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In the case of patients carrying defects in fukutin-related protein (FKRP), these diverse pathologies arise from mutations within the same gene. This is surprising as FKRP is a glycosyltransferase, whose only identified function is to transfer ribitol-5-phosphate to \u03b1-dystroglycan (\u03b1-DG). Although this modification is critical for extracellular matrix attachment, \u03b1-DG\u2019s glycosylation status relates poorly to disease severity, suggesting the existence of unidentified FKRP targets. Here we reveal that FKRP directs sialylation of fibronectin, a process essential for collagen recruitment to the muscle basement membrane. Thus, our results reveal that FKRP simultaneously regulates the two major muscle-ECM linkages essential for fibre survival, and establishes a new disease axis for the muscular dystrophies.<\/jats:p>","DOI":"10.1038\/s41467-021-23217-6","type":"journal-article","created":{"date-parts":[[2021,5,19]],"date-time":"2021-05-19T10:03:08Z","timestamp":1621418588000},"update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":28,"title":["FKRP-dependent glycosylation of fibronectin regulates muscle pathology in muscular dystrophy"],"prefix":"10.1038","volume":"12","author":[{"given":"A. J.","family":"Wood","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-1911-0034","authenticated-orcid":false,"given":"C. 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