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The dystroglycan subcomplex interacts with dystrophin and spans the sarcolemma where its extensive carbohydrates (matriglycan and CT2 glycan) directly interact with the extracellular matrix. In the current manuscript, we show that sarcospan overexpression enhances the laminin-binding capacity of dystroglycan in DMD muscle by increasing matriglycan glycosylation of \u03b1-dystroglycan. Furthermore, we find that this modification is not affected by loss of Galgt2, a glycotransferase, which catalyzes the CT2 glycan. Our findings reveal that the matriglycan carbohydrates, and not the CT2 glycan, are necessary for sarcospan-mediated amelioration of DMD. Overexpression of Galgt2 in the DMD mdx murine model prevents muscle pathology by increasing CT2 modified \u03b1-dystroglycan. Galgt2 also increases expression of utrophin, which compensates for the loss of dystrophin in DMD muscle. We found that combined loss of Galgt2 and dystrophin reduced utrophin expression; however, it did not interfere with sarcospan rescue of disease. These data reveal a partial dependence of sarcospan on Galgt2 for utrophin upregulation. In addition, sarcospan alters the cross-talk between the adhesion complexes by decreasing the association of integrin \u03b21D with dystroglycan complexes. In conclusion, sarcospan functions to re-wire the cell to matrix connections by strengthening the cellular adhesion and signaling, which, in turn, increases the resilience of the myofiber membrane.<\/jats:p>","DOI":"10.1093\/hmg\/ddab276","type":"journal-article","created":{"date-parts":[[2021,9,20]],"date-time":"2021-09-20T15:11:45Z","timestamp":1632150705000},"page":"718-732","source":"Crossref","is-referenced-by-count":9,"title":["Sarcospan increases laminin-binding capacity of \u03b1-dystroglycan to ameliorate DMD independent of\n                    <i>Galgt2<\/i>"],"prefix":"10.1093","volume":"31","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-0879-6635","authenticated-orcid":false,"given":"Hafsa","family":"Mamsa","sequence":"first","affiliation":[{"name":"Department of Integrative Biology & Physiology, University of California, Los Angeles 90095, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Rachelle L","family":"Stark","sequence":"additional","affiliation":[{"name":"Department of Integrative Biology & Physiology, University of California, Los Angeles 90095, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kara M","family":"Shin","sequence":"additional","affiliation":[{"name":"Department of Integrative Biology & Physiology, University of California, Los Angeles 90095, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Aaron M","family":"Beedle","sequence":"additional","affiliation":[{"name":"Department of Pharmaceutical Sciences, Binghamton University State University of New York, New York 13902, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Rachelle H","family":"Crosbie","sequence":"additional","affiliation":[{"name":"Department of Integrative Biology & Physiology, University of California, Los Angeles 90095, USA"},{"name":"Broad Stem Cell Institute, University of California, Los Angeles 90095, USA"},{"name":"Department of Neurology, David Geffen School of Medicine, University of California, Los Angeles 90095, USA"},{"name":"Molecular Biology Institute, University of California, Los Angeles 90095, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"286","published-online":{"date-parts":[[2021,9,28]]},"reference":[{"key":"2022030413195329200_ref1","doi-asserted-by":"crossref","first-page":"919","DOI":"10.1016\/0092-8674(87)90579-4","article-title":"Dystrophin: the protein product of the Duchenne muscular dystrophy locus","volume":"51","author":"Hoffman","year":"1987","journal-title":"Cell"},{"key":"2022030413195329200_ref2","doi-asserted-by":"crossref","first-page":"304","DOI":"10.1002\/ana.23528","article-title":"Evidence-based path to newborn screening for Duchenne muscular dystrophy","volume":"71","author":"Mendell","year":"2012","journal-title":"Ann. 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