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• W2504491446 abstract "Significance Congenital muscular dystrophy (CMD) is caused by hypoglycosylation of α-dystroglycan (α-DG). In some CMD patients, mutations in the gene encoding protein O -linked mannose β1,2- N -acetylglucosaminyltransferase 1, POMGnT1 , are responsible for such hypoglycosylation. Many CMD-related genes are thought to be involved in the glycosylation of core M3, a specific O -mannose–type structure in α-DG. Although POMGnT1 has long been known to be associated with CMD, its role in the glycosylation of core M3 remains unclear. Our results reveal that the stem domain of POMGnT1 modulates O -mannosylation of α-DG via its carbohydrate-binding activity. These findings explain how POMGnT1 attaches β-GlcNAc to clustered O -mannose sites and influences postphosphoryl modification of core M3. Our study provides important insight into how disease-associated mutations cause CMD pathogenesis." @default.
• W2504491446 created "2016-08-23" @default.
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• W2504491446 date "2016-08-04" @default.
• W2504491446 modified "2023-10-16" @default.
• W2504491446 title "Carbohydrate-binding domain of the POMGnT1 stem region modulates <i>O</i> -mannosylation sites of α-dystroglycan" @default.
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• W2504491446 doi "https://doi.org/10.1073/pnas.1525545113" @default.
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