Dystroglycan function requires xylosyl-and glucuronyltransferase activities of LARGE
K Inamori, T Yoshida-Moriguchi, Y Hara, ME Anderson… - Science, 2012 - science.org
Science, 2012•science.org
Posttranslational modification of alpha-dystroglycan (α-DG) by the like-
acetylglucosaminyltransferase (LARGE) is required for it to function as an extracellular
matrix (ECM) receptor. Mutations in the LARGE gene have been identified in congenital
muscular dystrophy patients with brain abnormalities. However, the precise function of
LARGE remains unclear. Here we found that LARGE could act as a bifunctional
glycosyltransferase, with both xylosyltransferase and glucuronyltransferase activities, which …
acetylglucosaminyltransferase (LARGE) is required for it to function as an extracellular
matrix (ECM) receptor. Mutations in the LARGE gene have been identified in congenital
muscular dystrophy patients with brain abnormalities. However, the precise function of
LARGE remains unclear. Here we found that LARGE could act as a bifunctional
glycosyltransferase, with both xylosyltransferase and glucuronyltransferase activities, which …
Posttranslational modification of alpha-dystroglycan (α-DG) by the like-acetylglucosaminyltransferase (LARGE) is required for it to function as an extracellular matrix (ECM) receptor. Mutations in the LARGE gene have been identified in congenital muscular dystrophy patients with brain abnormalities. However, the precise function of LARGE remains unclear. Here we found that LARGE could act as a bifunctional glycosyltransferase, with both xylosyltransferase and glucuronyltransferase activities, which produced repeating units of [–3-xylose–α1,3-glucuronic acid-β1–]. This modification allowed α-DG to bind laminin-G domain–containing ECM ligands.
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