{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,16]],"date-time":"2026-10-16T09:57:59Z","timestamp":1792144679567,"version":"4.4.0"},"reference-count":45,"publisher":"eLife Sciences Publications, Ltd","license":[{"start":{"date-parts":[[2023,2,1]],"date-time":"2023-02-01T00:00:00Z","timestamp":1675209600000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"},{"start":{"date-parts":[[2023,2,1]],"date-time":"2023-02-01T00:00:00Z","timestamp":1675209600000},"content-version":"am","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"},{"start":{"date-parts":[[2023,2,1]],"date-time":"2023-02-01T00:00:00Z","timestamp":1675209600000},"content-version":"tdm","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"name":"Paul D. Wellstone Muscular Dystrophy Specialized Research Center","award":["1U54NS053672"],"award-info":[{"award-number":["1U54NS053672"]}]},{"DOI":"10.13039\/100000011","name":"Howard Hughes Medical Institute","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100000011","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001700","name":"Ministry of Education, Culture, Sports, Science and Technology","doi-asserted-by":"publisher","award":["19K07981"],"award-info":[{"award-number":["19K07981"]}],"id":[{"id":"10.13039\/501100001700","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elifesciences.org"],"crossmark-restriction":false},"short-container-title":[],"accepted":{"date-parts":[[2023,1,31]]},"abstract":"<jats:p>\n                    Dystroglycan (DG) requires extensive post-translational processing and\n                    <jats:italic>O<\/jats:italic>\n                    -glycosylation to function as a receptor for extracellular matrix (ECM) proteins containing laminin-G (LG) domains. Matriglycan is an elongated polysaccharide of alternating xylose (Xyl) and glucuronic acid (GlcA) that binds with high affinity to ECM proteins with LG domains and is uniquely synthesized on \u03b1-dystroglycan (\u03b1-DG) by like-acetylglucosaminyltransferase-1 (LARGE1). Defects in the post-translational processing or\n                    <jats:italic>O<\/jats:italic>\n                    -glycosylation of \u03b1-DG that result in a shorter form of matriglycan reduce the size of \u03b1-DG and decrease laminin binding, leading to various forms of muscular dystrophy. Previously, we demonstrated that protein\n                    <jats:italic>O<\/jats:italic>\n                    -mannose kinase (POMK) is required for LARGE1 to generate full-length matriglycan on \u03b1-DG (~150\u2013250 kDa) (Walimbe et al., 2020). Here, we show that LARGE1 can only synthesize a short, non-elongated form of matriglycan in mouse skeletal muscle that lacks the DG N-terminus (\u03b1-DGN), resulting in an ~100\u2013125 kDa \u03b1-DG. This smaller form of \u03b1-DG binds laminin and maintains specific force but does not prevent muscle pathophysiology, including reduced force production after eccentric contractions (ECs) or abnormalities in the neuromuscular junctions. Collectively, our study demonstrates that \u03b1-DGN, like POMK, is required for LARGE1 to extend matriglycan to its full mature length on \u03b1-DG and thus prevent muscle pathophysiology.\n                  <\/jats:p>","DOI":"10.7554\/elife.82811","type":"journal-article","created":{"date-parts":[[2023,2,1]],"date-time":"2023-02-01T09:53:12Z","timestamp":1675245192000},"update-policy":"https:\/\/doi.org\/10.7554\/elife.82811","source":"Crossref","is-referenced-by-count":22,"title":["N-terminal domain on dystroglycan enables LARGE1 to extend matriglycan on \u03b1-dystroglycan and prevents muscular dystrophy"],"prefix":"10.7554","volume":"12","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-2749-9855","authenticated-orcid":true,"given":"Hidehiko","family":"Okuma","sequence":"first","affiliation":[{"id":[{"id":"https:\/\/ror.org\/036jqmy94","id-type":"ROR","asserted-by":"publisher"}],"name":"Howard Hughes Medical Institute, Senator Paul D. 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