[HTML][HTML] Absence of post-phosphoryl modification in dystroglycanopathy mouse models and wild-type tissues expressing non-laminin binding form of α-dystroglycan
A Kuga, M Kanagawa, A Sudo, YM Chan… - Journal of Biological …, 2012 - ASBMB
α-Dystroglycan (α-DG) is a membrane-associated glycoprotein that interacts with several
extracellular matrix proteins, including laminin and agrin. Aberrant glycosylation of α-DG
disrupts its interaction with ligands and causes a certain type of muscular dystrophy
commonly referred to as dystroglycanopathy. It has been reported that a unique O-mannosyl
tetrasaccharide (Neu5Ac-α2, 3-Gal-β1, 4-GlcNAc-β1, 2-Man) and a phosphodiester-linked
modification on O-mannose play important roles in the laminin binding activity of α-DG. In …
extracellular matrix proteins, including laminin and agrin. Aberrant glycosylation of α-DG
disrupts its interaction with ligands and causes a certain type of muscular dystrophy
commonly referred to as dystroglycanopathy. It has been reported that a unique O-mannosyl
tetrasaccharide (Neu5Ac-α2, 3-Gal-β1, 4-GlcNAc-β1, 2-Man) and a phosphodiester-linked
modification on O-mannose play important roles in the laminin binding activity of α-DG. In …