Publications by authors named "Megan Devereaux"
Alpha-dystroglycan (αDG) is a highly glycosylated cell surface protein with a significant role in cell-to-extracellular matrix interactions in muscle. αDG interaction with extracellular ligands relies on the activity of the LARGE1 glycosyltransferase that synthesizes and extends the heteropolysaccharide matriglycan. Abnormalities in αDG glycosylation and formation of matriglycan are the pathogenic mechanisms for the dystroglycanopathies, a group of congenital muscular dystrophies.
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- Matriglycan acts as a structural support for extracellular matrix proteins, particularly in skeletal muscle, where it is synthesized and extended by LIKE-acetyl-glucosaminyltransferase 1 (LARGE1).
- Protein-Mannose Kinase (POMK) is essential for the phosphorylation of mannose on the core M3 structure, which is crucial for the production of full-length matriglycan on α-dystroglycan (α-DG).
- Without POMK, matriglycan synthesis is limited to a shorter form, resulting in impaired muscle function and increased risk of muscular dystrophy.