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We demonstrated that NRP1 was a constituent of adherens junctions that interacted with VE-cadherin and promoted its association with p120 catenin, stabilizing adherens junctions and inducing cytoskeletal remodeling in alignment with the direction of flow. We also showed that NRP1 interacted with transforming growth factor\u2013\u03b2 (TGF-\u03b2) receptor II (TGFBR2) and reduced the plasma membrane localization of TGFBR2 and TGF-\u03b2 signaling. NRP1 knockdown increased the abundance of proinflammatory cytokines and adhesion molecules, resulting in increased leukocyte rolling and atherosclerotic plaque size. These findings describe a role for NRP1 in promoting endothelial function and reveal a mechanism by which NRP1 reduction in ECs may contribute to vascular disease by modulating adherens junction signaling and promoting TGF-\u03b2 signaling and inflammation.<\/jats:p>","DOI":"10.1126\/scisignal.abo4863","type":"journal-article","created":{"date-parts":[[2023,5,23]],"date-time":"2023-05-23T18:05:13Z","timestamp":1684865113000},"update-policy":"https:\/\/doi.org\/10.34133\/aaas_crossmark","source":"Crossref","is-referenced-by-count":30,"title":["Neuropilin-1 interacts with VE-cadherin and TGFBR2 to stabilize adherens junctions and prevent activation of endothelium under flow"],"prefix":"10.1126","volume":"16","author":[{"ORCID":"https:\/\/orcid.org\/0000-0001-5316-0508","authenticated-orcid":true,"given":"Emy","family":"Bosseboeuf","sequence":"first","affiliation":[{"name":"William Harvey Research Institute, Barts and London School of Medicine and Dentistry, Centre of Cardiovascular 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