNED1 is a novel ECM protein with roles in development and metastasis. However, the mechanisms governing its assembly and signaling functions remain largely unknown. SNED1 contains two integrin-binding motifs, RGD and LDV, and we recently showed that its interaction with RGD-integrins mediates cell adhesion. Here, we investigated the role of SNED1\/integrin interactions in SNED1 ECM assembly. While SNED1\/integrin interactions were not necessary for its initial incorporation in the ECM, interaction with LDV-, but not RGD-, integrins, was required for ECM build-up and the patterning of SNED1 and the fibrillar proteins fibronectin and collagen I. Moreover, SNED1\/LDV-integrin interaction promoted ECM alignment, cell alignment, and cell proliferation, processes essential to SNED1-driven neural crest cell migration during craniofacial development and breast cancer invasion.<\/jats:p>\n                <jats:sec>\n                  <jats:title>SUMMARY STATEMENT<\/jats:title>\n                  <jats:p>Interaction of SNED1 with LDV-binding integrins, but not RGD-binding integrins, mediates ECM remodeling and controls cytoskeletal rearrangement and cell proliferation.<\/jats:p>\n                <\/jats:sec>","DOI":"10.64898\/2026.03.16.712162","type":"posted-content","created":{"date-parts":[[2026,3,17]],"date-time":"2026-03-17T13:35:14Z","timestamp":1773754514000},"source":"Crossref","is-referenced-by-count":1,"title":["SNED1 modulates ECM architecture and cell proliferation via LDV-binding integrins"],"prefix":"10.64898","author":[{"given":"Dharma","family":"Pally","sequence":"first","affiliation":[{"name":"Department of Physiology and Biophysics, University of Illinois Chicago, Chicago, IL, 60612, U.S.A"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Leanna","family":"Leverton","sequence":"additional","affiliation":[{"name":"Department of Physiology and Biophysics, University of Illinois Chicago, Chicago, IL, 60612, U.S.A"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Asantewaa","family":"Jones","sequence":"additional","affiliation":[{"name":"Department of Physiology and Biophysics, University of Illinois Chicago, Chicago, IL, 60612, U.S.A"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-4796-5614","authenticated-orcid":false,"given":"Alexandra","family":"Naba","sequence":"additional","affiliation":[{"name":"Department of Physiology and Biophysics, University of Illinois Chicago, Chicago, IL, 60612, U.S.A"},{"name":"University of Illinois Cancer Center, Chicago, IL 60612, U.S.A"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"54368","reference":[{"key":"2026031908001160000_2026.03.16.712162v1.1","doi-asserted-by":"publisher","DOI":"10.1002\/dvdy.258"},{"key":"2026031908001160000_2026.03.16.712162v1.2","doi-asserted-by":"publisher","DOI":"10.1038\/nrm3904"},{"key":"2026031908001160000_2026.03.16.712162v1.3","doi-asserted-by":"crossref","unstructured":"Campbell, I. D. and Humphries, M. J . (2011). Integrin structure, activation, and interactions. 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